Literature summary for 3.2.1.37 extracted from

Martins, M.; Ventorim, R.; Coura, R.; Maitan-Alfenas, G.; Alfenas, R.; Guimaraes, V.
The beta-xylosidase from Ceratocystis fimbriata RM35 improves the saccharification of sugarcane bagasse (2018), Biocatal. Agricult. Biotechnol., 13, 291-298 .

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Search for more literature for 3.2.1.37

Application

Application	Comment	Organism
biofuel production	the beta-xylosidase when combined with xylanase shows positive effect on xylan hydrolysis. The higher amount of glucose and xylose generated from sugarcane bagasse hydrolysis using the commercial cocktail Multifect CL supplemented with beta-xylosidase demonstrates that this enzyme has potential to be used as a supplement for commercial cocktails to improve the yield of xylose and glucose release, and this is of great importance for the production of second generation ethanol	Ceratocystis fimbriata
biotechnology	the beta-xylosidase when combined with xylanase shows positive effect on xylan hydrolysis. The higher amount of glucose and xylose generated from sugarcane bagasse hydrolysis using the commercial cocktail Multifect CL supplemented with beta-xylosidase demonstrates that this enzyme has potential to be used as a supplement for commercial cocktails to improve the yield of xylose and glucose release, and this is of great importance for the production of second generation ethanol	Ceratocystis fimbriata

Inhibitors

Inhibitors	Comment	Organism	Structure
AlCl3	about 85% residual activity at 1 mM	Ceratocystis fimbriata
CuSO4	about 70% residual activity at 1 mM	Ceratocystis fimbriata
D-xylose	competitive inhibition, about 65% residual activity at 1 mM	Ceratocystis fimbriata
FeSO4	about 65% residual activity at 1 mM	Ceratocystis fimbriata
additional information	not inhibited by CoCl2, KCl, MgSO4, CaCl2, EDTA, D-glucose, arabinose, and fructose	Ceratocystis fimbriata
SDS	about 82% residual activity at 1 mM	Ceratocystis fimbriata

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.326	-	4-nitrophenyl beta-D-xylopyranoside	pH 5.0, 50°C	Ceratocystis fimbriata
0.326	-	4-nitrophenyl beta-D-xylopyranoside	at pH 5.0 and 50°C	Ceratocystis fimbriata

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	-	Ceratocystis fimbriata	-	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
161600	-	SDS-PAGE	Ceratocystis fimbriata

Organism

Organism	UniProt	Comment	Textmining
Ceratocystis fimbriata	-	-	-
Ceratocystis fimbriata RM 35	-	-	-
Ceratocystis fimbriata RM35	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Ceratocystis fimbriata
DEAE-Sepharose column chromatography and Sephacryl S-300 gel filtration	Ceratocystis fimbriata

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.014	-	substrate: 4-nitrophenyl beta-D-glucoside, pH 5.0, 50°C	Ceratocystis fimbriata
0.126	-	substrate: 4-nitrophenyl beta-D-xylopyranoside, pH 5.0, 50°C	Ceratocystis fimbriata

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4-nitrophenyl beta-D-glucopyranoside + H2O	11.1% activity compared to beta-D-xylopyranoside	Ceratocystis fimbriata	4-nitrophenol + beta-D-glucopyranose	-	?
4-nitrophenyl beta-D-glucopyranoside + H2O	11.1% activity compared to beta-D-xylopyranoside	Ceratocystis fimbriata RM35	4-nitrophenol + beta-D-glucopyranose	-	?
4-nitrophenyl beta-D-glucopyranoside + H2O	11.1% activity compared to beta-D-xylopyranoside	Ceratocystis fimbriata RM 35	4-nitrophenol + beta-D-glucopyranose	-	?
4-nitrophenyl beta-D-glucoside + H2O	activity is 11.1% compared to activity with 4-nitrophenyl-beta-D-xylopyranoside. The enzyme shows selectivity for beta configuration	Ceratocystis fimbriata	4-nitrophenol + beta-D-glucose	-	?
4-nitrophenyl beta-D-glucoside + H2O	activity is 11.1% compared to activity with 4-nitrophenyl-beta-D-xylopyranoside. The enzyme shows selectivity for beta configuration	Ceratocystis fimbriata RM35	4-nitrophenol + beta-D-glucose	-	?
4-nitrophenyl beta-D-glucoside + H2O	activity is 11.1% compared to activity with 4-nitrophenyl-beta-D-xylopyranoside. The enzyme shows selectivity for beta configuration	Ceratocystis fimbriata RM 35	4-nitrophenol + beta-D-glucose	-	?
4-nitrophenyl beta-D-xylopyranoside + H2O	100% activity	Ceratocystis fimbriata	4-nitrophenol + beta-D-xylopyranose	-	?
4-nitrophenyl beta-D-xylopyranoside + H2O	the enzyme shows selectivity for beta configuration	Ceratocystis fimbriata	4-nitrophenol + beta-D-xylopyranose	-	?
4-nitrophenyl beta-D-xylopyranoside + H2O	100% activity	Ceratocystis fimbriata RM35	4-nitrophenol + beta-D-xylopyranose	-	?
4-nitrophenyl beta-D-xylopyranoside + H2O	the enzyme shows selectivity for beta configuration	Ceratocystis fimbriata RM35	4-nitrophenol + beta-D-xylopyranose	-	?
4-nitrophenyl beta-D-xylopyranoside + H2O	100% activity	Ceratocystis fimbriata RM 35	4-nitrophenol + beta-D-xylopyranose	-	?
4-nitrophenyl beta-D-xylopyranoside + H2O	the enzyme shows selectivity for beta configuration	Ceratocystis fimbriata RM 35	4-nitrophenol + beta-D-xylopyranose	-	?
additional information	no activity with 4-nitrophenyl alpha -L-arabinopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-mannopyranoside	Ceratocystis fimbriata	?	-	?
additional information	no activity with 4-nitrophenyl alpha -L-arabinopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-mannopyranoside	Ceratocystis fimbriata RM35	?	-	?
additional information	no activity with 4-nitrophenyl alpha -L-arabinopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-mannopyranoside	Ceratocystis fimbriata RM 35	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 161600, SDS-PAGE	Ceratocystis fimbriata

Synonyms

Synonyms	Comment	Organism
beta-xylosidase	-	Ceratocystis fimbriata

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
65	-	-	Ceratocystis fimbriata

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
50	70	significant enzyme activity in the range of 5565 °C.At 50°C and 70°C, the enzyme activity is reduced, reaching about 40% and 50% of its maximum activity, respectively. Considerable inactivation is detected below 35°C and above 75°C	Ceratocystis fimbriata
50	70	50°C: about 40% of maximal activity, 70°C: about 50% of maximal activity	Ceratocystis fimbriata

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
60	-	1 h, 14% loss of activity	Ceratocystis fimbriata
60	-	24 h, 30% loss of activity	Ceratocystis fimbriata
60	-	the enzyme maintains 70% of its maximum activity after 24 h of incubation at 60°C	Ceratocystis fimbriata
65	-	30 min, 48% loss of activity, 1 h, 47% loss of activity	Ceratocystis fimbriata
70	-	5 min, 74% loss of activity, Completely inactivated after 1 h	Ceratocystis fimbriata

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
3.9	-	-	Ceratocystis fimbriata

pH Range

pH Minimum	pH Maximum	Comment	Organism
3.8	5	the enzyme retains more than 90% of its maximum activity at a pH range from pH 3.8 to pH 4.3 at 50°C. At pH 5.0 the enzyme maintains about 60% of its maximal activity	Ceratocystis fimbriata

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
2.9	-	pH 5.0, room temperature, 12 h, the enzyme maintains 73.1% of its maximal activity	Ceratocystis fimbriata
2.9	8	the enzyme maintains significant activity when pre-incubated at pH from 2.9 to 8.0 for 12 h, with 73.1% and 51.5% of its maximum activity, respectively	Ceratocystis fimbriata
8	-	pH 5.0, room temperature, 12 h, the enzyme maintains 51.1% of its maximal activity	Ceratocystis fimbriata

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
4.79	-	D-xylose	pH 5.0, 50°C	Ceratocystis fimbriata
4.79	-	D-xylose	at pH 5.0 and 50°C	Ceratocystis fimbriata

General Information

General Information	Comment	Organism
metabolism	beta-xylosidase combined with a xylanase had an additive effect on beechwood xylan hydrolysis, generating xylose as a final product	Ceratocystis fimbriata

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Release 2023.1 (January 2023)