Characterization of acid catalytic domains for cellulose hydrolysis and glucose degradation
Cellulolytic enzymes consist of a catalytic domain, a linking peptide, and a binding domain. The paper describes research on carboxylic acids that have potential as catalytic domains for constructing organic macromolecules for use in cellulose hydrolysis that mimic the action of enzymes. The tested...
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Published in | Biotechnology and bioengineering Vol. 79; no. 6; pp. 610 - 618 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
New York
Wiley Subscription Services, Inc., A Wiley Company
20.09.2002
Wiley |
Subjects | |
Online Access | Get full text |
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Summary: | Cellulolytic enzymes consist of a catalytic domain, a linking peptide, and a binding domain. The paper describes research on carboxylic acids that have potential as catalytic domains for constructing organic macromolecules for use in cellulose hydrolysis that mimic the action of enzymes. The tested domains consist of the series of mono‐, di‐, and tricarboxylic acids with a range of pKa's. This paper systematically characterizes the acids with respect to hydrolysis of cellobiose, cellulose in biomass, and degradation of glucose and compares these kinetics data to dilute sulfuric acid. Results show that acid catalyzed hydrolysis is proportional to H+ concentration. The tested carboxylic acids did not catalyze the degradation of glucose while sulfuric acid catalyzed the degradation of glucose above that of water alone. Consequently, overall yields of glucose obtained from cellobiose and cellulose are higher for the best carboxylic acid tested, maleic acid, when compared to sulfuric acid at equivalent solution pH. © 2002 Wiley Periodicals, Inc. Biotechnol Bioeng 79: 610–618, 2002. |
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Bibliography: | National Science Foundation - No. BES-9727096; No. IGERT-9987576 istex:F85A51FF946FD1AAA47173C9CA5F507C2998B7EF ArticleID:BIT10316 ark:/67375/WNG-ZP3SSCFX-W ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 |
ISSN: | 0006-3592 1097-0290 |
DOI: | 10.1002/bit.10316 |