Low molecular weight thermostable β-D-glucosidase from Acidothermus cellulolyticus

W. S. Adney; M. P. Tucker; R. A. Nieves; S. R. Thomas; M. E. Himmel

doi:10.1007/BF00134195

Low molecular weight thermostable β-D-glucosidase from Acidothermus cellulolyticus

W. S. Adney
, M. P. Tucker
, R. A. Nieves
, S. R. Thomas
, M. E. Himmel

BioEconomy and Sustainable Transportation

National Renewable Energy Laboratory

Research output: Contribution to journal › Article › peer-review

4 Scopus Citations

Abstract

Industrial use of cellulase enzymes, including β-D-glucosidases, can be greatly improved and expanded by the discovery and characterization of more robust, thermotolerant enzymes. A new thermostable β-D-glucosidase was isolated from Acidothermus cellulolyticus culture broth. This enzyme has a molecular weight of 52.5 kDa, an isoelectric pI of 4.1, and a pH activity optimum of 4.5. The optimum temperature for activity on p-nitrophenyl-β-D-glucoside is 63°C. This value is approximately 20°C higher than temperature optima displayed by most previously characterized β-D-glucosidases.

Original language	American English
Pages (from-to)	49-54
Number of pages	6
Journal	Biotechnology Letters
Volume	17
Issue number	1
DOIs	https://doi.org/10.1007/BF00134195 https://doi.org/10.1007/BF00134195
State	Published - 1995

NLR Publication Number

NREL/JA-422-7312

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title = "Low molecular weight thermostable β-D-glucosidase from Acidothermus cellulolyticus",

abstract = "Industrial use of cellulase enzymes, including β-D-glucosidases, can be greatly improved and expanded by the discovery and characterization of more robust, thermotolerant enzymes. A new thermostable β-D-glucosidase was isolated from Acidothermus cellulolyticus culture broth. This enzyme has a molecular weight of 52.5 kDa, an isoelectric pI of 4.1, and a pH activity optimum of 4.5. The optimum temperature for activity on p-nitrophenyl-β-D-glucoside is 63°C. This value is approximately 20°C higher than temperature optima displayed by most previously characterized β-D-glucosidases.",

author = "Adney, \{W. S.\} and Tucker, \{M. P.\} and Nieves, \{R. A.\} and Thomas, \{S. R.\} and Himmel, \{M. E.\}",

year = "1995",

doi = "10.1007/BF00134195",

language = "American English",

volume = "17",

pages = "49--54",

journal = "Biotechnology Letters",

issn = "0141-5492",

publisher = "Springer Science and Business Media B.V.",

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TY - JOUR

T1 - Low molecular weight thermostable β-D-glucosidase from Acidothermus cellulolyticus

AU - Adney, W. S.

AU - Tucker, M. P.

AU - Nieves, R. A.

AU - Thomas, S. R.

AU - Himmel, M. E.

PY - 1995

Y1 - 1995

N2 - Industrial use of cellulase enzymes, including β-D-glucosidases, can be greatly improved and expanded by the discovery and characterization of more robust, thermotolerant enzymes. A new thermostable β-D-glucosidase was isolated from Acidothermus cellulolyticus culture broth. This enzyme has a molecular weight of 52.5 kDa, an isoelectric pI of 4.1, and a pH activity optimum of 4.5. The optimum temperature for activity on p-nitrophenyl-β-D-glucoside is 63°C. This value is approximately 20°C higher than temperature optima displayed by most previously characterized β-D-glucosidases.

AB - Industrial use of cellulase enzymes, including β-D-glucosidases, can be greatly improved and expanded by the discovery and characterization of more robust, thermotolerant enzymes. A new thermostable β-D-glucosidase was isolated from Acidothermus cellulolyticus culture broth. This enzyme has a molecular weight of 52.5 kDa, an isoelectric pI of 4.1, and a pH activity optimum of 4.5. The optimum temperature for activity on p-nitrophenyl-β-D-glucoside is 63°C. This value is approximately 20°C higher than temperature optima displayed by most previously characterized β-D-glucosidases.

UR - https://www.scopus.com/pages/publications/0028944786

U2 - 10.1007/BF00134195

DO - 10.1007/BF00134195

M3 - Article

AN - SCOPUS:0028944786

SN - 0141-5492

VL - 17

SP - 49

EP - 54

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 1

ER -

Low molecular weight thermostable β-D-glucosidase from Acidothermus cellulolyticus

Abstract

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