Substrate specificity of family 5, 6, 7, 9, 12, and 45 endoglucanases
| Autor: | Elena Vlasenko, M. Schülein, Joel R. Cherry, Feng Xu |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Environmental Engineering
Subfamily Bioengineering Cellulase Substrate Specificity Mannans chemistry.chemical_compound Polysaccharides Arabinoxylan Enzyme Stability Glycoside hydrolase Cellulose Waste Management and Disposal Phylogeny Mannan chemistry.chemical_classification biology Renewable Energy Sustainability and the Environment Temperature Galactose General Medicine Protein tertiary structure Xyloglucan Enzyme chemistry Biochemistry Multigene Family biology.protein Biocatalysis Xylans |
| Zdroj: | Bioresource technology. 101(7) |
| ISSN: | 1873-2976 |
| Popis: | Endoglucanases are important enzymes for biomass conversion and other industrial processes. Determining the specificity of endoglucanases from various glycoside hydrolase families is of interest for bioinformatic functional prediction and substrate-tailored enzyme development. To do so, we characterized ∼30 endoglucanases from six glycoside hydrolase families. For p -nitrophenyl cellobioside and lactoside, only family 7 enzymes showed significant activity. For xyloglucan, both family 7 and 12 enzymes showed significant activity. For xylan and arabinoxylan, only family 7 enzymes showed significant activity. For mannan and galactomannan, both family 5 and 9 enzymes showed significant activity. The difference in specificity was preliminarily attributed mainly to the structural difference of the enzymes’ active sites. For family 7 endoglucanases, difference in thermal stability might affect their performance in hydrolyzing various (hemi)cellulose substrates. Phylogenetic analysis on the subfamily distribution of family 5 endoglucanases (in relation with mannanases) suggested that their mannanase side-activity might be the remnant of an ancestral multi-function enzyme. Similar analysis was also made with the xyloglucanase or arabionxylans side-activity of family 12 and 7 endoglucanases. The apparent dependence of the specificity on family (primary/tertiary structure) might assist us in better understanding the structure–function relationship of the enzymes, and developing more versatile biocatalysts for the utilization of biomass. |
| Databáze: | OpenAIRE |
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