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Enzymatic hydrolysis of cellulose to glucose lung immobilized β‐glucosidase
Author(s) -
Sundstrom D. W.,
Klei H. E.,
Coughlin R. W.,
Biederman G. J.,
Brouwer C. A.
Publication year - 1981
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260230302
Subject(s) - cellobiose , cellulase , chemistry , beta glucosidase , cellulose , hydrolysis , trichoderma reesei , cellulosic ethanol , biochemistry , substrate (aquarium) , chromatography , enzymatic hydrolysis , immobilized enzyme , enzyme , biology , ecology
The production of sugars by enzymatic hydrolysis of cellulose is a multistep process which includes conversion of the intermediate cellobiose to glucose by β‐glucosidase. Aside from its role as an intermediate, cellobiose inhibits the endoglucanase components of typical cellulase enzyme systems. Because these enzyme systems often contain insufficient concentrations of β‐glucosidase to prevent accumulation of inhibitory cellobiose, this research investigated the use of supplemental immobilized β‐glucosidase to increase yield of glucose. Immobilized β‐glucosidase from Aspergillus phoenicis was produced by sorption at controlled‐pore alumina with about 90% activity retention. The product lost only about 10% of the original activity during an on‐stream reaction period of 500 hr with cellobiose as substrate; maximum activity occurred near pH 3.5 and the apparent activation energy was about 11 kcal/mol. The immobilized β‐glucosidase was used together with Trichoderma reesei cellulase to hydrolyze cellulosic materials, such as Solka Floc, corn stove and exploded wood. Increased yields of glucose and greater conversions of cellobiose of glucose were observed when the reaction systems contained supplemental immobilized β‐glucosidase.