A new thermostable endoglucanase, Acidothermus cellulolyticus E1 - Synergism with Trichoderma reesei CBH I and comparison to Thermomonospora fusca E5

John O. Baker; William S. Adney; Rafael A. Nleves; Steven R. Thomas; David B. Wilson; Michael E. Himmel

doi:10.1007/BF02941803

A new thermostable endoglucanase, Acidothermus cellulolyticus E1 - Synergism with Trichoderma reesei CBH I and comparison to Thermomonospora fusca E₅

John O. Baker, William S. Adney, Rafael A. Nleves, Steven R. Thomas, David B. Wilson, Michael E. Himmel

BioEconomy and Sustainable Transportation

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

52 Scopus Citations

Abstract

A new thermostable endoglucanase, Acidothermus cellulolyticus E1, and another bacterial endoglucanase, E₅ from Thermomonospora fusca, each exhibit striking synergism with a fungal cellobiohydrolase (Trichoderma reesei CBH I) in the saccharification of microcrystalline cellulose. In neither case did the ratio of endoglucanase to exoglucanase that demonstrated maximum synergism coincide exactly with the ratio that actually released the maximum quantity of soluble sugar for a given total cellulase loading. The difference between the two ratios, after significant hydrolysis of the substrate, was considerably larger in the case of A. cellulolyticus E1. For both endoglucanase pairings with CBH I, the offset between the ratio for maximum synergism and the ratio for maximal soluble sugar production was found to be a function of digestion time.

Original language	American English
Pages (from-to)	245-256
Number of pages	12
Journal	Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology
Volume	45/46
Issue number	1
DOIs	https://doi.org/10.1007/BF02941803 https://doi.org/10.1007/BF02941803
State	Published - 1994

NREL Publication Number

NREL/JA-422-5470

Keywords

Acidothermus cellulolyticus E1
endoglucanase
synergism
Thermomonospora fusca E
Trichoderma reesei CBH I

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Baker, J. O., Adney, W. S., Nleves, R. A., Thomas, S. R., Wilson, D. B., & Himmel, M. E. (1994). A new thermostable endoglucanase, Acidothermus cellulolyticus E1 - Synergism with Trichoderma reesei CBH I and comparison to Thermomonospora fusca E₅. Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology, 45/46(1), 245-256. https://doi.org/10.1007/BF02941803, https://doi.org/10.1007/BF02941803

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abstract = "A new thermostable endoglucanase, Acidothermus cellulolyticus E1, and another bacterial endoglucanase, E5 from Thermomonospora fusca, each exhibit striking synergism with a fungal cellobiohydrolase (Trichoderma reesei CBH I) in the saccharification of microcrystalline cellulose. In neither case did the ratio of endoglucanase to exoglucanase that demonstrated maximum synergism coincide exactly with the ratio that actually released the maximum quantity of soluble sugar for a given total cellulase loading. The difference between the two ratios, after significant hydrolysis of the substrate, was considerably larger in the case of A. cellulolyticus E1. For both endoglucanase pairings with CBH I, the offset between the ratio for maximum synergism and the ratio for maximal soluble sugar production was found to be a function of digestion time.",

keywords = "Acidothermus cellulolyticus E1, endoglucanase, synergism, Thermomonospora fusca E, Trichoderma reesei CBH I",

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Baker, JO, Adney, WS, Nleves, RA, Thomas, SR, Wilson, DB & Himmel, ME 1994, 'A new thermostable endoglucanase, Acidothermus cellulolyticus E1 - Synergism with Trichoderma reesei CBH I and comparison to Thermomonospora fusca E₅', Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology, vol. 45/46, no. 1, pp. 245-256. https://doi.org/10.1007/BF02941803, https://doi.org/10.1007/BF02941803

A new thermostable endoglucanase, Acidothermus cellulolyticus E1 - Synergism with Trichoderma reesei CBH I and comparison to Thermomonospora fusca E₅. / Baker, John O.; Adney, William S.; Nleves, Rafael A. et al.
In: Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology, Vol. 45/46, No. 1, 1994, p. 245-256.

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

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