Information on EC 3.2.1.168 - hesperidin 6-O-alpha-L-rhamnosyl-beta-D-glucosidase

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The expected taxonomic range for this enzyme is: Acremonium sp.

EC NUMBER
COMMENTARY
3.2.1.168
-
RECOMMENDED NAME
GeneOntology No.
hesperidin 6-O-alpha-L-rhamnosyl-beta-D-glucosidase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hesperidin + H2O = hesperetin + rutinose
show the reaction diagram
-
-
-
-
hesperidin + H2O = hesperetin + rutinose
show the reaction diagram
diglycosidase activity, transglycosylation and hydrolysis
-
hesperidin + H2O = hesperetin + rutinose
show the reaction diagram
diglycosidase activity, catalyzing the transglycosylation and hydrolysis reactions
-
hesperidin + H2O = hesperetin + rutinose
show the reaction diagram
diglycosidase activity, catalyzing the transglycosylation and hydrolysis reactions; diglycosidase activity, transglycosylation and hydrolysis
Acremonium sp. DSM 24697
-
-
SYSTEMATIC NAME
IUBMB Comments
hesperetin 7-(6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside) 6-O-alpha-rhamnopyranosyl-beta-glucohydrolase
The enzyme exhibits high specificity towards 7-O-linked flavonoid beta-rutinosides.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
alpha-rhamnosyl-beta-glucosidase
-
-
alpha-rhamnosyl-beta-glucosidase
-
a diglycosidase, catalyzing the transglycosylation and hydrolysis reactions
alpha-rhamnosyl-beta-glucosidase
Acremonium sp. DSM 24697
-
a diglycosidase, catalyzing the transglycosylation and hydrolysis reactions
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
enzyme is immobilized onto chitosan beads by adsorption and cross-linking
-
-
Manually annotated by BRENDA team
formerly identified as Stilbella fimetaria, under morphological basis reidentified as Acremonium sp. DSM 24697, i.e. Acremonium sp. SES201
-
-
Manually annotated by BRENDA team
SES201, isolated from South Patagonia, Argentina
-
-
Manually annotated by BRENDA team
Acremonium sp. DSM 24697
-
-
-
Manually annotated by BRENDA team
Acremonium sp. DSM 24697
enzyme is immobilized onto chitosan beads by adsorption and cross-linking
-
-
Manually annotated by BRENDA team
Acremonium sp. DSM 24697
formerly identified as Stilbella fimetaria, under morphological basis reidentified as Acremonium sp. DSM 24697, i.e. Acremonium sp. SES201
-
-
Manually annotated by BRENDA team
Acremonium sp. DSM 24697
SES201, isolated from South Patagonia, Argentina
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-phenethyl rutinoside + H2O
2-phenylethanol + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
Acremonium sp., Acremonium sp. DSM 24697
-
purified aromatic an terpenyl rutinosides are incubated as substrates, no activity in aqueous medium, 3.8% in 12% ethanol
-
-
?
diosmin + H2O
didymin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
Acremonium sp., Acremonium sp. DSM 24697
-
a 7-O-beta-rutinoside, pH 5.0, 60C, 3.3% relative activity compared to hesperidin as substrate
-
-
?
eriocitrin + H2O
eriodictyol + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
-
a 7-O-beta-rutinoside, pH 5.0, 60C, 89.7% relative activity compared to hesperidin as substrate
-
-
?
geranyl rutinoside + H2O
geraniol + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
Acremonium sp., Acremonium sp. DSM 24697
-
purified aromatic an terpenyl rutinosides are incubated as substrates, no activity in aqueous medium, 2.9% in 12% ethanol
-
-
?
hesperidin + H2O
hesperetin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
-
-
-
-
?
hesperidin + H2O
hesperetin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
-
-
i.e. hesperetin + rutinose
-
?
hesperidin + H2O
hesperetin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
-
pH 5.0, 60C
-
-
?
hesperidin + H2O
hesperetin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
-
i.e. hesperitin 7-(6-O-alpha-rhamnopyranosyl)-beta-D-glucopyranoside, pH 5.0, 60C, substrates and products of the enzymatic reaction are analyzed by UV-MALDI-TOF/TOF mass spectrometry
i.e. hesperetin + rutinose, substrates and products of the enzymatic reaction are analyzed by UV-Maldi-TOF/TOF mass spectrometry
-
?
hesperidin + H2O
hesperetin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
-
herperidin occurs in lemons and oranges in high concentrations and contributes to juice clouding. Enzymatic hydrolysis via the diglycosidase is useful to remove the unpleasant taste or for juice clarification, a deglycosylation (hydrolysis and transglycosylation) in a single step
i.e. hesperetin + rutinose
-
?
hesperidin + H2O
hesperetin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
-
purified aromatic and terpenyl rutinosides are incubated as substrates, 14.3% relative activity in aqueous medium, 21.7% in 12% ethanol
i.e. hesperetin + rutinose
-
?
hesperidin + H2O
hesperetin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
Acremonium sp. DSM 24697
-
herperidin occurs in lemons and oranges in high concentrations and contributes to juice clouding. Enzymatic hydrolysis via the diglycosidase is useful to remove the unpleasant taste or for juice clarification, a deglycosylation (hydrolysis and transglycosylation) in a single step
i.e. hesperetin + rutinose
-
?
hesperidin + H2O
hesperetin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
Acremonium sp. DSM 24697
-
-
i.e. hesperetin + rutinose
-
?
hesperidin + H2O
hesperetin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
Acremonium sp. DSM 24697
-
purified aromatic and terpenyl rutinosides are incubated as substrates, 14.3% relative activity in aqueous medium, 21.7% in 12% ethanol
i.e. hesperetin + rutinose
-
?
hesperidin + H2O
hesperetin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
Acremonium sp. DSM 24697
-
pH 5.0, 60C
-
-
?
hesperidin + H2O
hesperetin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
Acremonium sp. DSM 24697
-
i.e. hesperitin 7-(6-O-alpha-rhamnopyranosyl)-beta-D-glucopyranoside, pH 5.0, 60C, substrates and products of the enzymatic reaction are analyzed by UV-MALDI-TOF/TOF mass spectrometry
i.e. hesperetin + rutinose, substrates and products of the enzymatic reaction are analyzed by UV-Maldi-TOF/TOF mass spectrometry
-
?
hesperidin + H2O
hesperetin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
Acremonium sp. DSM 24697
-
-
-
-
?
hesperidin methylchalcone + H2O
hesperetin methylchalcone + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
-
-
-
-
?
hesperidin methylchalcone + H2O
hesperetin methylchalcone + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
-
a 7-O-beta-rutinoside, pH 5.0, 60C, 58.5% relative activity compared to hesperidin as substrate
-
-
?
narirutin + H2O
naringenin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
-
a 7-O-beta-rutinoside, pH 5.0, 60C, 61% relative activity compared to hesperidin as substrate
-
-
?
neryl rutinoside + H2O
nerol + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
Acremonium sp., Acremonium sp. DSM 24697
-
purified aromatic an terpenyl rutinosides are incubated as substrates, no activity in aqueous medium, 2.9% in 12% ethanol
-
-
?
hesperidin methylchalcone + H2O
hesperetin methylchalcone + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
Acremonium sp. DSM 24697
-
-
-
-
?
additional information
?
-
-
in addition, when incubated with 5% (v/v) ethanol as acceptor and hesperidin and hesperidin methylchalcone as sugar donors another glycosylated product is found as a result of a transglycosylation reaction: ethyl rutinoside, indicating that alpha-rhamnosyl-beta-glucosidase is able to transfer disaccharide units to OH-acceptors in an aqueous medium, no dectectable enzyme activity using the 7-O-beta-neohesperidosides: naringin and neohesperidin as substrates, or the 3-O-beta-rutinoside rutin
-
-
-
additional information
?
-
Acremonium sp., Acremonium sp. DSM 24697
-
hydrolysis not detected in aqueous medium without ethanol
-
-
-
additional information
?
-
Acremonium sp. DSM 24697
-
in addition, when incubated with 5% (v/v) ethanol as acceptor and hesperidin and hesperidin methylchalcone as sugar donors another glycosylated product is found as a result of a transglycosylation reaction: ethyl rutinoside, indicating that alpha-rhamnosyl-beta-glucosidase is able to transfer disaccharide units to OH-acceptors in an aqueous medium, no dectectable enzyme activity using the 7-O-beta-neohesperidosides: naringin and neohesperidin as substrates, or the 3-O-beta-rutinoside rutin
-
-
-
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
hesperidin + H2O
hesperetin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
show the reaction diagram
Acremonium sp., Acremonium sp. DSM 24697
-
pH 5.0, 60C
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
reduces the activity in the range of 10-50%
Ca2+
-
reduces the activity in the range of 10-50%
Cu2+
-
deleterious for enzyme activity
EDTA
-
reduces the activity in the range of 10-50%
Fe2+
-
reduces the activity in the range of 10-50%
Hg2+
-
deleterious for enzyme activity
Ni2+
-
reduces the activity in the range of 10-50%
Zn2+
-
reduces the activity in the range of 10-50%
Mg2+
-
reduces the activity in the range of 10-50%
additional information
-
no influence of manganese on the enzyme activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
DMSO
-
hydrolytic activity tested with 1.8 mM hesperidin as substrate. Activity is not modified by addition of 2% (v/v) DMSO, but is significantly diminished when the concentration is increased up to 10% (v/v). Hydrolysis yield is increased upon addition of DMSO, with hesperetin final concentrations in the range of 0.47-0.95 mM after 18 h reaction
DMSO
-
1 h incubation at 60C, no loss of activity at 10% v/v DSMO, 40% loss at 20% v/v DSMO, and no activity at 50% v/v DSMO of the free enzyme. The immobilized enzyme retains 82% of the activity, independently of DSMO concentration after the exposure at high temperature
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.77
-
hesperidin
-
pH 5.0, 60C
1.8
-
hesperidin
-
free enzyme, pH 5.0, 60C
8
-
hesperidin
-
immobilized enzyme, pH 5.0, 60C, the change in the affinity of the enzyme to its substrate compared to the free enzyme is probably caused by structural changes introduced by the immobilization process and by the lower accessibility to the active site
8.7
-
hesperidin methylchalcone
-
free enzyme, pH 5.0, 60C
8.73
-
hesperidin methylchalcone
-
pH 5.0, 60C
38.7
-
hesperidin methylchalcone
-
immobilized enzyme, pH 5.0, 60C, the change in the affinity of the enzyme to its substrate compared to the free enzyme is probably caused by structural changes introduced by the immobilization process and by the lower accessibility to the active site
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
32.4
-
hesperidin
-
pH 5.0, 60C
68.2
-
hesperidin methylchalcone
-
pH 5.0, 60C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
18.3
-
hesperidin
-
pH 5.0, 60C
78254
7.8
-
hesperidin methylchalcone
-
pH 5.0, 60C
293278
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
8
-
pH 4: ca. 70% relative activity, pH 8: ca. 60% relative activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
60
-
-
assay at
70
-
-
also active at 5C, Tm of 74.6C and a calculated activation energy Ea of 183.3 kJ/mol
additional information
-
-
study of the effect of temperature on the leakage of alpha-rhamnosyl-beta-glucosidase immoblized on chitosan-silica-polyethyleneimine beads
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
80
-
40C: ca. 20% relative activity, 80C: ca. 50% relative activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.7
-
-
isoelectric focusing
5.7
-
-
since the isoelectric point of the enzyme is acidic, it is expected to interact with polyethyleneimine under the conditions of the immobilzation procedure
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Acremonium sp. DSM 24697
-
-
-
-
Manually annotated by BRENDA team
Acremonium sp. DSM 24697
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
42220
-
-
mass spectrometry
46000
-
-
SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
-
glycoprotein
Acremonium sp. DSM 24697
-
-
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
74.6
-
-
Tm of 74.6C and a calculated activation energy Ea of 183.3 kJ/mol
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ethanol
-
increasing ethanol concentration 0-20% shows to diminish hesperidin hydrolysis, but total activity, hydrolysis plus transglycosylation activity increases
Ethanol
-
hydrolysis only in the presence of 12% ethanol, no enzyme activity in aqueous medium
Ethanol
Acremonium sp. DSM 24697
-
hydrolysis only in the presence of 12% ethanol, no enzyme activity in aqueous medium; increasing ethanol concentration 0-20% shows to diminish hesperidin hydrolysis, but total activity, hydrolysis plus transglycosylation activity increases
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
8C, immobilized enzyme, retains 100% activity during a long-term storage
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
to homogeneity, fractionation with ammonium sulfate and two chromatographic steps: butyl-agarose and QAE-Sephadex
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
bulk biotransformations, the hydrolytic and transglycosidic activity of alpha-rhamnosyl-beta-glucosidase has potential use for industrial processing of plant-based food and the products of the transglycosylation products could play a role as starting materials for the development of new drugs. The immobilization allows the kinetic control of the process
food industry
-
herperidin occurs in lemons and oranges in high concentrations and contributes to juice clouding. Enzymatic hydrolysis via the diglycosidase is useful to remove the unpleasant taste or for juice clarification, a deglycosylation (hydrolysis and transglycosylation) in a single step
food industry
-
potential use of the enzyme for biotechnoligical applications, e.g. in aroma modulation of fermented foods
biotechnology
Acremonium sp. DSM 24697
-
bulk biotransformations, the hydrolytic and transglycosidic activity of alpha-rhamnosyl-beta-glucosidase has potential use for industrial processing of plant-based food and the products of the transglycosylation products could play a role as starting materials for the development of new drugs. The immobilization allows the kinetic control of the process
-
food industry
Acremonium sp. DSM 24697
-
herperidin occurs in lemons and oranges in high concentrations and contributes to juice clouding. Enzymatic hydrolysis via the diglycosidase is useful to remove the unpleasant taste or for juice clarification, a deglycosylation (hydrolysis and transglycosylation) in a single step; potential use of the enzyme for biotechnoligical applications, e.g. in aroma modulation of fermented foods
-