A new thermostable endoglucanase, acidothermus cellulolyticus E1

Journal Article · · Applied Biochemistry and Biotechnology; (United States)

DOI:https://doi.org/10.1007/BF02941803· OSTI ID:6778775

Baker, J O; Adney, W S; Nieves, R A; Thomas, S R; Himmel, M E ^[1]; Wilson, D B ^[2]

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1. National Renewable Energy Lab., Golden, CO (United States)
2. Cornell Univ., Ithaca, NY (United States)

A new thermostable endoglucanase, Acidothermus cellulolyticus E1, and another bacterial endoglucanase, E[sub 5] 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 the 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. 19 refs., 5 figs.

• OSTI ID: 6778775
• Journal Information: Applied Biochemistry and Biotechnology; (United States), Journal Name: Applied Biochemistry and Biotechnology; (United States) Journal Issue: 1 Vol. 45-46; ISSN ABIBDL; ISSN 0273-2289
• Country of Publication: United States
• Language: English

Related Subjects

09 BIOMASS FUELS
090900* -- Biomass Fuels-- Processing-- (1990-)
CARBOHYDRATES
CELLULASE
CELLULOSE
CHEMICAL REACTIONS
DECOMPOSITION
ENZYMES
GLYCOSYL HYDROLASES
HYDROLASES
HYDROLYSIS
LYSIS
O-GLYCOSYL HYDROLASES
ORGANIC COMPOUNDS
POLYSACCHARIDES
PROTEINS
SACCHARIDES
SACCHARIFICATION
SOLVOLYSIS
SYNERGISM
THERMOPHILIC CONDITIONS