Premium
Synergistic cellulose hydrolysis can be described in terms of fractal‐like kinetics
Author(s) -
Väljamäe Priit,
Kipper Kalle,
Pettersson Göran,
Johansson Gunnar
Publication year - 2003
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.10775
Subject(s) - trichoderma reesei , chemistry , kinetics , cellulase , substrate (aquarium) , cellulose , hydrolysis , enzyme kinetics , diffusion , fractal , stereochemistry , enzyme , thermodynamics , organic chemistry , active site , physics , mathematics , mathematical analysis , oceanography , quantum mechanics , geology
Abstract A fractal‐like kinetics model was used to describe the synergistic hydrolysis of bacterial cellulose by Trichoderma reesei cellulases. The synergistic action of intact cellobiohydrolase Cel7A and endoglucanase Cel5A at low enzyme‐to‐substrate ratios showed an apparent substrate inhibition consistent with a case where two‐dimensional (2‐D) surface diffusion of the cellobiohydrolase is rate‐limiting. The action of Cel7A core and Cel5A was instead consistent with a three‐dimensional (3‐D) diffusion‐based mode of action. The synergistic action of intact Cel7A was far superior to that of the core at a high enzyme‐to‐substrate ratio, but this effect was gradually reduced at lower enzyme‐to‐substrate ratios. The apparent fractal kinetics exponent h obtained by nonlinear fit of hydrolysis data to the fractal‐like kinetics analogue of a first‐order reaction was a useful empirical parameter for assessing the rate retardation and its dependence on the reaction conditions. © 2003 Wiley Periodicals, Inc. Biotechnol Bioeng 84: 254–257, 2003.