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EC Tree
IUBMB Comments The enzyme degrades unsaturated oligosaccharides produced by the action of alginate lyases (EC 4.2.2.3 and EC 4.2.2.11) on alginate, by repeatedly removing the unsaturated residue from the non-reducing end until only unsaturated monosaccharides are left. The enzyme catalyses a beta-elimination reaction, generating a new unsaturated non-reducing end after removal of the pre-existing one.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Cleavage of poly(4-deoxy-alpha-L-erythro-hexopyranuronoside) oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends into 4-deoxy-alpha-L-erythro-hex-4-enopyranuronate monosaccharides
Synonyms
oalc6, oalc17, oals17, oligo-alginate lyase,
more
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Alg17C
-
-
Oal
-
Smlt2602
locus name
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Cleavage of poly(4-deoxy-alpha-L-erythro-hexopyranuronoside) oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends into 4-deoxy-alpha-L-erythro-hex-4-enopyranuronate monosaccharides
-
-
-
-
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alginate oligosaccharide 4-deoxy-alpha-L-erythro-hex-4-enopyranuronate-(1?4)-hexananopyranuronate lyase
The enzyme degrades unsaturated oligosaccharides produced by the action of alginate lyases (EC 4.2.2.3 and EC 4.2.2.11) on alginate, by repeatedly removing the unsaturated residue from the non-reducing end until only unsaturated monosaccharides are left. The enzyme catalyses a beta-elimination reaction, generating a new unsaturated non-reducing end after removal of the pre-existing one.
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alginate
unsaturated algino-monosaccharides
alginate + H2O
?
-
enzyme degrades alginate more efficiently than polyM and polyG block into a monomeric sugar acid
-
?
algino-oligosaccharide
unsaturated algino-monosaccharides
-
-
-
-
?
algino-polysaccharide
unsaturated algino-monosaccharides
-
-
-
-
?
oligoalginate
unsaturated monosaccharides
oligoalginate + H2O
4-deoxy-L-erythro-5-hexoseulose uronic acid
poly(alpha-1,4-L-guluronate)
?
-
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid + 4-deoxy-beta-D-erythro-hex-4-enopyranuronic acid
poly(beta-(1,4)glucuronate)
4-deoxy-alpha-L-threo-hex-4-enopyranuronic acid
poly(beta-(1,4)guluronate)
4-deoxy-beta-D-erythro-hex-4-enopyranuronic acid
poly(beta-(1->4)-D-mannuronate)
unsaturated monosaccharides
poly(beta-(1->4)guluronate) + H2O
?
i.e. linear block polymer of alpha-L-guluronic acid
-
-
?
poly(beta-(1->4)mannuronate) + H2O
?
i.e. linear block polymer of beta-D-mannuronic acid
-
-
?
poly(beta-1,4-D-mannuronate)
?
-
-
-
?
additional information
?
-
alginate
unsaturated algino-monosaccharides
-
-
-
?
alginate
unsaturated algino-monosaccharides
-
alginate substrate is almost completely depolymerized into monosaccharides
-
?
alginate
unsaturated algino-monosaccharides
-
alginate substrate is almost completely depolymerized into monosaccharides
-
?
alginate
unsaturated algino-monosaccharides
-
-
-
?
alginate
unsaturated algino-monosaccharides
-
enzyme completely degrades alginate into unsaturated uronate monomer
-
?
alginate
unsaturated algino-monosaccharides
-
-
-
?
alginate
unsaturated algino-monosaccharides
-
enzyme completely degrades alginate into unsaturated uronate monomer
-
?
oligoalginate
unsaturated monosaccharides
-
-
-
?
oligoalginate
unsaturated monosaccharides
-
-
-
?
oligoalginate + H2O
4-deoxy-L-erythro-5-hexoseulose uronic acid
-
-
enzyme preferentially acts on oligoalginates with degrees of polymerization higher than 2 to produce the alginate monomer, 4-deoxy-L-erythro-5-hexoseulose uronic acid
-
?
oligoalginate + H2O
4-deoxy-L-erythro-5-hexoseulose uronic acid
-
-
enzyme preferentially acts on oligoalginates with degrees of polymerization higher than 2 to produce the alginate monomer, 4-deoxy-L-erythro-5-hexoseulose uronic acid
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid
-
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid
-
-
-
?
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid + 4-deoxy-beta-D-erythro-hex-4-enopyranuronic acid
-
-
-
?
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid + 4-deoxy-beta-D-erythro-hex-4-enopyranuronic acid
-
-
-
?
poly(beta-(1,4)glucuronate)
4-deoxy-alpha-L-threo-hex-4-enopyranuronic acid
-
-
-
?
poly(beta-(1,4)glucuronate)
4-deoxy-alpha-L-threo-hex-4-enopyranuronic acid
-
-
-
?
poly(beta-(1,4)guluronate)
4-deoxy-beta-D-erythro-hex-4-enopyranuronic acid
-
-
-
?
poly(beta-(1,4)guluronate)
4-deoxy-beta-D-erythro-hex-4-enopyranuronic acid
-
-
-
?
poly(beta-(1->4)-D-mannuronate)
unsaturated monosaccharides
best substrate
-
-
?
poly(beta-(1->4)-D-mannuronate)
unsaturated monosaccharides
best substrate
-
-
?
additional information
?
-
-
no substrates: alginate, poly(beta-(1->4)-D-mannuronate), poly(alpha-(1->4)-L-guluronate)
-
-
?
additional information
?
-
no substrates: starch, agarose and agar
-
-
?
additional information
?
-
no substrates: starch, agarose and agar
-
-
?
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oligoalginate + H2O
4-deoxy-L-erythro-5-hexoseulose uronic acid
oligoalginate + H2O
4-deoxy-L-erythro-5-hexoseulose uronic acid
-
-
enzyme preferentially acts on oligoalginates with degrees of polymerization higher than 2 to produce the alginate monomer, 4-deoxy-L-erythro-5-hexoseulose uronic acid
-
?
oligoalginate + H2O
4-deoxy-L-erythro-5-hexoseulose uronic acid
-
-
enzyme preferentially acts on oligoalginates with degrees of polymerization higher than 2 to produce the alginate monomer, 4-deoxy-L-erythro-5-hexoseulose uronic acid
-
?
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Fe2+
-
1.4- to 2fold stimulation
K+
1 mM, 115% of initial activity
KCl
1 mM, 120% of initial activity
Mg2+
-
1.4- to 2fold stimulation
Mn2+
-
1.4- to 2fold stimulation
Ca2+
10 mM, 117% of initial activity
Ca2+
10 mM, 127% of initial activity
Ca2+
-
1.4- to 2fold stimulation
Na+
10 mM, 142% of initial activity
Na+
10 mM, 151% of initial activity
NaCl
10 mM, 147% of initial activity, 300 mM, 276% of initial activity
NaCl
1 mM, 115% of initial activity
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Ca2+
1 mM, 80% residual activity
Hg2+
1 mM, no residual activity
K+
1 mM, 72% of initial activity
Mn2+
1 mM, 63% of initial activity; 1 mM, 63% of initial activity
Al3+
1 mM, 35% of initial activity; 1 mM, 62% of initial activity
Al3+
1 mM, 56% residual activity
Cu2+
1 mM, 40% of initial activity; 1 mM, 54% of initial activity
Cu2+
1 mM, 5% residual activity
EDTA
1 mM, 22% of initial activity; 1 mM, 43% of initial activity
EDTA
1 mM, 49% residual activity
Fe3+
1 mM, 24% of initial activity; 1 mM, 36% of initial activity
Fe3+
1 mM, 44% residual activity
Ni2+
1 mM, 57% of initial activity; 1 mM, 66% of initial activity
Ni2+
1 mM, 40% residual activity
SDS
1 mM, 62% of initial activity; 1 mM, 68% of initial activity
SDS
1 mM, 34% residual activity
Zn2+
1 mM, 48% of initial activity; 1 mM, 61% of initial activity
Zn2+
1 mM, 30% residual activity
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dithiothreitol
-
1 mM, 7fold stimulation
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0.41
poly(beta-(1,4)-D-mannuronate)
0.57 - 0.98
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
-
0.57 - 1.4
poly(beta-(1,4)glucuronate)
-
2.22 - 5.99
poly(beta-(1,4)guluronate)
-
additional information
alginate
0.67
alginate
wild-type, pH 8.0, 25°C
1.35
alginate
mutant H208F, pH 8.0, 25°C
0.41
poly(beta-(1,4)-D-mannuronate)
wild-type, pH 8.0, 25°C
0.41
poly(beta-(1,4)-D-mannuronate)
mutant H208F, pH 8.0, 25°C
0.57
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
wild-type, pH 8.0, 25°C
-
0.98
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
mutant H208F, pH 8.0, 25°C
-
0.57
poly(beta-(1,4)glucuronate)
mutant H208F, pH 8.5, 25°C
-
1.4
poly(beta-(1,4)glucuronate)
wild-type, pH 8.5, 25°C
-
2.22
poly(beta-(1,4)guluronate)
mutant H208F, pH 8.0, 25°C
-
5.99
poly(beta-(1,4)guluronate)
wild-type, pH 8.0, 25°C
-
additional information
alginate
Km value 0.79 mg/ml, pH 7.0, 40°C
additional information
alginate
Km value 0.79 mg/ml, pH 7.0, 40°C
additional information
alginate
Km value 0.95 mg/ml, pH 7.0, 40°C
additional information
alginate
Km value 0.95 mg/ml, pH 7.0, 40°C
additional information
oligoalginate
-
the KM and Vmax of Alg17C are 35.2 mg/ml and 41.7 U/mg, respectively, pH 6.0, 40°C
-
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21.3 - 62.2
poly(beta-(1,4)-D-mannuronate)
2 - 22.2
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
-
0.4 - 6.1
poly(beta-(1,4)glucuronate)
-
1.4 - 34.6
poly(beta-(1,4)guluronate)
-
14.6
alginate
mutant H208F, pH 8.0, 25°C
34.8
alginate
wild-type, pH 8.0, 25°C
21.3
poly(beta-(1,4)-D-mannuronate)
mutant H208F, pH 8.0, 25°C
62.2
poly(beta-(1,4)-D-mannuronate)
wild-type, pH 8.0, 25°C
2
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
mutant H208F, pH 8.0, 25°C
-
22.2
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
wild-type, pH 8.0, 25°C
-
0.4
poly(beta-(1,4)glucuronate)
wild-type, pH 8.5, 25°C
-
6.1
poly(beta-(1,4)glucuronate)
mutant H208F, pH 8.5, 25°C
-
1.4
poly(beta-(1,4)guluronate)
mutant H208F, pH 8.0, 25°C
-
34.6
poly(beta-(1,4)guluronate)
wild-type, pH 8.0, 25°C
-
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51.5 - 151.8
poly(beta-(1,4)-D-mannuronate)
2.1 - 38.7
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
-
0.3 - 10.6
poly(beta-(1,4)glucuronate)
-
0.7 - 5.8
poly(beta-(1,4)guluronate)
-
additional information
alginate
10.8
alginate
mutant H208F, pH 8.0, 25°C
52.2
alginate
wild-type, pH 8.0, 25°C
51.5
poly(beta-(1,4)-D-mannuronate)
mutant H208F, pH 8.0, 25°C
151.8
poly(beta-(1,4)-D-mannuronate)
wild-type, pH 8.0, 25°C
2.1
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
mutant H208F, pH 8.0, 25°C
-
38.7
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
wild-type, pH 8.0, 25°C
-
0.3
poly(beta-(1,4)glucuronate)
wild-type, pH 8.5, 25°C
-
10.6
poly(beta-(1,4)glucuronate)
mutant H208F, pH 8.5, 25°C
-
0.7
poly(beta-(1,4)guluronate)
mutant H208F, pH 8.0, 25°C
-
5.8
poly(beta-(1,4)guluronate)
wild-type, pH 8.0, 25°C
-
additional information
alginate
kcat/Km value 114.4 ml/mg/s, pH 7.0, 40°C
additional information
alginate
kcat/Km value 114.4 ml/mg/s, pH 7.0, 40°C
additional information
alginate
kcat/Km value 118.8 ml/mg/s, pH 7.0, 40°C
additional information
alginate
kcat/Km value 118.8 ml/mg/s, pH 7.0, 40°C
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12.6
substrate poly(beta-1,4-D-mannuronate), pH 7.0, 40°C
24
substrate polyM, pH 7.0, 50°C
32
substrate alginate, pH 7.0, 50°C
33.7
substrate alginate, pH 7.0, 40°C
5
substrate polyG, pH 7.0, 50°C
76.8
substrate poly(alpha-1,4-L-guluronate), pH 7.0, 40°C
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37
-
-
40
-
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8.3
calculated from sequence
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UniProt
brenda
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UniProt
brenda
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UniProt
brenda
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-
-
brenda
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-
-
brenda
-
-
-
brenda
-
UniProt
brenda
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UniProt
brenda
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UniProt
brenda
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UniProt
brenda
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-
-
brenda
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UniProt
brenda
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UniProt
brenda
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UniProt
brenda
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-
-
brenda
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physiological function
enzyme degrades both alginate polymers and oligomers into monomers in an exolytic mode. Isoform OalC6 prefers alpha-L-guluronate blocks, while isoform OalC17 prefers poly beta-D-mannuronate blocks. The combination of OalC6 and OalC17 shows synergistic degradation ability toward both alginate polymers and oligomers
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EALGL_SACD2
Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
736
0
81582
Swiss-Prot
-
EALGL_STRMK
Stenotrophomonas maltophilia (strain K279a)
742
0
82406
Swiss-Prot
-
A0A2H5X6K9_9BACT
690
0
77194
TrEMBL
-
A0A2N9DBT1_9XANT
747
0
81339
TrEMBL
-
A0A8F4NUG1_9BACT
747
0
83304
TrEMBL
-
A0A5Q2N1Y4_9FIRM
617
0
71605
TrEMBL
-
A0A4P6ZFL4_9FLAO
752
0
85586
TrEMBL
-
A0A653Z9P7_9BURK
748
0
83329
TrEMBL
-
A0A7G7SM37_9XANT
747
0
81523
TrEMBL
-
A0A654E7V7_9BACT
741
0
83249
TrEMBL
-
A0A644V2N7_9ZZZZ
734
1
83391
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A7J0A0X9_9BACE
735
0
82505
TrEMBL
-
A0A383SR69_XANCJ
747
1
81178
TrEMBL
-
A0A653NLF1_9CAUL
746
1
81162
TrEMBL
-
A0A5S9NJS0_9GAMM
728
0
80536
TrEMBL
-
A0A2Z2NX85_9GAMM
715
0
78853
TrEMBL
-
A0A381LMM3_9XANT
747
0
81240
TrEMBL
-
A0A653P0M5_9FLAO
744
0
84096
TrEMBL
-
A0A7L4ZPJ7_9FLAO
762
0
86086
TrEMBL
-
A0A653JV75_9SPHN
727
0
80254
TrEMBL
-
A0A2H5XCS9_9BACT
707
1
79252
TrEMBL
-
A0A5E7ZQW3_9SPHN
721
0
79675
TrEMBL
-
A0A5J4SY82_9ZZZZ
644
0
73946
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A857JM87_9ALTE
749
0
84032
TrEMBL
-
A0A7G7SZP4_9XANT
747
0
81581
TrEMBL
-
A0A088CA41_9GAMM
763
0
85631
TrEMBL
-
A0A345ANR9_9FLAO
Cellulophaga sp
775
0
85870
TrEMBL
-
A0A345ANS0_9FLAO
Cellulophaga sp
754
0
85724
TrEMBL
-
A9CEJ9_AGRFC
Agrobacterium fabrum (strain C58 / ATCC 33970)
776
0
87871
TrEMBL
other Location (Reliability: 2 )
G1EH67_9SPHN
731
0
79953
TrEMBL
-
T1RPY0_STEMA
742
0
82081
TrEMBL
other Location (Reliability: 2 )
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79000
-
x * 81600, calculated, x * 79000, SDS-PAGE
79900
x * 79900, calculated
81600
-
x * 81600, calculated, x * 79000, SDS-PAGE
82000
x * 82000, SDS-PAGE
85000
-
x * 86543, calculated, x * 85000, SDS-PAGE
86543
-
x * 86543, calculated, x * 85000, SDS-PAGE
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?
x * 85700, calculated from sequence, x * 85000, SDS-PAGE
?
x * 85900, calculated from sequence, x * 85000, SDS-PAGE
?
-
x * 81600, calculated, x * 79000, SDS-PAGE
?
-
x * 81600, calculated, x * 79000, SDS-PAGE
-
?
-
x * 86543, calculated, x * 85000, SDS-PAGE
?
-
x * 79900, calculated
-
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proteolytic modification
sequence contains a putative signal peptide of 44 amino acid residues
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H178A
mutant shows reduced oligoalginate lyase activity
H389A
mutant shows reduced oligoalginate lyase activity
N177A
mutant shows reduced oligoalginate lyase activity
R236A
mutant exhibits endolytic activity. The overexpressed mutant protein (79.6 kDa) is proteolytically cleaved into the N-terminal 32.0-kDa and the C-terminal 47.6-kDa fragments. Both fragments show endolytic lyase activity
Y234F
mutant shows reduced oligoalginate lyase activity
Y426F
mutant shows reduced oligoalginate lyase activity
H178A
-
mutant shows reduced oligoalginate lyase activity
-
N177A
-
mutant shows reduced oligoalginate lyase activity
-
R236A
-
mutant exhibits endolytic activity. The overexpressed mutant protein (79.6 kDa) is proteolytically cleaved into the N-terminal 32.0-kDa and the C-terminal 47.6-kDa fragments. Both fragments show endolytic lyase activity
-
Y234F
-
mutant shows reduced oligoalginate lyase activity
-
Y426F
-
mutant shows reduced oligoalginate lyase activity
-
H208F
in addition to cleaving alginate-based substrates, mutant displays significant exolytic glucuronan activity
N207L
completely inactive
Y264F
completely inactive
Y455F
significantly diminished yet measurable activity toward alginate and M and G blocks
H208F
-
in addition to cleaving alginate-based substrates, mutant displays significant exolytic glucuronan activity
-
N207L
-
completely inactive
-
Y264F
-
completely inactive
-
Y455F
-
significantly diminished yet measurable activity toward alginate and M and G blocks
-
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6 - 8
6 h, 4°C, more than 80% residual activity
748525
6 - 8
6 h, 4°C, more than 85% residual activity
748525
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40
1 h, 55% residual activity
40
1 h, 20% residual activity
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expression in Escherichia coli
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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degradation
combining exotype alginate lyases OalC6 and OalC17 and the endotype alginate lyase AlySY08 enables the production of alginate monomers due to synergistic processes
degradation
enzymatical saccharification of acid pretreated and untreated brown macroalgae, first at pH 7.5, 25°C for 12 h with a blend of recombinant alginate and oligoalginate lyases, then at pH 5.2 using a commercial cellulase cocktail. The use of recombinant alginate lyases and oligoalginate lyases in combination with cellulases increases the release of glucose from untreated seaweed. For saccharification of pretreated algae, only cellulases are needed to achieve high glucose yields
degradation
-
enzymatical saccharification of acid pretreated and untreated brown macroalgae, first at pH 7.5, 25°C for 12 h with a blend of recombinant alginate and oligoalginate lyases, then at pH 5.2 using a commercial cellulase cocktail. The use of recombinant alginate lyases and oligoalginate lyases in combination with cellulases increases the release of glucose from untreated seaweed. For saccharification of pretreated algae, only cellulases are needed to achieve high glucose yields
-
synthesis
saccharification of alginate into alginate monosaccharides. Unsaturated monosaccharides up to 3.3 mg/ml are successfully prepared from 1% (w/v) alginate by using the recombinant oligoalginate lyase of Sphingomonas sp. MJ-3
synthesis
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saccharification of alginate into alginate monosaccharides. Unsaturated monosaccharides up to 3.3 mg/ml are successfully prepared from 1% (w/v) alginate by using the recombinant oligoalginate lyase of Sphingomonas sp. MJ-3
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Hashimoto, W.; Miyake, O.; Momma, K.; Kawai, S.; Murata, K.
Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate
J. Bacteriol.
182
4572-4577
2000
Sphingomonas sp.
brenda
Suzuki, H.; Suzuki, K.; Inoue, A.; Ojima, T.
A novel oligoalginate lyase from abalone, Haliotis discus hannai, that releases disaccharide from alginate polymer in an exolytic manner
Carbohydr. Res.
341
1809-1819
2006
Haliotis discus hannai
brenda
Kim, H.T.; Chung, J.H.; Wang, D.; Lee, J.; Woo, H.C.; Choi, I.G.; Kim, K.H.
Depolymerization of alginate into a monomeric sugar acid using Alg17C, an exo-oligoalginate lyase cloned from Saccharophagus degradans 2-40
Appl. Microbiol. Biotechnol.
93
2233-2239
2012
Saccharophagus degradans, Saccharophagus degradans 2-40 / ATCC 43961
brenda
Wang,L.; Li, S.; Yu, W.; Gong, Q.
Cloning, overexpression and characterization of a new oligoalginate lyase from a marine bacterium, Shewanella sp.
Biotechnol. Lett.
37
665-671
2015
Shewanella sp. (A0A088CA41)
brenda
Ryu, M.; Lee, E.
Saccharification of alginate by using exolytic oligoalginate lyase from marine bacterium Sphingomonas sp. MJ-3
J. Ind. Eng. Chem.
17
853-858
2011
Sphingomonas sp. (G1EH67), Sphingomonas sp. MJ-3 (G1EH67)
-
brenda
Shin, J.W.; Lee, O.K.; Park, H.H.; Kim, H.S.; Lee, E.Y.
Molecular characterization of a novel oligoalginate lyase consisting of AlgL- and heparinase II/III-like domains from Stenotrophomonas maltophilia KJ-2 and its application to alginate saccharification
Korean J. Chem. Engin.
32
917-924
2015
Stenotrophomonas maltophilia (T1RPY0), Stenotrophomonas maltophilia KJ-2 (T1RPY0)
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brenda
Kim, H.S.; Chu, Y.J.; Park, C.-H.; Lee, E.Y.; Kim, H.S.
Site-directed mutagenesis-based functional analysis and characterization of endolytic lyase activity of N- and C-terminal domains of a novel oligoalginate lyase from Sphingomonas sp. MJ-3 possessing exolytic lyase activity in the intact enzyme
Mar. Biotechnol.
17
782-792
2015
Sphingomonas sp. (G1EH67), Sphingomonas sp. MJ-3 (G1EH67)
brenda
Ravanal, M.; Sharma, S.; Gimpel, J.; Reveco-Urzua, F.; Overland, M.; Horn, S.; Lienqueo, M.
The role of alginate lyases in the enzymatic saccharification of brown macroalgae, Macrocystis pyrifera and Saccharina latissima
Algal Res.
26
287-293
2017
Agrobacterium fabrum (A9CEJ9), Agrobacterium fabrum ATCC 33970 (A9CEJ9)
-
brenda
MacDonald, L.C.; Weiler, E.B.; Berger, B.W.
Engineering broad-spectrum digestion of polyuronides from an exolytic polysaccharide lyase
Biotechnol. Biofuels
9
43
2016
Stenotrophomonas maltophilia (B2FSW8), Stenotrophomonas maltophilia K279a (B2FSW8)
brenda
Li, S.; Wang, L.; Chen, X.; Zhao, W.; Sun, M.; Han, Y.
Cloning, expression, and biochemical characterization of two new oligoalginate lyases with synergistic degradation capability
Mar. Biotechnol.
20
75-86
2018
Cellulophaga sp. SY116 (A0A345ANR9), Cellulophaga sp. SY116 (A0A345ANS0)
brenda
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