Information on EC 3.2.1.11 - dextranase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
3.2.1.11
-
RECOMMENDED NAME
GeneOntology No.
dextranase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Endohydrolysis of (1->6)-alpha-D-glucosidic linkages in dextran
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
hydrolysis of O-glycosyl bond
-
-
hydrolysis of O-glycosyl bond
-
-
-
SYSTEMATIC NAME
IUBMB Comments
6-alpha-D-glucan 6-glucanohydrolase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1,6-alpha-D-glucan-6-glucanohydrolase
-
-
Alpha-1,6-glucan-6-glucanohydrolase
-
-
-
-
alpha-D-1,6-glucan-6-glucanohydrolase
-
-
-
-
alpha-dextranase
-
-
AODex
A9UKG4
-
AODex
Arthrobacter oxydans DSM20119T
A9UKG4
-
-
DexA
Streptococcus mutans ATCC 700610
Q54443
-
-
dextran hydrolase
-
-
-
-
dextranase
-
-
dextranase
-
-
dextranase
Lipomyces starkeyi KSM22
-
-
-
dextranase
-
-
dextranase
Penicillium sp. NRRL 21969
-
-
-
dextranase DL 2
-
-
-
-
dextransucrase
-
-
DL 2
-
-
-
-
DXSR
A9UKG4
fusion protein of endo-dextranase and dextransucrase
endo-dextranase
-
-
-
-
endo-dextranase
A9UKG4
-
endo-dextranase
Chaetomium erraticum
-
-
endo-dextranase
F5BA50
-
endo-dextranase
F5BA50
-
-
endo-dextranase
-
-
endodextranase
-
-
-
-
extracellular dextranase
-
-
rDex
-
recombinant dextranase
SmDex
F5BA50
-
TLDex
A8F6K5
recombinant protein
TLDex
A8F6K5
recombinant protein
-
TPDex
Thermoanaerobacter pseudethanolicus ATCC 33223 39E
-
-
-
LSD1
Lipomyces starkeyi KSM22
-
-
-
additional information
F5BA50
the enzyme belongs to the glycoside hydrolase family (GH) 66
additional information
F5BA50
the enzyme belongs to the glycoside hydrolase family (GH) 66
-
CAS REGISTRY NUMBER
COMMENTARY
9025-70-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
aerobic bacterium SRI 2125
commentary isolated from the hot environs of a raw sugar factory
-
-
Manually annotated by BRENDA team
aerobic bacterium SRI 2126
commentary isolated from the hot environs of a raw sugar factory
-
-
Manually annotated by BRENDA team
aerobic bacterium SRI 2128
commentary isolated from the hot environs of a raw sugar factory
-
-
Manually annotated by BRENDA team
aerobic bacterium SRI 2140
commentary isolated from the hot environs of a raw sugar factory
-
-
Manually annotated by BRENDA team
anaerobic thermophilic bacterium AB11A
gram-negative, thermophilic, anaerobic, isolated from the non-volcanic low-temperature field, the Great Artesian Basin in Queensland
-
-
Manually annotated by BRENDA team
gene dex2
UniProt
Manually annotated by BRENDA team
isolated from sugar-cane farm soil, gene aodex
UniProt
Manually annotated by BRENDA team
Arthrobacter oxydans DSM20119T
isolated from sugar-cane farm soil, gene aodex
UniProt
Manually annotated by BRENDA team
Arthrobacter oxydans KQ11
-
-
-
Manually annotated by BRENDA team
dextranase I and II
-
-
Manually annotated by BRENDA team
strain MT-G2
-
-
Manually annotated by BRENDA team
Bacillus circulans MT-G2
strain MT-G2
-
-
Manually annotated by BRENDA team
Bacillus subtilis NRC-B233b
-
-
-
Manually annotated by BRENDA team
Catenovulum sp.
-
-
-
Manually annotated by BRENDA team
Catenovulum sp. SP03
-
-
-
Manually annotated by BRENDA team
Cellvibrio fulva
-
-
-
Manually annotated by BRENDA team
Chaetomium erraticum
-
-
-
Manually annotated by BRENDA team
Chaetomium erraticum
concentrated dextranase 2 and non-concentrated dextranase 4
-
-
Manually annotated by BRENDA team
concentrated dextranase 1 and non-concentrated dextranase 3
-
-
Manually annotated by BRENDA team
I and II
-
-
Manually annotated by BRENDA team
Chaetomium sp.
-
-
-
Manually annotated by BRENDA team
var. coprophilum
-
-
Manually annotated by BRENDA team
Chaetomium thermophilum ATCC28076
var. coprophilum
-
-
Manually annotated by BRENDA team
Chaetomium thermophilum ATCC58195
var. coprophilum
-
-
Manually annotated by BRENDA team
Chaetomium virescens ATCC32319
-
-
-
Manually annotated by BRENDA team
strain M-73
-
-
Manually annotated by BRENDA team
Flavobacterium sp. M-73
dextranase II
-
-
Manually annotated by BRENDA team
Lactobacillus bifidus
-
-
-
Manually annotated by BRENDA team
ATCC 20825, I-IV; IGC 4047; KSM 22
-
-
Manually annotated by BRENDA team
ATCC 29825
-
-
Manually annotated by BRENDA team
IGC 4047
-
-
Manually annotated by BRENDA team
NCYC 1436
-
-
Manually annotated by BRENDA team
strain 1390
-
-
Manually annotated by BRENDA team
strain KSM22
-
-
Manually annotated by BRENDA team
Lipomyces starkeyi 1390
strain 1390
-
-
Manually annotated by BRENDA team
Lipomyces starkeyi IGC 4047
IGC 4047
-
-
Manually annotated by BRENDA team
Lipomyces starkeyi KSM 22
KSM 22
-
-
Manually annotated by BRENDA team
Lipomyces starkeyi KSM22
KSM22
-
-
Manually annotated by BRENDA team
Lipomyces starkeyi KSM22
strain KSM22
-
-
Manually annotated by BRENDA team
Lipomyces starkeyi NCYC 1436
NCYC 1436
-
-
Manually annotated by BRENDA team
no activity in Streptococcus anginosus
strain NCTC10713
-
-
Manually annotated by BRENDA team
no activity in Streptococcus anginosus NCTC10713
strain NCTC10713
-
-
Manually annotated by BRENDA team
no activity in Streptococcus constellatus
strain ATCC27823
-
-
Manually annotated by BRENDA team
no activity in Streptococcus constellatus ATCC27823
strain ATCC27823
-
-
Manually annotated by BRENDA team
no activity in Streptococcus gordonii
strain ATCC10558
-
-
Manually annotated by BRENDA team
no activity in Streptococcus gordonii ATCC10558
strain ATCC10558
-
-
Manually annotated by BRENDA team
no activity in Streptococcus intermedius
strain GAI-1157
-
-
Manually annotated by BRENDA team
no activity in Streptococcus intermedius GAI-1157
strain GAI-1157
-
-
Manually annotated by BRENDA team
no activity in Streptococcus oralis
strain ATCC10557
-
-
Manually annotated by BRENDA team
no activity in Streptococcus oralis ATCC10557
strain ATCC10557
-
-
Manually annotated by BRENDA team
no activity in Streptococcus sanguinis
strain ATCC10556
-
-
Manually annotated by BRENDA team
no activity in Streptococcus sanguinis ATCC10556
strain ATCC10556
-
-
Manually annotated by BRENDA team
dextranase I, II and III
-
-
Manually annotated by BRENDA team
isoenzyme 1; isoenzyme 2; isoenzyme 3
-
-
Manually annotated by BRENDA team
15 isolates with dextranolytic activity
-
-
Manually annotated by BRENDA team
strain Dex40-8 and Dex50-2
-
-
Manually annotated by BRENDA team
strain Dex70-1B and Dex70-34
-
-
Manually annotated by BRENDA team
strain Dex40-8 and Dex50-2
-
-
Manually annotated by BRENDA team
strain Dex70-1B and Dex70-34
-
-
Manually annotated by BRENDA team
Westling 1, I und II
-
-
Manually annotated by BRENDA team
strain D5884
-
-
Manually annotated by BRENDA team
strain NRRL 21969
-
-
Manually annotated by BRENDA team
Penicillium sp. D5884
strain D5884
-
-
Manually annotated by BRENDA team
Penicillium sp. NRRL 21969
strain NRRL 21969
-
-
Manually annotated by BRENDA team
Prevotella oralis Ig4a
Ig4a
-
-
Manually annotated by BRENDA team
strain UQM 733, dextranase D1, dextranase D2, dextranase D3 and dextranase D4
-
-
Manually annotated by BRENDA team
Pseudomonas sp. UQM 733
strain UQM 733, dextranase D1, dextranase D2, dextranase D3 and dextranase D4
-
-
Manually annotated by BRENDA team
strain ATCC 10114
-
-
Manually annotated by BRENDA team
Purpureocillium lilacinum 6R
strain 6R
-
-
Manually annotated by BRENDA team
Purpureocillium lilacinum NRRL 895
NRRL 895
-
-
Manually annotated by BRENDA team
IP29-strain
-
-
Manually annotated by BRENDA team
Sporothrix schenckii IP29
IP29-strain
-
-
Manually annotated by BRENDA team
strain ATCC19642, serotype a
SwissProt
Manually annotated by BRENDA team
strain E49, serotype a
SwissProt
Manually annotated by BRENDA team
strain HS-1, serotype a
-
-
Manually annotated by BRENDA team
Streptococcus criceti ATCC19642
strain ATCC19642, serotype a
SwissProt
Manually annotated by BRENDA team
Streptococcus criceti E49
strain E49, serotype a
SwissProt
Manually annotated by BRENDA team
Streptococcus criceti HS-1
strain HS-1, serotype a
-
-
Manually annotated by BRENDA team
strain MFe28, serotype h
SwissProt
Manually annotated by BRENDA team
strain MFe28, serotype h
SwissProt
Manually annotated by BRENDA team
strain K1-R
-
-
Manually annotated by BRENDA team
strain MT8148, serotype c, and strain MT8148, serotype f
SwissProt
Manually annotated by BRENDA team
Streptococcus mutans ATCC 700610
-
SwissProt
Manually annotated by BRENDA team
Streptococcus mutans Ingbritt
-
-
-
Manually annotated by BRENDA team
Streptococcus mutans Ingbritt
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
Streptococcus mutans K1-R
strain K1-R
-
-
Manually annotated by BRENDA team
strain ATCC19645
-
-
Manually annotated by BRENDA team
strain BHT, serotype b
SwissProt
Manually annotated by BRENDA team
Streptococcus ratti ATCC19645
strain ATCC19645
-
-
Manually annotated by BRENDA team
Streptococcus ratti BHT
strain BHT, serotype b
SwissProt
Manually annotated by BRENDA team
Streptococcus salivarius M36
strain M36
-
-
Manually annotated by BRENDA team
strain 6715, dextranase C and D
-
-
Manually annotated by BRENDA team
strain SL1, serotype d, and strain 6715DP, serotype g
SwissProt
Manually annotated by BRENDA team
strain 6715, dextranase C and D
-
-
Manually annotated by BRENDA team
Streptococcus sobrinus UAB66
strain UAB66
-
-
Manually annotated by BRENDA team
ATCC 10409
-
-
Manually annotated by BRENDA team
strain ATCC 10409
-
-
Manually annotated by BRENDA team
I und II; strain NRRL 1768
-
-
Manually annotated by BRENDA team
Talaromyces funiculosus 258
258
-
-
Manually annotated by BRENDA team
Talaromyces funiculosus NRRL 1768
strain NRRL 1768
-
-
Manually annotated by BRENDA team
strain ATCC 9644
-
-
Manually annotated by BRENDA team
Talaromyces luteus ATCC9644
ATCC9644
-
-
Manually annotated by BRENDA team
strain IMI068219
SwissProt
Manually annotated by BRENDA team
Talaromyces minioluteus IMI068219
strain IMI068219
SwissProt
Manually annotated by BRENDA team
Thermoanaerobacter pseudethanolicus ATCC 33223 39E
-
-
-
Manually annotated by BRENDA team
isolated from an active volcanic zone high-temperature field at the biothermal springs at Rotoruna, New Zealand
-
-
Manually annotated by BRENDA team
strain AB11Ad; strain RT364
-
-
Manually annotated by BRENDA team
Thermoanaerobacter sp. AB11Ad
strain AB11Ad
-
-
Manually annotated by BRENDA team
Thermoanaerobacter sp. Rt364
isolated from an active volcanic zone high-temperature field at the biothermal springs at Rotoruna, New Zealand
-
-
Manually annotated by BRENDA team
Thermoanaerobacter sp. Rt364
strain RT364
-
-
Manually annotated by BRENDA team
thermophilic bacterium DP17
-
-
-
Manually annotated by BRENDA team
strain TMO
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
A9UKG4
dextranase hydrolyzes the alpha-1,6 glucosidic bond of dextran to release isomaltooligosaccharides, as endo-dextranase, produced by various microorganisms including bacteria, yeast, and fungi
physiological function
Arthrobacter oxydans DSM20119T
-
dextranase hydrolyzes the alpha-1,6 glucosidic bond of dextran to release isomaltooligosaccharides, as endo-dextranase, produced by various microorganisms including bacteria, yeast, and fungi
-
additional information
F5BA50
N-terminal variable region and C-terminal variable region of the enzyme are not essentially required for catalytic activity, but induce hindered substrate binding to the active site
additional information
-
N-terminal variable region and C-terminal variable region of the enzyme are not essentially required for catalytic activity, but induce hindered substrate binding to the active site
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-sindacene-3-propionic acid, succinimidyl ester)-quenched dextran + H2O
?
show the reaction diagram
Talaromyces minioluteus, Talaromyces minioluteus IMI068219
Q27JJ3
-
-
-
?
alternan + H2O
?
show the reaction diagram
-
-
-
-
?
alternan + H2O
?
show the reaction diagram
A8F6K5
15% activity compared to dextran T70
-
-
?
alternan + H2O
?
show the reaction diagram
-
15% activity compared to dextran T70
-
-
?
alternan + H2O
?
show the reaction diagram
Thermoanaerobacter pseudethanolicus ATCC 33223 39E
-
-
-
-
?
amylopectin + H2O
?
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
?
show the reaction diagram
-
165% of the activity with dextran
-
-
?
amylopectin + H2O
?
show the reaction diagram
Thermoanaerobacter sp. AB11Ad, Thermoanaerobacter sp. Rt364
-
-
-
-
?
amylopectin + H2O
?
show the reaction diagram
Bacillus subtilis NRC-B233b
-
165% of the activity with dextran
-
-
?
amylose + H2O
?
show the reaction diagram
Thermoanaerobacter sp., Thermoanaerobacter sp. AB11Ad, Thermoanaerobacter sp. Rt364
-
-
-
-
?
arabinan + H2O
?
show the reaction diagram
-
-
-
-
?
beta-fructan + H2O
?
show the reaction diagram
Lipomyces starkeyi, Lipomyces starkeyi KSM 22, Lipomyces starkeyi IGC 4047
-
-
-
-
?
blue dextran + H2O
?
show the reaction diagram
-
-
-
-
?
blue dextran + H2O
?
show the reaction diagram
-
273% of the activity with dextran
-
-
?
blue dextran + H2O
?
show the reaction diagram
-
-
-
-
?
blue dextran + H2O
?
show the reaction diagram
-
-
-
-
?
blue dextran + H2O
?
show the reaction diagram
Bacillus subtilis NRC-B233b
-
273% of the activity with dextran
-
-
?
blue dextran brain heart infusion agar plates
?
show the reaction diagram
-
-
-
-
-
blue dextran brain heart infusion agar plates
?
show the reaction diagram
Q76EQ4
-
-
-
-
blue dextran brain heart infusion agar plates
?
show the reaction diagram
Q54443
-
-
-
-
blue dextran brain heart infusion agar plates
?
show the reaction diagram
P39653
-
-
-
-
blue dextran brain heart infusion agar plates
?
show the reaction diagram
Q8VLP4
-
-
-
-
blue dextran brain heart infusion agar plates
?
show the reaction diagram
Streptococcus salivarius M36
-
-
-
-
-
blue dextran brain heart infusion agar plates
?
show the reaction diagram
Streptococcus ratti BHT
Q76EQ4
-
-
-
-
blue-dextran + H2O
?
show the reaction diagram
-
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
show the reaction diagram
A4F2S5, Q1MVS0, -
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
show the reaction diagram
Q76EQ4
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
show the reaction diagram
Q54443
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
show the reaction diagram
P39653
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
show the reaction diagram
Q8VLP4
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
show the reaction diagram
Streptococcus criceti E49
Q1MVS0
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
show the reaction diagram
Streptococcus criceti HS-1
-
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
show the reaction diagram
Q8VLP4
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
show the reaction diagram
Streptococcus salivarius M36
-
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
show the reaction diagram
Streptococcus criceti ATCC19642
A4F2S5
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
show the reaction diagram
Streptococcus ratti BHT
Q76EQ4
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
-
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
Streptococcus mutans Ingbritt
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
Chaetomium sp.
-
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
A9UKG4
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
maltose, maltotriose and other maltosaccharides
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltotriose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltotriose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltotriose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltotriose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltotriose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltotriose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltotriose
?
dextran + H2O
oligosaccharides
show the reaction diagram
Flavobacterium sp. M-73
-
-
isomaltotriose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
show the reaction diagram
Flavobacterium sp. M-73
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
substrate dextran 250 kDa
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
substrates are dextrans of 15-25 kDa and 410 kDa. Ten units of dextranase can reduce dextran content by 67% in 24 h and 56% in 72 h from sugarcane juice of cane variety CoS 86032
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
Purpureocillium lilacinum 6R
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
Talaromyces luteus ATCC9644
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
show the reaction diagram
Talaromyces luteus ATCC9644
-
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
Sporothrix schenckii IP29
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
Bacillus subtilis NRC-B233b
-
substrate dextran 250 kDa
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
Lipomyces starkeyi IGC 4047
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
substrates are dextrans of 15-25 kDa and 410 kDa. Ten units of dextranase can reduce dextran content by 67% in 24 h and 56% in 72 h from sugarcane juice of cane variety CoS 86032
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
Talaromyces funiculosus 258
-
-
-
-
-
dextran + H2O
oligosaccharides
show the reaction diagram
Talaromyces funiculosus 258
-
-
-
-
?
dextran + H2O
?
show the reaction diagram
-
-
-
-
?
dextran + H2O
?
show the reaction diagram
-
-
-
-
?
dextran + H2O
?
show the reaction diagram
-
-
-
-
?
dextran + H2O
?
show the reaction diagram
-
-
-
-
?
dextran + H2O
?
show the reaction diagram
-
-
-
-
?
dextran + H2O
?
show the reaction diagram
Chaetomium erraticum
-
-
-
-
?
dextran + H2O
?
show the reaction diagram
-, Q6VUG7
-
-
-
?
dextran + H2O
?
show the reaction diagram
F5BA50
-
-
-
?
dextran + H2O
?
show the reaction diagram
-
extent of hydrolysis of 5-aminosalicylic acid-dextran conjugates (secondary amines) by dextranase is in part controlled by the degree of oxidation and by the amount of conjugated 5-aminosalicylic acid. Less oxidised dextrans (12%) conjugating proportionally less 5-aminosalicylic acid are successfully hydrolysed by dextranase
-
-
?
dextran + H2O
?
show the reaction diagram
-
substrate dextran T-20 98.9%, dextran 20000 91.3%, dextran T-70 98.3%, dextran T-500 85.1%, dextran T-2000 86.7% relative activity, respectively
-
-
?
dextran + H2O
?
show the reaction diagram
Lipomyces starkeyi NCYC 1436
-
-
-
-
?
dextran + H2O
?
show the reaction diagram
Lipomyces starkeyi KSM22
-
-
-
-
?
dextran + H2O
?
show the reaction diagram
Penicillium sp. D5884
-
extent of hydrolysis of 5-aminosalicylic acid-dextran conjugates (secondary amines) by dextranase is in part controlled by the degree of oxidation and by the amount of conjugated 5-aminosalicylic acid. Less oxidised dextrans (12%) conjugating proportionally less 5-aminosalicylic acid are successfully hydrolysed by dextranase
-
-
?
dextran + H2O
?
show the reaction diagram
Lipomyces starkeyi 1390
-
-
-
-
?
dextran + H2O
?
show the reaction diagram
Arthrobacter oxydans KQ11
-
substrate dextran T-20 98.9%, dextran 20000 91.3%, dextran T-70 98.3%, dextran T-500 85.1%, dextran T-2000 86.7% relative activity, respectively
-
-
?
dextran + H2O
?
show the reaction diagram
F5BA50, -
-
-
-
?
dextran + H2O
isomaltotriose
show the reaction diagram
Streptococcus mutans, Streptococcus mutans K1-R
-
-
-
-
?
dextran + H2O
fragments of dextran
show the reaction diagram
-
-
-
-
?
dextran + H2O
fragments of dextran
show the reaction diagram
-
-
-
-
?
dextran + H2O
fragments of dextran
show the reaction diagram
-
-
-
-
?
dextran + H2O
fragments of dextran
show the reaction diagram
-
-
-
-
?
dextran + H2O
fragments of dextran
show the reaction diagram
P48845, -
-
-
-
?
dextran + H2O
fragments of dextran
show the reaction diagram
Streptococcus ratti ATCC19645
-
-
-
-
?
dextran + H2O
D-glucose + isomaltose
show the reaction diagram
-
-
-
-
?
dextran + H2O
D-glucose + isomaltotriose + isomaltose + isomaltooligosaccharide
show the reaction diagram
Prevotella oralis, Prevotella oralis Ig4a
-
-
-
-
?
dextran + H2O
D-glucose + isomaltose + isomalto-oligosaccharides
show the reaction diagram
-
-
-
-
?
dextran + H2O
d-glucose + isomaltose + isomaltotriose + ?
show the reaction diagram
-
-
-
-
?
dextran + H2O
isomalto-oligosaccharides
show the reaction diagram
-
-
-
-
?
dextran + H2O
isomalto-oligosaccharides
show the reaction diagram
-
dextranase D1
isomaltobiose-isomaltodecaose
-
?
dextran + H2O
isomalto-oligosaccharides
show the reaction diagram
-
dextranase D2
isomaltotetraose-isomaltodecaose
-
?
dextran + H2O
isomalto-oligosaccharides
show the reaction diagram
Lipomyces starkeyi KSM 22
-
-
-
-
?
dextran + H2O
isomalto-oligosaccharides
show the reaction diagram
Pseudomonas sp. UQM 733
-
dextranase D1
isomaltobiose-isomaltodecaose
-
?
dextran + H2O
isomalto-oligosaccharides
show the reaction diagram
Pseudomonas sp. UQM 733
-
dextranase D2
isomaltotetraose-isomaltodecaose
-
?
dextran + H2O
isomalto-oligosaccharides
show the reaction diagram
Lipomyces starkeyi IGC 4047
-
-
-
-
?
dextran + H2O
isomalto-oligosaccharides + D-glucose
show the reaction diagram
Pseudomonas sp., Pseudomonas sp. UQM 733
-
D4
-
-
?
dextran + H2O
isomaltooligosaccharides
show the reaction diagram
-
-
-
-
?
dextran + H2O
isomaltooligosaccharides
show the reaction diagram
-
immobilized enzyme
-
-
?
dextran + H2O
isomaltotriose + D-glucose
show the reaction diagram
-
-
-
-
?
dextran + H2O
isomaltotetraose + cycloisomaltooligosaccharides
show the reaction diagram
H2EI27
-
main products are isomaltotetraose and small amounts of cycloisomaltooligosaccharides with a degree of polymerization of 7-14
-
?
dextran 742CB + H2O
?
show the reaction diagram
Thermoanaerobacter pseudethanolicus, Thermoanaerobacter pseudethanolicus ATCC 33223 39E
-
-
-
-
?
dextran derivates + H2O
?
show the reaction diagram
-
-
-
-
?
dextran T10 + H2O
isomaltose + isomaltotriose
show the reaction diagram
A8F6K5
73% activity compared to dextran T70
-
-
?
dextran T10 + H2O
isomaltose + isomaltotriose
show the reaction diagram
-
73% activity compared to dextran T70
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose
show the reaction diagram
A8F6K5
96% activity compared to dextran T70, the enzyme activity is very specific for alpha-(1-6)-glucosidic glucan
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose
show the reaction diagram
-
96% activity compared to dextran T70, the enzyme activity is very specific for alpha-(1-6)-glucosidic glucan
-
-
?
dextran T2000 + H2O
?
show the reaction diagram
-
-
-
-
?
dextran T2000 + H2O
?
show the reaction diagram
H2EI27
-
-
-
?
dextran T2000 + H2O
?
show the reaction diagram
Thermoanaerobacter pseudethanolicus ATCC 33223 39E
-
-
-
-
?
dextran T2000 + H2O
isomaltotriose + isomaltoteraose + isomaltopentaose
show the reaction diagram
-
-
main end-products
-
?
dextran T40 + H2O
isomaltose + isomaltotriose
show the reaction diagram
A8F6K5
88% activity compared to dextran T70
-
-
?
dextran T500 + H2O
isomaltose + isomaltotriose
show the reaction diagram
A8F6K5
96% activity compared to dextran T70
-
-
?
dextran T500 + H2O
?
show the reaction diagram
Thermoanaerobacter pseudethanolicus, Thermoanaerobacter pseudethanolicus ATCC 33223 39E
-
-
-
-
?
dextran T70 + H2O
isomaltose + isomaltotriose
show the reaction diagram
A8F6K5
100% activity
-
-
?
dextran-100 + H2O
isomaltose
show the reaction diagram
Talaromyces funiculosus, Talaromyces funiculosus NRRL 1768
-
-
-
-
?
dextrin + H2O
?
show the reaction diagram
-
-
-
-
?
glucan + H2O
?
show the reaction diagram
-
-
-
-
?
glucan + H2O
?
show the reaction diagram
-
-
-
-
?
glucan + H2O
?
show the reaction diagram
-
insoluble
-
-
?
glucan + H2O
?
show the reaction diagram
Lipomyces starkeyi KSM 22, Lipomyces starkeyi IGC 4047
-
-
-
-
?
glucan + H2O
?
show the reaction diagram
Bacillus circulans MT-G2
-
insoluble
-
-
?
glucan + H2O
?
show the reaction diagram
Streptococcus sobrinus UAB66
-
-
-
-
?
glucan + H2O
fragments of glucan
show the reaction diagram
-
-
-
-
?
glucan + H2O
D-glucose + isomaltose + isomaltotriose + ?
show the reaction diagram
-
from Streptococcus sobrinus K1-R
-
-
?
glycogen + H2O
?
show the reaction diagram
Bacillus circulans, Bacillus circulans MT-G2
-
-
-
-
?
inulin + H2O
?
show the reaction diagram
-
7% activity compared to dextran
-
-
?
inulin + H2O
?
show the reaction diagram
-
170% of the activity with dextran
-
-
?
inulin + H2O
?
show the reaction diagram
Lipomyces starkeyi KSM22
-
7% activity compared to dextran
-
-
?
inulin + H2O
?
show the reaction diagram
Bacillus subtilis NRC-B233b
-
170% of the activity with dextran
-
-
?
isolmaltodextrins + H2O
?
show the reaction diagram
-
-
-
-
?
isomaltodextrin + H2O
?
show the reaction diagram
-
-
-
-
?
isomaltodextrin + H2O
?
show the reaction diagram
Talaromyces luteus, Talaromyces luteus ATCC9644
-
-
-
-
?
isomaltoheptaose + H2O
?
show the reaction diagram
H2EI27
-
-
-
?
isomaltohexaose + H2O
?
show the reaction diagram
H2EI27
-
-
-
?
isomaltopentaose + H2O
?
show the reaction diagram
H2EI27
-
-
-
?
laminarin + H2O
?
show the reaction diagram
Bacillus circulans, Bacillus circulans MT-G2
-
-
-
-
?
levan + H2O
?
show the reaction diagram
-
-
-
-
?
levan + H2O
?
show the reaction diagram
-
4% activity compared to dextran
-
-
?
levan + H2O
?
show the reaction diagram
Lipomyces starkeyi KSM 22
-
-
-
-
?
levan + H2O
?
show the reaction diagram
Lipomyces starkeyi KSM22
-
4% activity compared to dextran
-
-
?
mutan + H2O
?
show the reaction diagram
Lipomyces starkeyi, Lipomyces starkeyi KSM22
-
8% activity compared to dextran
-
-
?
nigeran + H2O
?
show the reaction diagram
Bacillus circulans, Bacillus circulans MT-G2
-
-
-
-
?
pullulan + H2O
?
show the reaction diagram
A8F6K5
4% activity compared to dextran T70
-
-
?
pullulan + H2O
?
show the reaction diagram
-
4% activity compared to dextran T70
-
-
?
Sephadex G-100 + H2O
?
show the reaction diagram
Penicillium chrysogenum, Lipomyces starkeyi, Cytophaga sp., Purpureocillium lilacinum, Talaromyces aculeatus, Lipomyces starkeyi KSM 22, Purpureocillium lilacinum NRRL 895, Lipomyces starkeyi IGC 4047
-
-
-
-
?
Sephadex G-150 + H2O
?
show the reaction diagram
-
-
-
-
?
Sephadex G-200 + H2O
?
show the reaction diagram
-
-
-
-
?
Sephadex G-25 + H2O
?
show the reaction diagram
Penicillium chrysogenum, Talaromyces funiculosus, Purpureocillium lilacinum, Talaromyces aculeatus, Talaromyces funiculosus NRRL 1768, Purpureocillium lilacinum NRRL 895
-
-
-
-
?
Sephadex G-50 + H2O
?
show the reaction diagram
-
-
-
-
?
Sephadex G-75 + H2O
?
show the reaction diagram
Talaromyces funiculosus, Talaromyces funiculosus NRRL 1768
-
-
-
-
?
soluble starch + H2O
?
show the reaction diagram
Lipomyces starkeyi, Lipomyces starkeyi KSM22
-
22% activity compared to dextran
-
-
?
starch + H2O
?
show the reaction diagram
-
228% of the activity with dextran
-
-
?
starch + H2O
?
show the reaction diagram
Thermoanaerobacter sp. AB11Ad, Thermoanaerobacter sp. Rt364
-
-
-
-
?
starch + H2O
?
show the reaction diagram
Bacillus subtilis NRC-B233b
-
228% of the activity with dextran
-
-
?
starch + H2O
?
show the reaction diagram
Bacillus circulans MT-G2
-
-
-
-
?
streptococcal glucan + H2O
?
show the reaction diagram
Streptococcus mutans, Streptococcus mutans K1-R
-
-
-
-
?
sucrose + H2O
?
show the reaction diagram
-
100% of the activity with dextran
-
-
?
levan + H2O
?
show the reaction diagram
Lipomyces starkeyi IGC 4047
-
-
-
-
?
additional information
?
-
-
enzyme influences glucan synthesis, linkage remodeling and branching
-
-
-
additional information
?
-
-
dextrans with a maximum degree of oxidation (93%) giving maximum conjugation of 5-aminosalicylic acid are resistant to dextranase hydrolysis
-
-
-
additional information
?
-
A4F2S5, Q1MVS0, -
no activity on blue dextran brain heart infusion agar plates
-
-
-
additional information
?
-
A8F6K5
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
-
additional information
?
-
A9UKG4
AODex treatment of stale sugar cane juice results in a yield of square and light-colored sugar crystals
-
-
-
additional information
?
-
-
enzyme hydrolyzed alpha-1,6 glucosidic bonds but not alpha-1,4 glucosidic bonds
-
-
-
additional information
?
-
H2EI27
glycosyl hydrolase family 66 enzymes may be classified into three types: dextranases showing only dextranolytic activity, dextranases catalyzing hydrolysis with low cyclization activity, and cycloisomaltooligosaccharide glucanotransferases showing cycloisomaltooligosaccharide-forming activity with low dextranolytic activity, no or very low activity on substrates isomaltose, isomaltotriose, isomaltotetraose
-
-
-
additional information
?
-
H2EI27
glycosyl hydrolase family 66 enzymes may be classified into three types: dextranases showing only dextranolytic activity, dextranases catalyzing hydrolysis with low cyclization activity, and cycloisomaltooligosaccharide glucanotransferases showing cycloisomaltooligosaccharide-forming activity with low dextranolytic activity, no or very low activity on substrates isomaltose, isomaltotriose, isomaltotetraose
-
-
-
additional information
?
-
Streptococcus criceti E49
Q1MVS0
no activity on blue dextran brain heart infusion agar plates
-
-
-
additional information
?
-
Arthrobacter oxydans DSM20119T
A9UKG4
AODex treatment of stale sugar cane juice results in a yield of square and light-colored sugar crystals
-
-
-
additional information
?
-
Streptococcus criceti HS-1
-
no activity on blue dextran brain heart infusion agar plates
-
-
-
additional information
?
-
Penicillium sp. D5884
-
dextrans with a maximum degree of oxidation (93%) giving maximum conjugation of 5-aminosalicylic acid are resistant to dextranase hydrolysis
-
-
-
additional information
?
-
Streptococcus criceti ATCC19642
A4F2S5
no activity on blue dextran brain heart infusion agar plates
-
-
-
additional information
?
-
A8F6K5, -
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
-
additional information
?
-
Arthrobacter oxydans KQ11
-
enzyme hydrolyzed alpha-1,6 glucosidic bonds but not alpha-1,4 glucosidic bonds
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alternan + H2O
?
show the reaction diagram
A8F6K5
15% activity compared to dextran T70
-
-
?
alternan + H2O
?
show the reaction diagram
-
15% activity compared to dextran T70
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
Chaetomium sp.
-
-
-
-
?
dextran + H2O
oligosaccharides
show the reaction diagram
A9UKG4
-
-
-
?
dextran + H2O
fragments of dextran
show the reaction diagram
-
-
-
-
?
dextran + H2O
fragments of dextran
show the reaction diagram
-
-
-
-
?
dextran + H2O
fragments of dextran
show the reaction diagram
-
-
-
-
?
dextran + H2O
fragments of dextran
show the reaction diagram
-
-
-
-
?
dextran + H2O
fragments of dextran
show the reaction diagram
P48845, -
-
-
-
?
dextran + H2O
fragments of dextran
show the reaction diagram
Streptococcus ratti ATCC19645
-
-
-
-
?
dextran T10 + H2O
isomaltose + isomaltotriose
show the reaction diagram
A8F6K5
73% activity compared to dextran T70
-
-
?
dextran T10 + H2O
isomaltose + isomaltotriose
show the reaction diagram
-
73% activity compared to dextran T70
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose
show the reaction diagram
A8F6K5
96% activity compared to dextran T70, the enzyme activity is very specific for alpha-(1-6)-glucosidic glucan
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose
show the reaction diagram
-
96% activity compared to dextran T70, the enzyme activity is very specific for alpha-(1-6)-glucosidic glucan
-
-
?
dextran T40 + H2O
isomaltose + isomaltotriose
show the reaction diagram
A8F6K5
88% activity compared to dextran T70
-
-
?
dextran T500 + H2O
isomaltose + isomaltotriose
show the reaction diagram
A8F6K5
96% activity compared to dextran T70
-
-
?
dextran T70 + H2O
isomaltose + isomaltotriose
show the reaction diagram
A8F6K5
100% activity
-
-
?
pullulan + H2O
?
show the reaction diagram
A8F6K5
4% activity compared to dextran T70
-
-
?
pullulan + H2O
?
show the reaction diagram
-
4% activity compared to dextran T70
-
-
?
glucan + H2O
fragments of glucan
show the reaction diagram
-
-
-
-
?
additional information
?
-
A8F6K5
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
-
additional information
?
-
Arthrobacter oxydans, Arthrobacter oxydans DSM20119T
A9UKG4
AODex treatment of stale sugar cane juice results in a yield of square and light-colored sugar crystals
-
-
-
additional information
?
-
A8F6K5, -
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AgNO3
-
1 mM, 71% activity compared to control without any metal ion
AlCl3
-
1 mM, 96% activity compared to control without any metal ion
BaCl2
-
1 mM, 90% activity compared to control without any metal ion
Ca2+
-
no effect to enzyme stability
Ca2+
-
1 mM stimulates 2fold
CaCl2
-
1 mM, 94% activity compared to control without any metal ion
CdCl2
-
1 mM, 87% activity compared to control without any metal ion
Co2+
-
10 mM, 196% of initial activity
CoCl2
-
1 mM, 101% activity compared to control without any metal ion
CuCl2
-
1 mM, 107% activity compared to control without any metal ion
Fe2+
A9UKG4
stimulates activity of the dextransucrase-dextranase fusion protein
Fe3+
-
no effect to enzyme stability
FeCl3
-
1 mM, 96% activity compared to control without any metal ion
HgCl2
-
1 mM, 73% activity compared to control without any metal ion
K+
A9UKG4
stimulates activity of the dextransucrase-dextranase fusion protein
KCl
-
1 mM, 91% activity compared to control without any metal ion
Li+
A9UKG4
stimulates activity of the dextransucrase-dextranase fusion protein
LiCl
-
1 mM, 91% activity compared to control without any metal ion
Mg2+
-
1 mM enhances enzyme activity by 145%
Mg2+
A8F6K5
activity increases to 125% in the presence of 1 mM Mg2+
MgCl2
-
1 mM, 95% activity compared to control without any metal ion
NaCl
-
1 mM, 94% activity compared to control without any metal ion
Ni2+
A8F6K5
activity increases to 125% in the presence of 1 mM Ni2+
Ni2+
A9UKG4
stimulates activity of the dextransucrase-dextranase fusion protein
NiSO4
-
1 mM, 101% activity compared to control without any metal ion
RbCl
-
1 mM, 95% activity compared to control without any metal ion
SDS
-
1 mM, 94% activity compared to control without any metal ion
SnCl2
-
1 mM, 101% activity compared to control without any metal ion
ZnCl2
-
1 mM, 102% activity compared to control without any metal ion
MnCl2
-
1 mM, 71% activity compared to control without any metal ion
additional information
A8F6K5
Ca2+, Li+, K+, and Na+ (with chloride) do not show appreciable effects on activity
additional information
-
no effects on enzyme activity by K+, Mg2+, and Ca2+ on both free and immobilized enzymes
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
-
4-chloromercuribenzoate
-
immobilized enzyme
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
Flavobacterium sp. M-73
-
-
4-chloromercuribenzoate
-
CD-I only
4-chloromercuribenzoate
-
-
aflatoxin B1
Q27JJ3
inhibits dextranase activities of CYP3A4-expressing cultures, maximum inhibition of 22% at 2 microg/ml. Only negligibly inhibits strain INVSC1 expressing dextranase
aflatoxin G1
Q27JJ3
substantially less inhibitory towards dextranase activities of CYP3A4-expressing cultures than aflatoxin B1, showing a maximum inhibition of about 12% at 2 microg/ml, whereas strain INVSC1 expressing dextranase is only marginally inhibited
Ag+
A8F6K5
10% residual activity at 1 mM Ag+
Ag+
A9UKG4
strong inhibitor
AgNO3
-
1 mM, 71% activity compared to control without any metal ion
Al3+
-
1 mM completely inhibits enzyme activity
AlCl3
-
1 mM, 96% activity compared to control without any metal ion
BaCl2
-
1 mM, 90% activity compared to control without any metal ion
CaCl2
-
1 mM, 94% activity compared to control without any metal ion
Cd2+
-
5 mM, 54% residual activity
CdCl2
-
1 mM, 87% activity compared to control without any metal ion
Co2+
Flavobacterium sp. M-73
-
-
Cu2+
Flavobacterium sp. M-73
-
-
Cu2+
-
partial inhibition
Cu2+
-
1 mM completely inhibits enzyme activity
Cu2+
-
93% inhibition of the free enzme, 56.5% inhibition of the immobilized enzyme
deoxycholic acid
Streptococcus mutans Ingbritt
-
-
dextranase inhibitor
-
-
-
EDTA
Flavobacterium sp. M-73
-
-
Fe2+
A8F6K5
10% residual activity at1 mM Fe2+
Fe2+
-
41.5% inhibition of the free enzme, 18% inhibition of the immobilized enzyme
Fe3+
Streptococcus mutans Ingbritt
-
-
Fe3+
Flavobacterium sp. M-73
-
-
Fe3+
-
1 mM completely inhibits enzyme activity
Fe3+
-
5 mM, 5.04% residual activity
FeCl3
-
1 mM, 96% activity compared to control without any metal ion
Ferrous ammonium sulphate
-
-
guanidine/HCl
-
-
Hg2+
Streptococcus mutans Ingbritt
-
-
Hg2+
Flavobacterium sp. M-73
-
-
Hg2+
A9UKG4
strong inhibitor
Hg2+
-
complete inhibition of the free enzme and the immobilized enzyme
HgCl2
-
1 mM, 73% activity compared to control without any metal ion
KCl
-
1 mM, 91% activity compared to control without any metal ion
LiCl
-
1 mM, 91% activity compared to control without any metal ion
mercaptoethanol
-
immobilized enzyme
MgCl2
-
1 mM, 95% activity compared to control without any metal ion
Mn2+
-
23% inhibition of the free enzme, 6% inhibition of the immobilized enzyme
Na+
-
85% inhibition of the free enzme, 60% inhibition of the immobilized enzyme
NaCl
-
1 mM, 94% activity compared to control without any metal ion
NaCl
-
10%, 4fold decrease in activity
Ni2+
-
5 mM, 6.1% residual activity
Pb2+
-
partial inhibition
potassium ferricyanide
-
immobilized enzyme
RbCl
-
1 mM, 95% activity compared to control without any metal ion
Rose bengal
-
-
SDS
Streptococcus mutans Ingbritt
-
-
SDS
-
1 mM, 94% activity compared to control without any metal ion
SDS
-
1 mM completely inhibits enzyme activity
Sodium ascorbate
-
immobilized enzyme
Sodium azide
-
immobilized enzyme
sodium dodecylsulfate
-
0.05%, 14% residual activity
Sodium m-periodate
-
-
T-2 toxin
Q27JJ3
100% inhibition at 10 microg/ml of dextranase activities of CYP3A4-expressing cultures and strain INVSC1
Zn2+
Streptococcus mutans Ingbritt
-
-
Zn2+
Flavobacterium sp. M-73
-
-
Zn2+
-
21% inhibition of the free enzme, 8% inhibition of the immobilized enzyme
MnCl2
-
1 mM, 71% activity compared to control without any metal ion
additional information
-
not inhibited by Mn2+, Co2+, Zn2+, Ni2+, PCMB and EDTA
-
additional information
-
stable to EDTA
-
additional information
-
not inhibited by dithiothreitol, 2-mercaptoethanol and EDTA
-
additional information
-
stable to Cu2+, Fe3+, Mg2+, Zn2+, EDTA and iodoacetamide
-
additional information
-
stable to iodoacetate, PCMB and EDTA
-
additional information
-
not inhibited by Mn2+, Co2+, Al3+, Mg2+ and EDTA
-
additional information
-
stable to EDTA
-
additional information
-
degree of enzyme inactivation declines with increasing ratio dextranase per dextranase adsorbate bentonite, at a ratio below 0.5: (w/w) only one half of the initial activity is retained
-
additional information
Q27JJ3
no significant inhibition of dextranase activities of CYP3A4-expressing cultures and strain INVSC1 at concentrations of 2, 20, 200, and 2000 ng/ml by deoxynivalenol, fumonisin B1, and ochratoxin A
-
additional information
Chaetomium erraticum
-
for successful adsorption, enzyme to bentonite ratios greater than 0.4 (w/w) have to be used as lower ratios lead to 90% enzyme inactivation due to bentonite contact
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ca2+
Flavobacterium sp. M-73
-
-
CoCl2
-
1 mM, 101% activity compared to control without any metal ion
CuCl2
-
1 mM, 107% activity compared to control without any metal ion
Mg2+
Flavobacterium sp. M-73
-
-
NiSO4
-
1 mM, 101% activity compared to control without any metal ion
SnCl2
-
1 mM, 101% activity compared to control without any metal ion
ZnCl2
-
1 mM, 102% activity compared to control without any metal ion
Mn2+
Flavobacterium sp. M-73
-
-
additional information
-
highest immobilization efficiency at 200 mg Eupergit C with a ratio of activity of immobilized enzyme to the activity of soluble enzyme of 90%, higher amounts of Eupergit C yield lower immobilization efficiency. Immobilization duration increases immobilization efficiency
-
additional information
Chaetomium erraticum
-
bentonite carriers exhibit high monolayer protein and activity loads at pH 4.0 and after pH-shift to 5.4. If dextranase is adsorbed at pH 4.1 and hydroxyapatite is washed several times with buffer at pH 5.4 reveals highest activity yield so far (28%). Other selected carriers used are hydroxyapatite and Streamline DEAE. In general, immobilization yields are low and in case of DEAE the rather high particle size is problematic. Porous Eupergit differs only moderately in activity using low molecular weight substrate, whereas macroporous Eupergit reveals enhanced activity for high molecular weight substrates. Activation of the carbohydrate moiety of dextranase by metaperiodate results in active silica gels, whereas the activation of alginate via Woodwards reagent K exhibits extremely low activities
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00011
-
Dextran
-
-
0.0002
-
Dextran
-
substrate dextran 70 kDa, pH 5.0, 35C
0.0005
-
Dextran
-
substrate dextran 40 kDa, pH 5.0, 35C
0.00175
-
Dextran
-
substrate dextran 20 kDa, pH 5.0, 35C
0.003
0.456
Dextran
-
depends on the kind of dextran
0.025
-
Dextran
-
immobilized enzyme 0.029
0.0555
-
Dextran
-
soluble enzyme
0.067
-
Dextran
-
-
0.0714
-
Dextran
-
immobilized enzyme
1.1
-
Dextran
-
175000-molecular-weight dextranase
1.25
-
Dextran
-
160000-molecular-weight dextranase
0.0003
-
Dextran T-2000
-
-
-
0.000000183
-
dextran T2000
H2EI27
pH 5.5, 35C
-
0.000288
-
isomaltoheptaose
H2EI27
pH 5.5, 35C
1.3
-
isomaltoheptaose
-
-
2.1
-
isomaltoheptaose
-
-
0.000386
-
isomaltohexaose
H2EI27
pH 5.5, 35C
1.9
-
isomaltohexaose
-
-
2.3
-
isomaltohexaose
-
-
0.0004
-
isomaltopentaose
H2EI27
pH 5.5, 35C
2.6
-
isomaltopentaose
-
-
4.1
-
isomaltopentaose
-
-
4
-
isomaltotetraose
-
-
6.5
-
isomaltotetraose
-
-
25
-
isomaltotriose
-
-
3.05
-
Dextran
-
pH not specified in the publication, temperature not specified in the publication
additional information
-
dextran 742CB
-
Km value is 2.9 mg/ml, pH 5.2, 70C
-
0.0004
-
Dextran T-2000
-
-
-
additional information
-
dextran T2000
-
Km value is 6.4 mg/ml, pH 5.2, 70C
-
0.0095
-
dextran T2000
A8F6K5
in 40 mM sodium acetate buffer (pH4.3) at 55C
-
additional information
-
dextran T500
-
Km value is 2.5 mg/ml, pH 5.2, 70C
-
31
-
isomaltotriose
-
-
additional information
-
additional information
-
0.06 microgram/ml, dextran
-
additional information
-
additional information
-
0.26 g/l, dextran
-
additional information
-
additional information
Chaetomium erraticum
-
KM-values of soluble and adsorbed enzymes do not differ significantly
-
additional information
-
additional information
-
0.9 g (500 kDa dextran) per l; 1.3 g (500 kDa dextran) per l
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
760
-
Dextran
-
dextranase I
760
-
Dextran
-
based on the molecular weight of isomaltose
2230
-
Dextran
-
dextranase II
2230
-
Dextran
-
based on the molecular weight of isomaltose
3.7
-
dextran 742CB
-
pH 5.2, 70C
-
10.2
-
dextran T2000
-
pH 5.2, 70C
-
44.3
-
dextran T2000
H2EI27
pH 5.5, 35C
-
8.1
-
dextran T500
-
pH 5.2, 70C
-
7.93
-
isomaltoheptaose
H2EI27
pH 5.5, 35C
7.53
-
isomaltohexaose
H2EI27
pH 5.5, 35C
4.36
-
isomaltopentaose
H2EI27
pH 5.5, 35C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
27500
-
isomaltoheptaose
H2EI27
pH 5.5, 35C
4096
19500
-
isomaltohexaose
H2EI27
pH 5.5, 35C
3244
10500
-
isomaltopentaose
H2EI27
pH 5.5, 35C
3077
additional information
-
dextran 742CB
-
Km value is 1.25ml per mg and s, pH 5.2, 70C
0
additional information
-
dextran T2000
-
kcat_/Km value is 5.9 ml per mg and s, pH 5.2, 70C
0
242000000
-
dextran T2000
H2EI27
pH 5.5, 35C
0
additional information
-
dextran T500
-
Km value is 3.3 ml per mg and s, pH 5.2, 70C
0
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.005
0.085
-
depends on the growth rate
0.03
-
aerobic bacterium SRI 2125
-
-
0.06
-
aerobic bacterium SRI 2128
-
-
0.12
-
anaerobic thermophilic bacterium AB11A
-
-
0.21
-
thermophilic bacterium DP17
-
-
0.4
40
-
units of dextran per ml, value depends on the medium
0.5
-
-
substrate alternan, pH 5.2, 70C
2.7
-
-
substrate dextran 742CB, pH 5.2, 70C
3.02
-
F5BA50
purified recombinant enzyme SmDex95, the 95 kDa variant, pH 5.0, temperature not specified in the publication
6.2
-
-
substrate dextran T500, pH 5.2, 70C
7.37
-
-
substrate dextran T2000, pH 5.2, 70C
8.21
-
F5BA50
purified recombinant enzyme SmDex90, the 90 kDa variant, pH 5.0, temperature not specified in the publication
11.9
-
-
pH 5.5, 45C
12.7
-
-
isomaltose
13.66
-
-
wild type enzyme, at pH 4.5, 30C
14.93
-
-
mutant enzyme D279C/S289C, at pH 4.5, 43C
18.2
-
-
dextranase II, U/ml
25.6
-
-
mutant enzyme T245C/N248C, at pH 5.0, 33C
34.6
-
-
dextranase I, U/ml
36.5
-
Flavobacterium sp. M-73
-
-
43
-
-
units/A units
44.52
-
-
mutant enzyme D279C/S289C, at pH 5.0, 33C
90
-
-
3.5% dextran; immobilized enzyme 57 U/mg
123
-
-
-
182
-
-
enzyme purified 17.56fold
188.3
-
-
enzyme purified 18.18fold
218
-
-
Tsuchiya medium
238
-
-
Fukumota medium
292
-
-
Fukumota medium
493
-
-
units/OD
762
-
Streptococcus mutans Ingbritt
-
-
770
-
-
dextranase I
950
1000
-
recombinant dextranase
1560
-
-
bovine serum albumin immobilized enzyme, pH 5.5, 60C
1670
-
-
dextranase II
1920
-
-
CD-II
1960
-
-
CD-I
2500
-
-
dextranase II
2560
-
-
dextranase I
8130
-
-
free enzyme, pH 5.5, 60C
10580
-
-
160000-molecular-weight dextranase
14500
-
-
175000-molecular-weight dextranase
additional information
-
-
release of 78.5 mg of Remazol Blue R-250 dye/min at 50C
additional information
-
Chaetomium erraticum
-
6356.3 dextranase units/mg, one unitis the amount of enzyme that degrades dextran to produce reducing sugar equivalent to 1 mg maltose per h per g at 40C and pH 5.4
additional information
-
-
60603.3 dextranase units/mg, concentrated dextranase 1, one dextranase unit is the amount of enzyme that degrades dextran to produce reducing sugar equivalent to 1 mg maltose per h per g at 40C and pH 5.4; 8290.8 dextranase units/mg, concentrated dextranase 3, factory 2, amount of enzyme that degrades dextran to produce reducing sugar equivalent to 1 mg maltose per h per g at 40C and pH 5.4; 8402.8 dextranase units/mg, concentrated dextranase 3, factory 1, amount of enzyme that degrades dextran to produce reducing sugar equivalent to 1 mg maltose per h per g at 40C and pH 5.4
additional information
-
A9UKG4
activities of recombinant fusion protein and of wild-type dextranase in fermentation, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.3
-
A8F6K5
-
4.5
5.5
-
dextranase D1
4.5
7.5
-
dextranase D2
4.6
-
-
dextranase II
4.8
-
-
dextranase I and II
5
6.5
-
-
5
-
-
dextranase I
5.2
-
-
160000-molecular-weight dextranase
5.2
-
-
dextranase D
5.2
-
A9UKG4
recombinant wild-type dextranase
5.3
-
Cellvibrio fulva
-
-
5.4
5.8
Chaetomium erraticum, Chaetomium gracile
-
in juice, syrups are less optimal than juices
5.4
-
-
175000-molecular-weight dextranase
5.4
-
-
dextranase C
5.4
-
Chaetomium erraticum
-
soluble and adsorbed enzyme
5.5
-
-
immobilized enzyme pH 6.0
5.5
-
Streptococcus mutans Ingbritt
-
-
5.5
-
-
dextranase D4
5.5
-
-
free enzyme
5.6
-
-
immobilized enzyme
5.8
-
A9UKG4
recombinant engineered fusion protein DSXR
6
6.5
-
dex2 from strain Dex50-2
6
-
-
immobilized enzyme
7
7.5
-
dex1 from strain Dex40-8
7
-
Flavobacterium sp. M-73
-
-
7
-
-
dex1 from strain Dex50-2
8
-
Catenovulum sp.
-
-
additional information
-
-
optimum pH for activity 4.5-5.5 is not affected by immobilization
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.5
4.5
A8F6K5
-
3
6
-
approx. 50% of maximal activity at pH 6.3, complete loss of activity above pH 7.5
3.5
7
-
less than 50% activity below pH 3.8 and above pH 6.2
4
8
Streptococcus mutans Ingbritt
-
not active below or above
4
8
-
marked decrease of activity above pH 8 and below pH 4
4.5
11.8
-
4C and 24 h
4.5
8
-
activity range of both free and immobilized enzyme
5
5.5
-
strains AB11A and Rt364
5
5.5
-
10 min reaction
5
6.4
A9UKG4
-
5
6.4
A9UKG4
great loss in activity below and above that values, recombinant wild-type dextranase and engineered fusion protein DSXR
5
6.5
-
-
5
6.5
Lactobacillus bifidus
-
-
5
7.5
-
at 37C for 60 min
5
9
-
approx. 50% of maximal activity at pH 5.2 and pH 8.0
5.5
8.3
A9UKG4
70-100% activity at pH 6.0-8.0, 50% activity at pH 5.5 and pH 8.3
6
11
Catenovulum sp.
-
more than 60% of maximum activity
6.5
8
-
dex1 from strain Dex40-8, higher than 80% maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
40
-
dex1 from strain Dex40-8 and dex2 from strain Dex50-2,inactive above 50C
37
-
A9UKG4
assay at
40
45
-
dextranase D2
40
-
Catenovulum sp.
-
-
43.3
54.4
Chaetomium erraticum, Chaetomium gracile
-
-
45
-
-
dex1 from strain Dex50-2
50
-
aerobic bacterium SRI 2140
-
-
50
-
-
dextranase I and II
55
60
A8F6K5
for 15 min incubation
55
-
-
strains SRI2085, SRI2120
55
-
-
dextranase D1
58
-
-
dextranase D4
60
-
-
immobilized enzyme 80C
60
-
aerobic bacterium SRI 2126, Talaromyces funiculosus
-
-
60
-
-
enzyme retains more than 70% maximal activity after incubation at 57C for 9.5 h in the absence of substrate
60
-
-, Q6VUG7
temperature optima of mutants are similar to that of the wild-type
60
-
-
both free and immobilized enzyme
63
-
aerobic bacterium SRI 2125
-
-
65
-
aerobic bacterium SRI 2128, thermophilic bacterium DP17
-
-
70
-
anaerobic thermophilic bacterium AB11A
-
-
additional information
-
-
ranges for both soluble or immobilized enzyme between 30-35C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
-
Catenovulum sp.
-
26.5% residual activity
25
45
-
approx. 50% of maximal activity at 30C, dramatic decrease in activity above 45C
25
60
A9UKG4
over 80% activity retained within the range of 37-50C, 50% of maximal activity at 25C and 60C
28
40
-
marked decrease of activity above 40C and below 28C
30
60
-
approx. 35% of maximal activity at 30C, approx. 10% of maximal activity at 60C
35
50
Catenovulum sp.
-
more than 88% of maximum ativity
40
65
A8F6K5
-
50
60
Chaetomium erraticum
-
non-concentrated dextranase 4
50
75
-
concentrated dextranase 1
55
60
Chaetomium erraticum
-
concentrated dextranase 2
55
60
-
concentrated dextranase 3
55
-
-
35% activity
60
-
-
4% activity
65
-
-
0% activity
additional information
-
-
below 50C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
-
-
isoelectric focusing, isoenzyme 7
3.9
-
-
isoelectric focusing, isoenzyme 6
3.98
-
-
dextranase I
4
-
-
isoelectric focusing, isoenzyme 1
4
-
-
dextranase III
4.12
-
-
dextranase I
4.19
-
-
dextranase II
4.2
-
-
dextranase II
4.2
-
-
isoelectric focusing, isoenzyme 5
4.2
-
A4F2S5, Q1MVS0, -
sequence analysis
4.35
-
-
dextranase II
4.7
-
-
isoelectric focusing, isoenzyme 2
4.75
-
-
dextranase II
4.8
-
-
isoelectric focusing, isoenzyme 4
4.9
-
-
dextranase I
4.9
-
-
isoelectric focusing, isoenzyme 3
4.9
-
-
isoelectric focusing, isoenzyme 1
4.95
-
-
dextranase I
5
-
-
isoelectric focusing, isoenzyme 3
5
-
-
isoelectric focusing, isoenzyme 2
5.2
-
-
2D-PAGE
5.3
-
-
isoelectric focusing, isoenzyme 1
5.6
-
-
dextranase I
5.7
-
-
2D-PAGE
5.8
-
-
dextranase II
5.9
-
-
dextranase III
6.1
-
-
dextranase IV
6.9
7.3
-
dextranase D4
9.1
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
F5BA50
cells are cultivated in brain-heart infusion medium
Manually annotated by BRENDA team
additional information
-
cells are cultivated in brain-heart infusion medium
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Streptococcus mutans Ingbritt
-
recombinant enzyme
Manually annotated by BRENDA team
Streptococcus mutans Ingbritt
-
-
-
Manually annotated by BRENDA team
-
dextranase D1 and D2
-
Manually annotated by BRENDA team
Purpureocillium lilacinum 6R, Thermoanaerobacter sp. AB11Ad, Talaromyces funiculosus NRRL 1768, Streptococcus mutans K1-R, Talaromyces luteus ATCC9644, Thermoanaerobacter sp. Rt364, Lipomyces starkeyi KSM 22, Streptococcus sobrinus 6715
-
-
-
-
Manually annotated by BRENDA team
Pseudomonas sp. UQM 733
-
dextranase D1 and D2
-
-
Manually annotated by BRENDA team
Purpureocillium lilacinum NRRL 895, Prevotella oralis Ig4a, Lipomyces starkeyi IGC 4047, Bacillus circulans MT-G2, Streptococcus sobrinus UAB66, Talaromyces funiculosus 258
-
-
-
-
Manually annotated by BRENDA team
Lactobacillus bifidus, Cellvibrio fulva
-
-
Manually annotated by BRENDA team
Pseudomonas sp. UQM 733
-
dextranase D4
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Penicillium minioluteum
Penicillium minioluteum
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
14000
-
Flavobacterium sp. M-73
-
electrophoretic analysis
23000
-
-
gel filtration
26500
-
-
SDS-PAGE and gel filtration
39000
-
-
gel filtration
44000
-
-
gel filtration
46000
-
-
ultracentrifugal analysis
50100
-
-
dextranase II
55800
-
-
dextranase I
59000
-
-
dextranase I, SDS-PAGE
59000
-
-
SDS-PAGE
60000
-
-
sedimentation equilibrium experiments
60000
-
-
-
64000
-
A8F6K5
SDS-PAGE
65000
-
-
dextranase IV
66000
-
-
enzyme after deglycosylation, SDS-PAGE and Western blot analysis
67200
-
-
calculated from amino acid sequence
67600
-
-
calculated
68000
-
-
gel filtration
68000
-
-
dextranase III
68300
-
-
dex2 gene from strain Dex50-2, calculated from sequence analysis
68600
-
-
dex1 gene from Dex70-1B, calculated from sequence analysis
69000
-
-
SDS-PAGE
69000
-
-
-
69200
-
-
dex1 gene from Dex70-34, calculated from sequence analysis
70000
120000
-
blue dextran in activity gels
70000
-
-
SDS-PAGE and Western blot analysis
71000
-
-
ultracentrifugal analysis
71000
-
-
ultracentrifugal analysis
71000
-
-
CD-II
71000
-
-
dextranase I
71000
-
-
II
71000
-
-
dextranase II
73000
-
-
analyzed by SDS-PAGE, expressed in Pichia pastoris
74000
-
-
dextranase I
76000
-
-
dextranase I
77000
-
-
CD-I
78000
-
Streptococcus mutans Ingbritt
-
SDS-PAGE
79000
-
-
SDS-PAGE
80000
-
-
dextranase II, SDS-PAGE
80000
-
-
SDS-PAGE
80800
-
-
dex1 gene from strain Dex40-8, calculated from sequence analysis
89000
-
-
dextranase II
97000
-
A4F2S5, Q1MVS0, -
SDS-PAGE, dextranase band from whole-cell extract
97000
-
Q54443
strain MT8148, SDS-PAGE
100000
-
-
-
100000
-
P39653
strain 6715DP, SDS-PAGE
100100
-
-
dex1 gene from strain Dex50-2, calculated from sequence analysis
110000
-
-
dextranase III
115000
-
A4F2S5, Q1MVS0, -
SDS-PAGE, dextranase band from whole-cell extract
128100
-
A4F2S5, Q1MVS0, -
sequence analysis
132000
223000
-
SDS-PAGE
143300
-
-
DNA sequence analysis
150000
-
A4F2S5, Q1MVS0, -
SDS-PAGE, dextranase band from whole-cell extract; SDS-PAGE, dextranase band from whole-cell extract
160000
-
-
SDS-PAGE and gel filtration
160000
-
-
dextranase D
170000
-
A4F2S5, Q1MVS0, -
SDS-PAGE, dextranase band from whole-cell extract; SDS-PAGE, dextranase band from whole-cell extract; SDS-PAGE, dextranase band from whole-cell extract
170000
-
-
strain M36, SDS-PAGE
175000
-
-
SDS-PAGE and gel filtration
175000
-
-
dextranase C
180000
-
A4F2S5, Q1MVS0, -
SDS-PAGE, dextranase band from whole-cell extract; SDS-PAGE, dextranase band from whole-cell extract
190000
-
-
strain M36, SDS-PAGE
200000
-
A4F2S5, Q1MVS0, -
SDS-PAGE, dextranase band from whole-cell extract; SDS-PAGE, dextranase band from whole-cell extract
220000
-
P39653
strain 6715DP, SDS-PAGE
240000
-
A9UKG4
dextransucrase-dextranase fusion protein, SDS-PAGE
260000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
1 * 62000, SDS-PAGE
?
P48845
x * 67000, SDS-PAGE
?
-
x * 135000, SDS-PAGE
?
-
x * 130000, SDS-PAGE
?
-
x * 64000, SDS-PAGE
?
-
x * 66200, SDS-PAGE
?
-
x * 110000, SDS-PAGE, isoenzyme 1, x * 76000, SDS-PAGE, isoenzyme 3, x * 89000, SDS-PAGE, isoenzyme 2
?
-
x * 94500, deduced from nucleotide sequence
?
-
x * 97596, deduced from nucleotide sequence
?
-
1 * 66000, SDS-PAGE, 1 * 68000, SDS-PAGE, 1 * 78000, SDS-PAGE
?
A9UKG4
x * 71000, SDS-PAGE, x * 68300, about, sequence calculation
?
F5BA50
x * 94537, sequence calculation, x * 95400, unprocessed recombinant enzyme, SDS-PAGE, x * 89800, processed recombinant enzyme, SDS-PAGE
?
Lipomyces starkeyi NCYC 1436
-
1 * 66000, SDS-PAGE, 1 * 68000, SDS-PAGE, 1 * 78000, SDS-PAGE
-
?
Arthrobacter oxydans DSM20119T
-
x * 71000, SDS-PAGE, x * 68300, about, sequence calculation
-
?
Streptococcus ratti ATCC19645
-
x * 135000, SDS-PAGE, x * 97596, deduced from nucleotide sequence
-
?
-
x * 130000, SDS-PAGE
-
?
Arthrobacter oxydans KQ11
-
x * 66200, SDS-PAGE
-
?
-
x * 94537, sequence calculation, x * 95400, unprocessed recombinant enzyme, SDS-PAGE, x * 89800, processed recombinant enzyme, SDS-PAGE
-
?
Thermoanaerobacter pseudethanolicus ATCC 33223 39E
-
x * 70000, SDS-PAGE
-
dimer
-
2 * 130000, SDS-PAGE
dimer
Streptococcus sobrinus UAB66
-
2 * 130000, SDS-PAGE
-
monomer
Flavobacterium sp. M-73
-
-
monomer
-
1 * 66000
monomer
-
1 * 70000, purified enzyme, SDS-PAGE and Western blot analysis
monomer
Sporothrix schenckii IP29
-
-
-
multimer
Streptococcus sobrinus UAB66
-
-
-
monomer
Lipomyces starkeyi 1390
-
1 * 70000, purified enzyme, SDS-PAGE and Western blot analysis
-
additional information
F5BA50
the enzyme comprises four regions from the N- to C-termini: N-terminal variable region, N-VR, conserved region, CR, glucan-binding site, GBS, and C-terminal variable region, C-VR
additional information
-
the enzyme comprises four regions from the N- to C-termini: N-terminal variable region, N-VR, conserved region, CR, glucan-binding site, GBS, and C-terminal variable region, C-VR
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
Streptococcus mutans Ingbritt
-
-
glycoprotein
-
-
glycoprotein
Talaromyces funiculosus NRRL 1768
-
-
-
glycoprotein
-
10-12% of dextranase mass corresponds to carbohydrate in the form of N-linked oligosaccharide chains
glycoprotein
-
3 potential N-glycosylation sites, differences in glycosylation profiles between native and recombinant dextranase
glycoprotein
P48845
glycosylation sites at N5, N537 and N540
additional information
-
rDEX has 2 disulphide bridges
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of the conserved fragment from residue Gln100 to Ile732, devoid of its N- and C-terminal variable regions, 1.6 A resolution. Structural domain N possesses an immunoglobulin-like beta-sandwich fold, domain A contains the enzyme's catalytic module, comprising a (beta/alpha)8-barrel, and domain C forms a beta-sandwich structure containing two Greek key motifs. In the enzyme-isomaltotriose complex structure, the bound isomaltooligosaccharide with four glucose moieties is observed in the catalytic glycone cleft and considered to be the transglycosylation product of the enzyme, indicating the presence of four subsites in the catalytic cleft. The complexed structure with suicide substrate 4',5'-epoxypentyl-alpha-D-glucopyranoside reveals that the epoxide ring reacts to form a covalent bond with the Asp385 side chain. Asp385 is the catalytic nucleophile and Glu453 is the acid/base of the double displacement mechanism
Q54443, -
crystal structure of apo-Dex49A and Dex49A complexed with product at 1.8 A and 1.65 A, respectively
P48845
crystallization of selenomethionyl-rDEX
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
7.5
-
stable at 22C for 72 h
2.5
6
-
stable at 25C for 72 min
2.5
7
-
below 40C
3.1
8.5
-
70C, stable for 7.4 h
3.5
7
-
at 30C for 24 min
3.5
7
-
stable to 24 h incubation at 30C
4
8.8
-
20% activity, 0% activity at pH 2.5 and 11.0
4.3
10
A8F6K5
stable from pH 4.3-10.0 after incubation at 4C for 20 h, activity drops sharply above pH 10.0 and below pH 4.3
4.5
11.8
-
stable at 4C for 24 h
4.5
4.75
-
half-life at 55C is 18 min
4.5
5.6
-
stable for 2 months
4.5
9
-
stable for 24 h at 30C
4.5
-
A9UKG4
purified enzyme, 3 h, 40% activity remaining
4.8
9
-
at 0-37C for 24 h
4.8
9
-
stable at 0-37C for 24 h
4.9
9
-
at 30C for 24 min
5
7
-
stable at 4C for at least 1 year
5
7.5
-
at 37C for 60 min
5
-
-
18 min half-life at 55C
5
-
-
stable 15 min incubation below 50C
5
-
-
stable during 12 h at 75C
5.5
7.5
-
at 4C for several months
5.5
7.5
-
stable on 60 min incubation at 37C
6
11
Catenovulum sp.
-
-
6
8
A9UKG4
more than 80% activity at pH 6.0-8.0
6
-
A9UKG4
purified enzyme, 3 h, 70% activity remaining
6.5
12
Flavobacterium sp. M-73
-
at 4C for 24 h
7
7.5
A9UKG4
purified enzyme, 3 h, 100% activity
8
-
A9UKG4
purified enzyme, 3 h, 90% activity remaining
9
-
A9UKG4
purified enzyme, 3 h, 60% activity remaining
additional information
-
-
immobilized enzyme is more stable in lower pH (3.5-4.0) and higher pH (6.0-7.5) ranges
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
37
-
stable for 24 h at pH 4.8-9.0
4
-
-
stable for 24 h above pH 6.5-12
28
-
A9UKG4
stable at temperatures below 28C
35
-
-
completely stable at temperatures below 45C
35
-
Flavobacterium sp. M-73
-
; and below for 10 min
35
-
-
stable for 10 min
40
-
-
D4, stable at 40C and less for 1h at pH 5.5
40
-
-
stable 30 min incubation at pH 6.0
40
-
F5BA50
purified recombinant enzymes, stable up to
40
-
A9UKG4
purified enzyme, 3 h, stable below
43
-
-
D2, activity decreases after 1h at pH 5.5
45
-
-
20 min; immobilized enzyme
50
-
-
50C and below
50
-
-
50C and below
50
-
-
1 hr; soluble enzyme
50
-
-
50% loss of activity after 7.6 h
50
-
-
no loss of activity after 60 min
50
-
-
after 48 h at pH 5.0 enzyme retaines 30% activity
50
-
-
stable in solutions at temperatures less than 50C
50
-
-
stable for 60 min at pH below 6.0
51
-
-
dextranase D1, stable for 1 h at pH 5.5
55
-
-
55C and below
55
-
-
rapidly inactivated above
55
-
-
half-live 452 s
55
-
A9UKG4
purified enzyme, 3 h, 80% activity remaining
60
65
A8F6K5
over 75% of the original activity is sustained at 60C for 4 h, the half-life of the enzyme is 1.5 h at 65C with pH4.3 in the absence of added dextran
60
-
-
thermal denaturation
60
-
-
approx. 50% loss of activity
60
-
-
half-live 78 s
60
-
-
half-life of the free enyzme is 331.15 min, and of the immobilized enzyme 431.8 min
60
-
A9UKG4
purified enzyme, 3 h, inactivation
60
-
-
1 h, 60% residual activity
65
-
-
half-live 42 s
70
-
-
half-life of the free enyzme is 49.22 min, and of the immobilized enzyme 70.15 min
75
-
-
half-life is 6.5 h at pH 5.0 in the absence of dextran
75
-
-
half-life is 6.5 h at pH 5.0 in the absence of dextran; stable during 12 h at pH 5.0
75
-
-
1 h, no loss of activity
80
-
-
half-life is 2 h at pH 5.0 in the absence of dextran
80
-
-
half-life of the free enyzme is 4.21 min, and of the immobilized enzyme 30.43 min
additional information
-
-
below 50C stable for 15 min at pH 5.5
additional information
-
-
below 45C stable for 10 min at pH 6.5
additional information
-
-
below 50C stable for 3 min at pH 5.5
additional information
-
-
plateau of tolerance to higher temperatures up to 44C, at higher temperatures rapid decrease of activity
additional information
-
-
immobilized enzyme is more stable at high temperatures
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
non-concentrated dextranase unstable at refridgerator temperatures
Chaetomium erraticum, Chaetomium gracile
-
matrix-bound stable when stored as acetone-dried powder or as a suspension in acetate buffer for about 3 weeks at 4C
-
Ca2+, Mn2+, Fe3+, Ni2+, Co2+, Sr2+, Cu2+, EDTA have no effect to enzyme stability
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acetone
-
stable in acetone
Acetone
Talaromyces funiculosus NRRL 1768
-
stable in acetone
-
Methanol
-
stable in methanol
Methanol
Talaromyces funiculosus NRRL 1768
-
stable in methanol
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
23-27C in the dark
Chaetomium erraticum, Chaetomium gracile
-
non-concentrated dextranase very unstable at storage in a refrigeerator
-
4C, buffer, pH 5-10, several months
-
4C, 2 mM NaN3, 6 months, the purified SmDex90 is proteolytically degraded to more than seven polypeptides of 23-70 kDa during long storage
F5BA50
30C, stable up to 3 days
-
-20C, dextranase II stable for 560 days
-
-20C, acetate buffer pH 5.4, 10% (w/v) sucrose, 10% (v/v) glycerol, no activity loss over 560 days (crude enzyme preparation)
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native enzyme by anion exchange chromatography, recombinant His-tagged enzyme 16fold from Escherichia coli by nickel affinity chromatography
A9UKG4
the dextransucrase-dextranase fusion protein is partially purified by DEAE-Sepharose column chromatography
A9UKG4
-
Flavobacterium sp. M-73
-
17.56fold by cation-exchange chromatography, 18.18fold followed by Ni-affinity chromatography
-
ammonium sulfate, 20% polyethylene glycol 6000, interphase adsorption, DEAE-Sepharose
-
11 isolates at 40 or 50C, 3 isolates purified at 60C
-
isolated from australian sugarcane-mill samples
-
isolated from garden compost
-
N-terminal His-tag purified enzyme
-, Q6VUG7
recombinant form with six histidine residues tagged in the C-terminus partially purified on Ni-NTA column
A4F2S5, Q1MVS0, -
recombinant dextranase
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) CodonPlus-RIL by nickel affinity chromatography, ultrafilatration, and hydrophobic interaction and anion exchange chromatography
F5BA50
-
Streptococcus mutans Ingbritt
-
recombinant dextranse
-
expression in Escherichia coli
-
recombinant and native dextranase
-
recombinant Dex49A
P48845
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene aodex, DNA and amino acid sequence determination and analysis, expression of the His-tagged enzyme in Escherichia coli
A9UKG4
gene dex2, expression of the engineered fusion enzyme DSXR in Escherichia coli strain BL21(DE3)pLysS, optimization of protein expression conditions for enhancement of protein production by the effects of three-level-three-factors and their mutual interaction in Escherichia coli
A9UKG4
the dextransucrase-dextranase fusion protein is expressed in Escherichia coli BL21(DE3) cells
A9UKG4
-
Catenovulum sp.
-
expressed in Pichia pastoris strain GS115
-
into vector pPIC9k-His6 and expressed in Pichia pastoris GS115 strain under the control of AOX1 promoter
-
isoenzyme lsd1, expression in Saccharomyces cerevisiae INVSc1
-
dex1 gene from Dex70-1B and Dex70-34, expression in Escherichia coli TOP10F
-
dex1 gene from strain Dex40-8 and strain Dex50-2, expression in Escherichia coli TOP10F
-
wild-type dex1 gene directly cloned into NotI and XbaI sites of pEH75 and transformed into Escherichia coli Mach1TM-T1 cells. Dex1 coding regions from wild-type and thermostable mutants PCR-amplified from pEH75 and cloned into pET-45b(+) and transformed into Escherichia coli expression host BL21(DE3)
-, Q6VUG7
into vector pET-21a(+), recombinant form with six histidine residues tagged in the C-terminus expressed in Escherichia coli strain BL21(DE3)
A4F2S5, Q1MVS0, -
DNA and amino acid sequence determination and analysis, sequence comparisons, expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) CodonPlus-RIL
F5BA50
expression in Escherichia coli
-
expression in Escherichia coli
Streptococcus mutans Ingbritt
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expressed in Saccharomyces cerevisiae INVSc1 via fusion of the DNA segment encoding the mature dextranase protein with alpha-factor signal sequence, and insertion into the GAL1-controlled expression vector pYES2/CT (construction of the four dextranase-expressing plasmids pYES2/CT-dex, pYES2/CT-dex-tag, pYES2/CT-alphaF-dex(m) and pYES2/CT-alphaF-dex(m)-tag). Dextranase construct pYESCT2-alphaF-dex(m) introduced into a strain of Saccharomyces cerevisiae expressing the human cytochrome P4503A4 (CYP3A4) and the cognate reductase
Q27JJ3
expression in Pichia pastoris
-
expressed in Escherichia coli BL21(DE3) cells
A8F6K5
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression is induced by 1% dextran T2o
Catenovulum sp.
-
expression is induced by 1% dextran T2o
Catenovulum sp. SP03
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D279C/S289C
-
the mutant shows a more than 13C improvement on its optimal temperature compared to the wild type enzyme, the mutant shows a more than 3C improvement on its optimal temperature compared to the wild type enzyme
T245C/N248C
-
the mutant shows a more than 3C improvement on its optimal temperature compared to the wild type enzyme
D1254N
H2EI27
36% of wild-type activity
D189A
H2EI27
application of achemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms small sized dextran from alpha-isomaltotetraosyl fluoride in the presence of NaN3
D340G
H2EI27
application of a chemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms beta-isomaltotetraosyl azide indicating residue D340 as nucleophile catalyst
D1254N
-
36% of wild-type activity
-
D189A
-
application of achemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms small sized dextran from alpha-isomaltotetraosyl fluoride in the presence of NaN3
-
D340G
-
application of a chemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms beta-isomaltotetraosyl azide indicating residue D340 as nucleophile catalyst
-
W793L
A4F2S5, Q1MVS0, -
loss of dextranase activity
W793L
Streptococcus criceti E49
-
loss of dextranase activity
-
D380N
-
similar activity as wild-type
D385E
-
no activity
D385N
-
no activity
D385T
-
no activity
D385V
-
no activity
N5A/N537A/N540A
P48845
glycosylation-free mutant of Dex49A
additional information
A9UKG4
generation of an engineered fusion enzyme of dextransucrase, from dsrBCB4 gene from Leuconostoc mesenteroides B-1299CB4, and Arthrobacter oxydans dextranase, i.e. DSXR. DSXR is potentially useful for reliable production of long isomalto-oligosaccharides from sucrose by a one-step reaction
additional information
-
immobilization of dextranase on several carriers by entrapment and covalent binding with cross-linking. Entrapment in sodium alginate with Ca2+. Dextranase immobilized on bovine serum albumin with a cross-linking agent shows the highest activity and considerable immobilization yield of 66.7%. The optimum pH of the immobilized enzyme is shifted to pH 6.0 as compared to the free enzyme pH 5.5. The optimum temperature of the reaction is at 60C for both free and immobilized enzyme. Thermal and pH stability are significantly improved by the immobilization process. Km of the immobilized dextranase is higher than that of the free dextranase, while Vmax of the immobilized enzyme is lower than that of the free dextranase. The immobilized enzyme is able to retain 76% of the initial catalytic activity after 5.0 cycles
E412Q
H2EI27
application of a chemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms alpha-isomaltotetraosyl azide indicating residue E412 as acid/base catalyst
additional information
-, Q6VUG7
dexI mutants with improved thermostability. In terms of their relative specific activity towards dextran, noticeable differences among mutants showing increased, similar or reduced enzyme activity as compared to wild-type
additional information
H2EI27
a C-terminal truncated enzyme, residues Ala39-Ser1304, has 50% wild-type activity
E412Q
-
application of a chemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms alpha-isomaltotetraosyl azide indicating residue E412 as acid/base catalyst
-
additional information
-
a C-terminal truncated enzyme, residues Ala39-Ser1304, has 50% wild-type activity
-
D453E
A4F2S5, Q1MVS0, -
loss of dextranase activity
additional information
A4F2S5, Q1MVS0, -
deletion mutant of the C-terminal region can hydrolyze blue dextrans. Double mutant W793L and deletion mutant of the C-terminal region has no dextranase activity
D453E
Streptococcus criceti E49
-
loss of dextranase activity
-
additional information
Streptococcus criceti E49
-
deletion mutant of the C-terminal region can hydrolyze blue dextrans. Double mutant W793L and deletion mutant of the C-terminal region has no dextranase activity
-
D389N
-
similar activity as wild-type
additional information
-
loss of activity in N-terminal deletion mutants
additional information
F5BA50
generation of five truncated SmDexs by deleting the N-terminal variable region, the glucan-binding site, or the C-terminal variable region. Two truncation-mutant enzymes devoid of C-terminal variable region or of C-terminal variable region and N-terminal variable region are catalytically active, thereby indicating that the two regions are not essential for the catalytic activity, mutant structures compared to the wild-type enzyme, overview
additional information
-
generation of five truncated SmDexs by deleting the N-terminal variable region, the glucan-binding site, or the C-terminal variable region. Two truncation-mutant enzymes devoid of C-terminal variable region or of C-terminal variable region and N-terminal variable region are catalytically active, thereby indicating that the two regions are not essential for the catalytic activity, mutant structures compared to the wild-type enzyme, overview
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
plays a role in dental caries
nutrition
-
evluation of the storage stability of dextranase by adding enzyme protective reagents, i.e. stabilizers and antiseptics. Best stabilizers of dextranase are glycerol (16%), sodium acetate (18%) and sodium citrate (20%). 4-Hydroxybenzoic acid compound sodium acetate (0.05%), sodium D-isoascorbiate (0.03%), and potassium sorbate (0.05%)are the best antiseptics
nutrition
Arthrobacter oxydans KQ11
-
evluation of the storage stability of dextranase by adding enzyme protective reagents, i.e. stabilizers and antiseptics. Best stabilizers of dextranase are glycerol (16%), sodium acetate (18%) and sodium citrate (20%). 4-Hydroxybenzoic acid compound sodium acetate (0.05%), sodium D-isoascorbiate (0.03%), and potassium sorbate (0.05%)are the best antiseptics
-
medicine
-
isoform Dex410 effectively inhibits the Streptococcus mutans biofilm growth in coverage, biomass, and water-soluble glucan by more than 80, 90, and 95%, respectively. For short-term use of 1.5 months in animal experiment, both Dex410 and the commercial mouthwash Biotene have a significant inhibitory effect on caries, while for 3 months use, only Dex410 shows significant inhibitory effect on dental caries
synthesis
-
maximum enzyme production is obtained in a self designed medium (pH 6.0) containing 1% dextran 5000 Da, after 24 h culture incubation at 37C.High dextranase production is achieved when medium is supplemented with dextran as only carbon source and no enzyme production is found in medium having glucose, sucrose or starch. Dextranase production is inversely proportional to dextran polymer length and extent of branching
synthesis
-
optimized culture conditions for dextranase productions are 37C, pH 10, 32 h, and 20% (v/w) moisture content. The addition of 0.175 mM CrCl3 increases the enzyme production by about 4.5fold
synthesis
Bacillus subtilis NRC-B233b
-
optimized culture conditions for dextranase productions are 37C, pH 10, 32 h, and 20% (v/w) moisture content. The addition of 0.175 mM CrCl3 increases the enzyme production by about 4.5fold
-
synthesis
Catenovulum sp.
-
optimal conditions for synthesis of enzyme are 28 h, 8.0, 30C, and 25% volume of liquid in 100-ml Erlenmeyer flasks, respectively
synthesis
Catenovulum sp. SP03
-
optimal conditions for synthesis of enzyme are 28 h, 8.0, 30C, and 25% volume of liquid in 100-ml Erlenmeyer flasks, respectively
-
agriculture
Chaetomium erraticum, Chaetomium gracile
-
sugar manufacture
food industry
Chaetomium sp.
-
the use of the dextranase enzyme is the most efficient method for hydrolyzing the dextrans at sugar mills
medicine
-
plays a role in dental caries
drug development
-
fractionated dextrans possess commercial interest in cosmetics, drug formulations, vaccines, cryoprotectants
medicine
-
treatment of dental plaque
nutrition
-
sugar industry, stabilizers in food industry
biotechnology
-
bioconversion, modification of alternan
medicine
-
less oxidised dextrans conjugating proportionally less 5-aminosalicylic acid successfully hydrolysed by dextranase, suggest their potential applications for the treatment of Crohns disease in the distal ileum and proximal colon
medicine
Penicillium sp. D5884
-
less oxidised dextrans conjugating proportionally less 5-aminosalicylic acid successfully hydrolysed by dextranase, suggest their potential applications for the treatment of Crohns disease in the distal ileum and proximal colon
-
biotechnology
Penicillium sp. NRRL 21969
-
bioconversion, modification of alternan
-
synthesis
-
investigation on various adding times of dextranase to the dextransucrase system to reveal the synergistic processes of dextransucrase and dextranase. Dextranase added into the dextransucrase-sucrose system at different times gives rise to different main dextran products. Dextranase added into sucrose system at the same time with dextransucrase synthesizes low molecular weight dextran targeted to 5 kDa, while dextranase added during the reaction process of dextransucrase directionally prepares dextran with medium Mw of 10 kDa and 20 kDa. The synthesized oligodextrans are mainly composed of alpha-1,6-glycosidic linkages and low alpha-1,3-glycosidic branches
medicine
-
plays a role in dental caries, partial hydrolysis of native dextran in the preparation of blood substitutes
synthesis
-
manufacture of dentifrices, application in sugar cane mills
synthesis
Purpureocillium lilacinum 6R
-
manufacture of dentifrices, application in sugar cane mills
-
medicine
-
enzyme plays a role in controlling both the adhesive properties of extracellular glucan and the ability to utilize extracellular glucan as a nutrient source
medicine
Streptococcus mutans Ingbritt
-
-
medicine
-
plays a role in dental caries
medicine
Streptococcus sobrinus UAB66
-
plays a role in dental caries
-
medicine
-
present in the biofilm known as dental plaque
synthesis
-
application in sugar cane mills
medicine
-
partial hydrolysis of native dextran in the preparation of blood substitutes
synthesis
-
manufacture of dentifrices
synthesis
-
application in sugar cane mills
medicine
Talaromyces funiculosus 258
-
partial hydrolysis of native dextran in the preparation of blood substitutes
-
synthesis
Talaromyces funiculosus 258
-
manufacture of dentifrices, -, application in sugar cane mills
-