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Information on EC 3.2.1.75 - glucan endo-1,6-beta-glucosidase
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EC Tree
3.2.1.75 glucan endo-1,6-beta-glucosidaseIUBMB Comments
Acts on lutean, pustulan and 1,6-oligo-beta-D-glucosides.
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Word Map
- 3.2.1.75
- trichoderma
- harzianum
-
mycoparasitic
- beta-1,3-glucanase
-
biocontrol
- gentiobiose
- laminarin
- beta-glucanases
- virens
- neotyphodium
- chitinases
-
wall-degrading
- biotechnology
-
rhizoctonia
- analysis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
beta-1,6-glucanase, bgn16.3, endo-beta-1,6-glucanase, neg-1, gly30b, bt3312, beta-1,6-endoglucanase, acidic beta-1,6-glucanase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acidic beta-1,6-glucanase
beta-(1->6)-glucanase
beta-1,6-glucan 6-glucanohydrolase
-
-
-
-
beta-1,6-glucan hydrolase
-
-
-
-
beta-1,6-glucanase-pustulanase
-
-
-
-
beta-1-6-glucan hydrolase
-
-
-
-
BGN16.3
BT3312
endo-(1-6)-beta-D-glucanase
-
-
-
-
endo-1,6-beta-glucanase
endo-beta-1,6-glucanase
PUL1,6-beta-glucan
Pus30A
endo-1,6-beta-glucanase
-
-
-
-
endo-beta-1,6-glucanase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gentiononaose + 2 H2O = gentiobiose + gentiotriose + gentiotetraose
-
-
-
-
gentiononaose + 2 H2O = gentiobiose + gentiotriose + gentiotetraose
hydrolytic cooperation of both an endo-type and saccharifying-type reaction by a single enzyme, which plays a bifunctional role, leading to complete hydrolysis of the glucan. the enzyme varies its mode of action depending on the chain length derived from the glucan
-
gentiononaose + 2 H2O = gentiobiose + gentiotriose + gentiotetraose
hydrolytic cooperation of both an endo-type and saccharifying-type reaction by a single enzyme, which plays a bifunctional role, leading to complete hydrolysis of the glucan. the enzyme varies its mode of action depending on the chain length derived from the glucan
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
6-beta-D-glucan glucanohydrolase
Acts on lutean, pustulan and 1,6-oligo-beta-D-glucosides.
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CAS REGISTRY NUMBER
COMMENTARY
37278-39-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-(1,6)-glucan + H2O
?
-
highly branched beta-(1,6)-glucan, that contains about 75-80% of linear beta-(1,6)-glucose linked units, preared from yeast cell walls
-
-
?
Eisenia bicyclis laminarin + H2O
?
27% of the activity with pustulan
-
-
?
gentiopentaosylsorbitol + H2O
gentiotetraose + gentiobiose + D-glucose
-
-
-
?
methyl beta-gentiobioside + H2O
methyl beta-D-glucoside + beta-D-glucose
-
low activity
-
-
?
methyl beta-gentiohexaoside + H2O
methyl beta-D-glucoside + 2 beta-D-glucose + gentiobiose
-
the major cleavages occur at bonds 2, 3, and 4 in approximately equal proportion, the nonreducing end glucosyl residues of Gen4-6 beta-OMe are either not or scarcely cleaved by the enzyme
-
-
?
methyl beta-gentiopentaoside + H2O
methyl beta-D-glucoside + 3 beta-D-glucose
-
the major cleavages occur at bonds 2, 3, and 4 in approximately equal proportion
-
-
?
methyl beta-gentiotetraoside + H2O
methyl beta-D-glucoside + 2 beta-D-glucose
-
cleavage at the second (bond 2) and third (bond 3) glucosidic bonds from the methyl group
-
-
?
methyl beta-gentiotrioside + H2O
methyl beta-D-glucoside + gentiobiose
-
the second glucosidic bond (bond 2) from the methyl group is cut preferentially
Glc beta-OMe and Gen2 beta-OMe in the ratio 91:9
-
?
beta-glucan + H2O
glucose + laminari-oligosaccharides + gentio-oligosaccharides
-
yeast glucans
-
?
beta-glucan + H2O
glucose + laminari-oligosaccharides + gentio-oligosaccharides
-
yeast glucans
-
-
?
beta-glucan + H2O
glucose + laminari-oligosaccharides + gentio-oligosaccharides
-
yeast glucans
-
-
?
beta-glucan + H2O
glucose + laminari-oligosaccharides + gentio-oligosaccharides
-
Neurospora crassa cell wall beta-glucan
-
-
?
beta-glucan + H2O
glucose + laminari-oligosaccharides + gentio-oligosaccharides
-
yeast glucans
-
-
?
beta-glucan + H2O
glucose + laminari-oligosaccharides + gentio-oligosaccharides
Niallia circulans WL-12
-
yeast glucans
-
-
?
beta-glucan + H2O
glucose + laminari-oligosaccharides + gentio-oligosaccharides
-
Ecklonia radiata glucan, poor substrate
-
-
?
beta-glucan + H2O
glucose + laminari-oligosaccharides + gentio-oligosaccharides
-
Ecklonia radiata glucan, poor substrate
-
-
?
beta-glucan + H2O
glucose + laminari-oligosaccharides + gentio-oligosaccharides
-
yeast glucans
-
-
?
beta-glucan + H2O
glucose + laminari-oligosaccharides + gentio-oligosaccharides
-
Saccharomyces cerevisiae glucan
-
-
?
beta-glucan + H2O
glucose + laminari-oligosaccharides + gentio-oligosaccharides
-
Saccharomyces cerevisiae glucan
-
-
?
gentiohexaose + H2O
gentiobiose + gentiotriose + gentiotetraose
-
-
-
?
gentiopentaose + H2O
D-glucose + gentiotetraose + gentiotriose + gentiobiose
-
reduced
-
?
gentiopentaose + H2O
D-glucose + gentiotetraose + gentiotriose + gentiobiose
-
-
-
-
?
gentiopentaose + H2O
D-glucose + gentiotetraose + gentiotriose + gentiobiose
-
-
gentiobiose and gentiotriose only
?
gentiopentaose + H2O
D-glucose + gentiotetraose + gentiotriose + gentiobiose
-
-
gentiobiose and gentiotriose only
?
gentiotetraose + H2O
D-glucose + gentiotriose + gentiobiose
-
reduced
-
?
gentiotetraose + H2O
D-glucose + gentiotriose + gentiobiose
-
-
gentiobiose only
?
gentiotetraose + H2O
D-glucose + gentiotriose + gentiobiose
-
-
gentiobiose only
?
glucan + H2O
?
-
substrate from yeast, 18% of maximal activity
-
-
?
laminarin + H2O
D-glucose + ?
3% activity compared to pustulan
the main product is D-glucose
-
?
laminarin + H2O
D-glucose + ?
3% activity compared to pustulan
the main product is D-glucose
-
?
laminarin + H2O
gentobiose + D-glucose
22.4% activity compared to pustulan
-
-
?
luteose + H2O
gentiobiose + gentiotriose + gentiotetraose
-
-
-
?
p-nitrophenyl-beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
Flavobacterium M64
-
-
-
?
p-nitrophenyl-beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
pustulan + H2O
?
high substrate specificity, 100% activity
-
-
?
pustulan + H2O
?
-
the enzyme completely hydrolyzes pustulan in three steps: in the initial stage, the enzyme quickly cleaves the glucan with a pattern resembling an endo-hydrolase to produce a short-chain glucan (degree of polymerization DP 45) as an intermediate. In the midterm stage, the resulting short-chain glucan is further cleaved into two fractions corresponding to DP 15-7 and DP 2-4 with great regularity. In the final stage, the lower oligomers corresponding to DP 3 and DP 4 are very slowly hydrolyzed into glucose and gentiobiose
-
-
?
pustulan + H2O
?
-
the enzyme completely hydrolyzes pustulan in three steps: in the initial stage, the enzyme quickly cleaves the glucan with a pattern resembling an endo-hydrolase to produce a short-chain glucan (degree of polymerization DP 45) as an intermediate. In the midterm stage, the resulting short-chain glucan is further cleaved into two fractions corresponding to DP 15-7 and DP 2-4 with great regularity. In the final stage, the lower oligomers corresponding to DP 3 and DP 4 are very slowly hydrolyzed into glucose and gentiobiose
-
-
?
pustulan + H2O
gentobiose + D-glucose
highly specific substrate
-
-
?
pustulan + H2O
gentobiose + D-glucose
highly specific substrate
-
-
?
pustulan + H2O
glucose + gentiobiose
-
-
glucose and oligosaccharides
?
pustulan + H2O
glucose + gentiobiose
-
-
glucose, gentiobiose and gentiotriose
?
pustulan + H2O
glucose + gentiobiose
-
-
also gentiopentaose, gentiotetraose and gentiotriose
?
pustulan + H2O
glucose + gentiobiose
Niallia circulans WL-12
-
-
also gentiopentaose, gentiotetraose and gentiotriose
?
pustulan + H2O
glucose + gentiobiose
-
-
gentiotetraose and longer chains, gentiotriose, gentiotriose and glucose
?
pustulan + H2O
glucose + gentiobiose
-
-
glucose, gentiotetraose, gentiobiose
?
pustulan + H2O
glucose + gentiobiose
-
-
glucose, gentiotetraose, gentiobiose
?
pustulan + H2O
oligomers of pustulan
-
best substrate
product analysis, most abundant products are di-, tri-, and tetra-beta-1,6-glucosides
-
?
pustulan + H2O
oligomers of pustulan
-
best substrate
product analysis, most abundant products are di-, tri-, and tetra-beta-1,6-glucosides
-
?
starch + H2O
?
-
soluble, from corn, from potato, from wheat
-
-
?
starch + H2O
?
-
soluble, from corn, from potato, from wheat
-
-
?
additional information
?
-
-
is active on Candida albicans cell walls, is able to release a GPI-anchored cell wall protein linked to the beta-1,6-glucan polymer through a remnant of its anchor. No activity with beta-1,3-glucan, dextran and amylose
-
-
?
additional information
?
-
the enzyme shows no activity on gentiobiose, 1,3-beta-glucan, 1,4-beta-glucan, or 1,6-beta-galactan
-
-
?
additional information
?
-
-
the enzyme shows no activity on gentiobiose, 1,3-beta-glucan, 1,4-beta-glucan, or 1,6-beta-galactan
-
-
?
additional information
?
-
the enzyme shows no activity on gentiobiose, 1,3-beta-glucan, 1,4-beta-glucan, or 1,6-beta-galactan
-
-
?
additional information
?
-
no activity is detected when gentiobiose, lentinan, laminarioligosaccharides, pachyman, CM-pachyman, and lichenan are used as substrates
-
-
?
additional information
?
-
the purified endo-beta-1,6-glucanase Pus30A catalyzes depolymerization of beta-1,6-glucan endolytically and is highly specific toward beta-1,6-glucan polysaccharide. Pus30A shows hydrolyzing activity against the cell wall components of Lentinula edodes fruiting bodies (54.5% activity compared to pustulan)
-
-
?
additional information
?
-
no activity is detected when gentiobiose, lentinan, laminarioligosaccharides, pachyman, CM-pachyman, and lichenan are used as substrates
-
-
?
additional information
?
-
the purified endo-beta-1,6-glucanase Pus30A catalyzes depolymerization of beta-1,6-glucan endolytically and is highly specific toward beta-1,6-glucan polysaccharide. Pus30A shows hydrolyzing activity against the cell wall components of Lentinula edodes fruiting bodies (54.5% activity compared to pustulan)
-
-
?
additional information
?
-
-
the enzyme is a specific beta-(1->6)-glucanase, it shows no activity with soluble starch, carboxymethyl cellulose, curdlan from Alcaligenes faecalis, and 4-nitrophenyl beta-gentiobioside, it shows poor activity with yeast glucan and 4-nitrophenyl beta-gentiotrioside. The cleavage point of 4-nitrophenyl oligosacchride derivatives with DP 4 or higher shifts such that the enzyme keeps away from the 4-nitrophenyl group at the terminus, in all the tested substrates, release of 4-nitrophenol is not observed. Gentiooligosaccharides (DP 3-9) are prepared from the starting substance gentiobiose by the sequential transglycosylation reactions of beta-glucosidase and beta-(1->6)-glucanase
-
-
?
additional information
?
-
-
the enzyme is a specific beta-(1->6)-glucanase, it shows no activity with soluble starch, carboxymethyl cellulose, curdlan from Alcaligenes faecalis, and 4-nitrophenyl beta-gentiobioside, it shows poor activity with yeast glucan and 4-nitrophenyl beta-gentiotrioside. The cleavage point of 4-nitrophenyl oligosacchride derivatives with DP 4 or higher shifts such that the enzyme keeps away from the 4-nitrophenyl group at the terminus, in all the tested substrates, release of 4-nitrophenol is not observed. Gentiooligosaccharides (DP 3-9) are prepared from the starting substance gentiobiose by the sequential transglycosylation reactions of beta-glucosidase and beta-(1->6)-glucanase
-
-
?
additional information
?
-
no activity with curdlan, barley beta-glucan, xylan and carboxymethyl cellulose
-
-
?
additional information
?
-
-
no activity with curdlan, barley beta-glucan, xylan and carboxymethyl cellulose
-
-
?
additional information
?
-
-
little activity against beta-(1-3)- or beta-(1-4)-linkages
-
-
?
additional information
?
-
-
BGN16.3 is part of the extracellular beta-1,6-glucanase multienzyme complex, regulation of enzyme expression, overview
-
-
?
additional information
?
-
-
substrate specificity, BGN16.3 shows endohydrolytic activity against substrates with beta-1,6-glycosidic linkages, no activity with colloidal chitin, pachyman, starch, cellulose, nigeran, and dextran, no activity with the beta-1,6-disaccharide gentiobiose
-
-
?
additional information
?
-
-
no activity with laminarin, chitin, and mannan
-
-
?
additional information
?
-
-
BGN16.3 is part of the extracellular beta-1,6-glucanase multienzyme complex, regulation of enzyme expression, overview
-
-
?
additional information
?
-
-
substrate specificity, BGN16.3 shows endohydrolytic activity against substrates with beta-1,6-glycosidic linkages, no activity with colloidal chitin, pachyman, starch, cellulose, nigeran, and dextran, no activity with the beta-1,6-disaccharide gentiobiose
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
BGN16.3 is part of the extracellular beta-1,6-glucanase multienzyme complex, regulation of enzyme expression, overview
-
-
?
additional information
?
-
-
BGN16.3 is part of the extracellular beta-1,6-glucanase multienzyme complex, regulation of enzyme expression, overview
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
ethanol extracts of various marine invertebrates: Geodinella spherastrosa, Spirastrella digitata, Spirastrella vagabunda, Chondrilla australiensis, Phakelia cardius, Desmoxya lunata, Mycale monanchorata, Clathria frondifera, Clathria lendenfeldi, Iotrochota baculifera, Phorbas sp., Callyspongia diffusa, Callyspongia sp., Callyspongia subarmigera, Arenosclera sp., Amphimedon sp., Oceanapia imperfecta, Sigmadocia symbiotica, Dysidera herbacea, Dysidea fragilis, Thorecta cacos, Ircinia sp.
-
additional information
-
no inhibitory: D-glucono-1,5-lactone at 1-20 mM
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
BGN16.3 is induced rapidly and strongly by fungal cell walls
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Investigating the role of a Verticillium fungicola beta-1,6-glucanase during infection of Agaricus bisporus using targeted gene disruption.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0753
pustulan
-
assumed molecular weight for pustulan 17000 Da, or KM of 1.28 mg/ml
-
additional information
additional information
-
pustulan 0.4-1.3 mg/ml
-
additional information
additional information
-
lutean 1.38 mg/ml, laminarin 1.67 mg/ml
-
additional information
additional information
-
pustulan 2.78 mg/ml
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
224.7 U/mg, one U being 1 mg of liberated reducing sugar from pustulan after 2 h incubation
additional information
-
34.3 reducing sugars corresponding to 4.43 micro mol of glucose/min/mg
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
5 - 5.5
5.5
6.5
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 7
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
50
50 - 60
55
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
growth medium with lyophilized cells of Candida utilis as mian nutrient source
-
-
brenda
IMI 383068, growth on scleroglucan or pustulan as sole carbon source
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
expression profile of BGN16.3, regulation of BGN16.3 expression
brenda
additional information
-
expression profile of BGN16.3, regulation of BGN16.3 expression
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
secretion of the beta-1,6-glucanase multienzyme complex, BGN16.3 is part of the complex
-
brenda
-
secretion of the beta-1,6-glucanase multienzyme complex, BGN16.3 is part of the complex
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
endo-beta-1,6-glucanase Pus30A is responsible for the degradation of the cell wall components during fruiting body autolysis after harvest
physiological function
-
endo-beta-1,6-glucanase Pus30A is responsible for the degradation of the cell wall components during fruiting body autolysis after harvest
-
additional information
-
the hydrolytic cooperation of both an endo-type and saccharifying-type reaction by a single enzyme, which plays a bifunctional role, leads to complete hydrolysis of the glucan. Thus, beta-(1->6)-glucanase varies its mode of action depending on the chain length derived from the glucan
additional information
-
the hydrolytic cooperation of both an endo-type and saccharifying-type reaction by a single enzyme, which plays a bifunctional role, leads to complete hydrolysis of the glucan. Thus, beta-(1->6)-glucanase varies its mode of action depending on the chain length derived from the glucan
-
Show AA Sequence and Transmembrane Helices (103 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43000
50000
51000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer or dimer
additional information
additional information
-
BGN16.3 is part of the extracellular beta-1,6-glucanase multienzyme complex
additional information
-
BGN16.3 is part of the extracellular beta-1,6-glucanase multienzyme complex
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme or in complex with beta-glucosyl-1,6-deoxynojirimycin, hanging drop vapor diffusion method, using 0.2 M sodium bromide, 0.1 M Bis-Tris propane, pH 6.5, 20% w/v PEG 3350 or 0.2 M potassium thiocyanate 20% w/v PEG 3350, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C393S
the mutant shows 0.005% activity compared to the wild type enzyme
C396S
the mutant shows 0.03% activity compared to the wild type enzyme
D286A
the mutant shows 0.27% activity compared to the wild type enzyme
H281A
the mutant shows 0.006% activity compared to the wild type enzyme
N282A
the mutant shows 0.009% activity compared to the wild type enzyme
W345A
the mutant shows 0.004% activity compared to the wild type enzyme
C393S
-
the mutant shows 0.005% activity compared to the wild type enzyme
-
D286A
-
the mutant shows 0.27% activity compared to the wild type enzyme
-
H281A
-
the mutant shows 0.006% activity compared to the wild type enzyme
-
N282A
-
the mutant shows 0.009% activity compared to the wild type enzyme
-
food industry
the enzyme can be used to hydrolyze beta-1,6-glucans of brown algae or fungal cell walls for producing gentiobiose as a high-value sugar and glucose as a fermentable sugar
additional information
additional information
gene disruption mutant, shows reduced virulence against Agaricus bisporus and diminished ability to use chitin as a carbon source
additional information
-
gene disruption mutant, shows reduced virulence against Agaricus bisporus and diminished ability to use chitin as a carbon source
additional information
the 1,6-beta-D-glucanase gene (Neg1) is disrupted by repeat-induced point mutations. 9 nucleotides within the coding region of the gene change from GC to AT. No apparent phenotypic changes are observed in the mutant, but Congo-red, SDS, and cetyltrimethyl ammonium bromide, which affect fungal cell walls or membranes, markedly inhibit the hyphal growth of the mutant at a concentration that does not inhibi growth of the wild-type
additional information
-
the 1,6-beta-D-glucanase gene (Neg1) is disrupted by repeat-induced point mutations. 9 nucleotides within the coding region of the gene change from GC to AT. No apparent phenotypic changes are observed in the mutant, but Congo-red, SDS, and cetyltrimethyl ammonium bromide, which affect fungal cell walls or membranes, markedly inhibit the hyphal growth of the mutant at a concentration that does not inhibi growth of the wild-type
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 9
-
purified native enzyme, 4°C, 24 h, over 90% activity remaining
731583
4 - 6
4 - 8
the enzyme is stable over a broad pH range from pH 4.0 to 8.0 when treated at 4°C for 20 h
713912
5 - 8
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
the enzyme remains stable from 20-40°C for 30 min. At 50°C and above, the enzyme activity drops to 20% after 30 min incubation
50
60
70
60
the enzyme is completely inactivated after incubation at 60°C for 30 min
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 4 months, no loss of activity, -70°C, 12 months, no loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Sepharose Q column chromatography, Superdex 75 gel filtration, and DEAE-Toyopearly column chromatography
native enzyme 244.3fold from culture supernatant by ammonium sulfate fractionation, cation exchange and affinity chromatography using gentiotetraose as ligand
-
native extracellular BGN16.3 26fold to homogeneity by beta-1,6-glycan affinity chromatography, chromatofocusing, and gel filtration
-
Talon Co2+ affinity column chromatography and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
functional expression from yeast expression vector pYESH2 in Saccharomyces cerevisiae strain INVSc1. The recombinant enzyme does not show antifungal activity in yeast
-
into expression/secretion vector pINA1296+FLAG, expressed in Yarrowia lipolytica strain Po1g: MatA, leu2-270, ura3-302::pBR322-URA3, xpr2-322, axp-2, which contains an integrated pBR322 plasmid as a docking platform
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is up-regulated by 1,6-beta-glucan
the transcript level of endo-beta-1,6-glucanase Pus30A gene (lepus30a) is significantly increased in fruiting bodies 4 days after harvesting (approximately 18times in gills, 27times in stipes, and 32times in pilei) compared to fresh fruiting bodies
the transcript level of endo-beta-1,6-glucanase Pus30A gene (lepus30a) is significantly increased in fruiting bodies 4 days after harvesting (approximately 18times in gills, 27times in stipes, and 32times in pilei) compared to fresh fruiting bodies
the transcript level of endo-beta-1,6-glucanase Pus30A gene (lepus30a) is significantly increased in fruiting bodies 4 days after harvesting (approximately 18times in gills, 27times in stipes, and 32times in pilei) compared to fresh fruiting bodies
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the enzyme is used for analysis of yeast polysaccharides cell wall composition in a method combines acid and enzymatic hydrolysis, and involves a chitinase from Streptomyces griseus, an endo/exo-beta-(1,3)-glucanase from Trichoderma species, recombinant endo-beta-(1,6)-glucanase from Trichoderma harzianum, and a beta-glucosidase from Aspergillus niger, method development and evaluation, overview
biotechnology
biotechnology
-
maximal overproduction of enzyme is achieved in buffered medium where pH-induced aspartyl proteases are absent or when nitrogen sources such as yeast extract are substrate for these proteases
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hiura, N.; Nakajima, T.; Matsuda, K.
Purification and some properties of an endo-beta-1,6-glucanase from Neurospora crassa
Agric. Biol. Chem.
51
3315-3321
1987
Neurospora crassa, Neurospora crassa IFO-6068
-
brenda
Dubourdieu, D.; Desplanques, C.; Villettaz, J.C.; Ribereau-Gayon, P.
Investigations of an industrial beta-D-glucanase from Trichoderma harzianum
Carbohydr. Res.
144
277-287
1985
Trichoderma harzianum
-
brenda
Rudakova, V.Y.; Shevchenko, N.M.; Elyakova, L.A.
Isolation and some properties of endo-beta-1,6-glucanase from marine bivalve Chlamys abbidus
Comp. Biochem. Physiol. B
81
677-682
1985
Chlamys albidus
-
brenda
Schep, G.P.; Shepherd, M.G.; Sullivan, P.
Purification and properties of a beta-1,6-glucanase from Penicillium brefeldianum
Biochem. J.
223
707-714
1984
Penicillium brefeldianum, Penicillium brefeldianum QM 1873
brenda
Abe, J.; Amemura, A.; Harada, T.
An endo-(1-6)-beta-D-glucanase of Flavobacterium M64 hydrolyzing the octasaccharide repeating unit of succinoglycan to two tetrasaccharides
Agric. Biol. Chem.
44
1877-1884
1980
Flavobacterium M64
-
brenda
Katohda, S.; Suzuki, F.; Katsuki, S.; Sato, T.
Purification and some properties of endo-beta-1,6-glucanase from Acinetobacter sp.
Agric. Biol. Chem.
43
2029-2034
1979
Acinetobacter sp.
-
brenda
Del Rey, F.; Garcia-Acha, I.; Nombela, C.
The regulation of beta-glucanase synthesis in fungi and yeast
J. Gen. Microbiol.
110
83-89
1979
Saccharomyces cerevisiae, Neurospora crassa, Trichoderma viride
-
brenda
Miyazaki, T.; Oikawa, N.
An endo-(1-6)-beta-D-glucanase from Mucor hiemalis
Carbohydr. Res.
48
209-216
1976
Mucor hiemalis
brenda
Rombouts, F.M.; Phaff, H.J.
Lysis of yeast cell walls. Lytic beta-(1-6)-glucanase from Bacillus circulans WL-12
Eur. J. Biochem.
63
109-120
1976
Niallia circulans, Niallia circulans WL-12
brenda
Fleet, G.H.; Phaff, H.J.
Lysis of yeast cell walls: glucanases from Bacillus circulans WL-12
J. Bacteriol.
119
207-219
1974
Niallia circulans, Niallia circulans WL-12
brenda
Yamamoto, S.; Kobayashi, R.; Nagasaki, S.
Purification and properties of an endo beta-1,6-glucanase from Rhizopus chinensis R-69
Agric. Biol. Chem.
38
1493-1500
1974
Rhizopus microsporus var. chinensis, Rhizopus microsporus var. chinensis R-69
-
brenda
Shibata, Y.
Enzymatic hydrolysis of glucans containing beta-1,3- and beta-1,6-linkages. III. Gibberella beta-1,6-glucan 6-glucanohydrolase operative in the selective hydrolysis of beta-1,3-glucosidic linkages in Eisenia laminaran
J. Biochem.
75
85-92
1974
Fusarium fujikuroi
brenda
Shibata, Y.; Fukimbara, T.
A beta-1,6-glucan 6-glucanohydrolase from Gibberella fujikuroi
J. Ferment. Technol.
51
216-226
1973
Fusarium fujikuroi
-
brenda
Reese, E.T.; Parrish, F.W.; Mandels, M.
beta-D-1,6-Glucanases in fungi
Can. J. Microbiol.
8
327-329
1962
Aspergillus sp., Beauveria bassiana, Phanerodontia chrysosporium, Penicillium sp., Fusarium sambucinum, Wolfiporia cocos, Trichoderma viride
brenda
Shibata, Y.; Fukimbara, T.
Enzymic hydrolysis of glucans containing beta-1,3-and beta-1,6-linkages: (I) beta-1,6-glucan hydrolase of fungi
J. Ferment. Technol.
50
388-396
1972
Aspergillus niger, Aspergillus phoenicis, Aspergillus usamii, Fusarium oxysporum, Fusarium fujikuroi, Helminthosporium sesanum, Alternaria bataticola
-
brenda
Pitson, S.M.; Seviour, R.J.; McDougall, B.M.; Stone, B.A.; Sadek, M.
Purification and characterization of an extracellular (1,6)-beta-glucanase from the filamentous fungus Acremonium persicinum
Biochem. J.
316
841-846
1996
Acremonium persicinum
brenda
Soler, A.; de la Cruz, J.; Llobell, A.
Detection of beta-1,6-glucanase isozymes from Trichoderma strains in sodium dodecyl sulphate-polyacrylamide gel electrophoresis and isoelectrofocusing gels
J. Microbiol. Methods
35
245-251
1999
Trichoderma harzianum, Trichoderma sp.
brenda
Zvyagintseva, T.N.; Elyakova, L.A.; Krasohin, V.B.
The search for effectors of beta-D-glucanases among marine invertebrates
Comp. Biochem. Physiol. B
102
187-191
1992
Chlamys albidus
brenda
Lora, J.M.; de la Cruz, J.; Llobell, A.; Benitez, T.; Pintor-Toro, J.A.
Molecular characterization and heterologous expression of an endo-beta-1,6-glucanase gene from the mycoparasitic fungus Trichoderma harzianum
Mol. Gen. Genet.
247
639-645
1995
Trichoderma harzianum
brenda
De la Cruz, J.; Llobell, A.
Purification and properties of a basic endo-beta-1,6-glucanase (BGN16.1) from the antagonistic fungus Trichoderma harzianum
Eur. J. Biochem.
265
245-151
1999
Trichoderma harzianum, Trichoderma harzianum CECT 2313
brenda
Mulenga, D.K.; Berry, D.R.
Isolation and characterization of a uniqe endo-beta-1,6-glucanase from the yeast Saccharomycopsis fibuligera NCYC 451
Microbios
80
143-154
1994
Saccharomycopsis fibuligera, Saccharomycopsis fibuligera NCYC 451
brenda
Bom, I.J.; Dielbandhoesing, S.K.; Harvey, K.N.; Oomes, S.J.C.M.; Klis, F.M.; Brul, S.
A new tool for studying the molecular architecture of the fungal cell wall: one-step purification of recombinant Trichoderma beta-(1-6)-glucanase expressed in Pichia pastoris
Biochim. Biophys. Acta
1425
419-424
1998
Trichoderma harzianum
brenda
Fayad, K.P.; Simao-Beaunoir, A.M.; Gauthier, A.; Leclerc, C.; Mamady, H.; Beaulieu, C.; Brzezinski, R.
Purification and properties of a beta-1,6-glucanase from Streptomyces sp. EF-14, an actinomycete antagonistic to Phytophthora spp
Appl. Microbiol. Biotechnol.
57
117-123
2001
Streptomyces sp. EF-14
brenda
Delgado-Jarana, J.; Pintor-Toro, J.A.; Benitez, T.
Overproduction of beta-1,6-glucanase in Trichoderma harzianum is controlled by extracellular acidic proteases and pH
Biochim. Biophys. Acta
1481
289-296
2000
Trichoderma harzianum
brenda
Wu, H.; Shimoi, H.; Ito, K.
Purification and characterization of beta-1,6-glucanase of Streptomyces rochei application in the study of yeast cell wall proteins
Biosci. Biotechnol. Biochem.
66
2515-2519
2002
Streptomyces rochei
brenda
Jayus; McDougall, B.M.; Seviour, R.J.
Purification and properties of a (1-6)-beta-glucanase from Acremonium sp. IMI 383068
Enzyme Microb. Technol.
29
194-200
2001
Acremonium sp. (P82288)
brenda
Jayus; McDougall, B.M.; Seviour, R.J.
Factors affecting the synthesis of (1-3) and (1-6)-beta-glucanases by the fungus Acremonium sp. IMI 383068 grown in batch culture
Enzyme Microb. Technol.
31
289-299
2002
Acremonium sp.
-
brenda
Amey, R.C.; Mills, P.R.; Bailey, A.; Foster, G.D.
Investigating the role of a Verticillium fungicola beta-1,6-glucanase during infection of Agaricus bisporus using targeted gene disruption
Fungal Genet. Biol.
39
264-275
2003
Lecanicillium fungicola (Q7ZA48), Lecanicillium fungicola
brenda
Moy, M.; Li, H.M.; Sullivan, R.; White, J.F., Jr.; Belanger, F.C.
Endophytic fungal beta-1,6-glucanase expression in the infected host grass
Plant Physiol.
130
1298-1308
2002
Neotyphodium sp. (Q8NJN4), Neotyphodium sp. FCB-2002 (Q8NJN4)
brenda
Montero, M.; Sanz, L.; Rey, M.; Monte, E.; Llobell, A.
BGN16.3, a novel acidic beta-1,6-glucanase from mycoparasitic fungus Trichoderma harzianum CECT 2413
FEBS J.
272
3441-3448
2005
Trichoderma harzianum, Trichoderma harzianum CECT 2413
brenda
Oyama, S.; Inoue, H.; Yamagata, Y.; Nakajima, T.; Abe, K.
Functional analysis of an endo-1,6-beta-D-glucanase gene (neg-1) from Neurospora crassa
Biosci. Biotechnol. Biochem.
70
1773-1775
2006
Neurospora crassa (Q7M4T0), Neurospora crassa
brenda
Boisrame, A.; Gaillardin, C.
Heterologous expression and characterization of a beta-1,6-glucanase from Aspergillus fumigatus
Appl. Microbiol. Biotechnol.
82
663-669
2009
Aspergillus fumigatus
brenda
Ganiger, M.; Bhat, S.; Chettri, P.; Kuruvinashetti, M.
Production of endoglucanase by Trichoderma for control of phytopathogenic fungus Sclerotium rolfsii
J. Appl. Sci. Res.
5
870-875
2009
Trichoderma harzianum
-
brenda
Konno, N.; Sakamoto, Y.
An endo-beta-1,6-glucanase involved in Lentinula edodes fruiting body autolysis
Appl. Microbiol. Biotechnol.
91
1365-1373
2011
Lentinula edodes (F8WPI4), Lentinula edodes H 600 (F8WPI4)
brenda
Hattori, T.; Kato, Y.; Uno, S.; Usui, T.
Mode of action of a beta-(1->6)-glucanase from Penicillium multicolor
Carbohydr. Res.
366
6-16
2013
Penicillium multicolor, Penicillium multicolor LAM7153
brenda
Schiavone, M.; Vax, A.; Formosa, C.; Martin-Yken, H.; Dague, E.; Francois, J.M.
A combined chemical and enzymatic method to determine quantitatively the polysaccharide components in the cell wall of yeasts
FEMS Yeast Res.
14
933-947
2014
Trichoderma harzianum
brenda
Wang, D.; Kim, D.H.; Yun, E.J.; Park, Y.C.; Seo, J.H.; Kim, K.H.
The first bacterial beta-1,6-endoglucanase from Saccharophagus degradans 2-40T for the hydrolysis of pustulan and laminarin
Appl. Microbiol. Biotechnol.
101
197-204
2017
Saccharophagus degradans (Q21GC8), Saccharophagus degradans
brenda
Temple, M.J.; Cuskin, F.; Basle, A.; Hickey, N.; Speciale, G.; Williams, S.J.; Gilbert, H.J.; Lowe, E.C.
A Bacteroidetes locus dedicated to fungal 1,6-beta-glucan degradation Unique substrate conformation drives specificity of the key endo-1,6-beta-glucanase
J. Biol. Chem.
292
10639-10650
2017
Bacteroides thetaiotaomicron (Q8A2J3), Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron VPI-5482 (Q8A2J3)
brenda
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