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A theoretical-analysis of cellulase product inhibition - effect of cellulase binding constant, enzyme substrate ratio, and beta-glucosidase activity on the inhibition patternстатья
Информация о цитировании статьи получена из
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Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Gusakov A.V., Sinitsyn A.P.
- Журнал: Biotechnology and Bioengineering
- Том: 40
- Номер: 6
- Год издания: 1992
- Издательство: Wiley - V C H Verlag GmbbH & Co.
- Местоположение издательства: Germany
- Первая страница: 663
- Последняя страница: 671
- DOI: 10.1002/bit.260400604
- Аннотация: Theoretical analysis of cellulase product inhibition (by cellobiose and glucose) has been performed in terms of the mathematical model for enzymatic cellulose hydrolysis. The analysis showed that even in those cases when consideration of multienzyme cellulase system as one enzyme (cellulase) or two enzymes (cellulase and beta-glucosidase) is valid, double-reciprocal plots, usually used in a product inhibition study, may be nonlinear, and different inhibition patterns (noncompetitive, competitive, or mixed type) may be observed. Inhibition pattern depends on the cellulase binding constant, enzyme concentration, maximum adsorption of the enzyme (cellulose surface area accessible to the enzyme), the range in which substrate concentration is varied, and beta-glucosidase activity. A limitation of cellulase adsorption by cellulose surface area that may occur at high enzyme/substrate ratio is the main reason for nonlinearity of double-reciprocal plots. Also, the results of calculations showed that material balance by substrate, which is usually neglected by researchers studying cellulase product inhibition, must be taken into account in kinetic analysis even in those cases when the enzyme concentration is rather low.
- Добавил в систему: Гусаков Александр Васильевич