Inhibition of /beta/-glucosidase activity in Trichoderma reesei C30 cellulase by derivatives and isomers of glucose

Journal Article · Wed Jul 01 00:00:00 EDT 1981 · Biotechnol. Bioeng.; (United States)

DOI:https://doi.org/10.1002/bit.260230714· OSTI ID:5105689

Woodward, J; Arnold, S L

The inhibition of /beta/-glucosidase in Trichoderma reesei C30 cellulase by D-glucose, its isomers, and derivatives was studied using cellobiose and p-nitrophenyl-/beta/-glucoside as substrates for determining enzyme activity. The enzymatic hydrolysis of both substrates was inhibited competitively by glucose. This inhibition by glucose was maximal at pH 4.8 and no inhibition was observed at pH 6.5 and above. The /alpha/anomer of glucose inhibited /beta/-glucosidase to a greater extent than did the /beta/form. Compared with D-glucose, L-glucose, D-glucose-6-phosphate, and D-glucose-1-phosphate inhibited the enzyme to a much lesser extent, unlike D-glucose-L-cysteine which was almost as inhibitory as glucose itself when cellobiose was used as substrate. Fructose (2-100mM) was found to be a poor inhibitor of the enzyme. It is suggested that high rates of cellobiose hydrolysis catalyzed by /beta/-glucosidase may be prolonged by converting the reaction product glucose to fructose using a suitable preparation of glucose isomerase. 20 refs.

• Research Organization: Oak Ridge Natl Lab, TN
• OSTI ID: 5105689
• Journal Information: Biotechnol. Bioeng.; (United States), Vol. 23:7
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
GLUCOSIDASE
INHIBITION
CELLOBIOSE
CELLULASE
ENZYMATIC HYDROLYSIS
ENZYME ACTIVITY
GLUCOSE
ISOMERS
TRICHODERMA
ALDEHYDES
CARBOHYDRATES
CHEMICAL REACTIONS
DECOMPOSITION
DISACCHARIDES
ENZYMES
FUNGI
GLYCOSYL HYDROLASES
HEXOSES
HYDROLASES
HYDROLYSIS
LYSIS
MONOSACCHARIDES
O-GLYCOSYL HYDROLASES
OLIGOSACCHARIDES
ORGANIC COMPOUNDS
PLANTS
SACCHARIDES
SOLVOLYSIS
550200* - Biochemistry