Mechanism of substrate inhibition in cellulose synergistic degradation
2001 (English)In: European Journal of Biochemistry, ISSN 0014-2956, E-ISSN 1432-1033, Vol. 268, no 16, 4520-4526 p.Article in journal (Refereed) Published
A comprehensive experimental study of substrate inhibition in cellulose hydrolysis based on a well defined system is presented. The hydrolysis of bacterial cellulose by synergistically operating binary mixtures of cellobiohydrolase I from Trichoderma reesei and five different endoglucanases as well as their catalytic domains displays a characteristic substrate inhibition. This inhibition phenomenon is shown to require the two-domain structure of an intact cellobiohydrolase. The experimental data were in accordance with a mechanism where cellobiohydrolases previously bound to the cellulose by means of their cellulose binding domains are able to find chain ends by lateral diffusion. An increased substrate concentration at a fixed enzyme load will also increase the average diffusion distance/time needed for cellobiohydrolases to reach new chain ends created by endoglucanases, resulting in an apparent substrate inhibition of the synergistic action. The connection between the binding properties and the substrate inhibition is encouraging with respect to molecular engineering of the binding domain for optimal performance in biotechnological processes.
Place, publisher, year, edition, pages
2001. Vol. 268, no 16, 4520-4526 p.
cellulose, cellulase, substrate inhibition, synergism, hydrolysis, trichoderma-viride cellulase, cellobiohydrolase-i, crystalline cellulose, enzymatic-hydrolysis, binding domains, reesei, model, kinetics, reveals, enzymes
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:uu:diva-87239DOI: 10.1046/j.1432-1327.2001.02377.xOAI: oai:DiVA.org:uu-87239DiVA: diva2:334
Addresses: Johansson G, Univ Uppsala, Dept Biochem, POB 576, S-75123 Uppsala, Sweden. Univ Uppsala, Dept Biochem, S-75123 Uppsala, Sweden. Univ Tartu, Inst Mol & Cell Biol, Tartu, Estonia.2008-11-182008-09-102011-12-01Bibliographically approved