Cotton cellulose: Enzyme adsorption and enzymatic hydrolysis
β Scribed by P. L. Beltrame; P. Carniti; B. Focher; A. Marzetti; M. Cattaneo
- Publisher
- John Wiley and Sons
- Year
- 1982
- Tongue
- English
- Weight
- 542 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0021-8995
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β¦ Synopsis
Abstract
Adsorption of a crude cellulase complex from Trichoderma viride on variously pretreated cotton celluloses has been studied in the framework of the Langmuir approach, in the temperature range 2β8Β°C. The saturation amount of adsorbed enzyme has been related to their susceptibility to hydrolysis. In every case the adsorption process was found to be faster by 2β3 orders of magnitude than the hydrolysis step to give end products. For one substrate, the Langmuir parameters were found to be fairly well correlated with the value of the Michaelis constant K~m~, measured for its enzymatic hydrolysis, and the adsorptive complex (ES)~ad~ was indistinguishable from the complex (ES) of the MichaelisβMenten model for the hydrolysis.
π SIMILAR VOLUMES
## Abstract Waste cellulose was a suitable carbon source for cellulose production by __Trichoderma viride__. The enzyme can be produced in submerged fermentation using newspaper as a growth substrate. A variety of pure and complex cellulosic materials were hydrolyzed by culture filtrates. Saccharif
Cotton cellulose has been subjected to continuous and repeated enzymatic hydrolysis for different periods. It has been observed that the length of hydrocellulose particles obtained on repeated enzyme action is reduced to about 300500 8, as compared to 900-3OOO 8, obtained on prolonged enzyme treatme