Lignocellulosic hydrolysate inhibitors selectively inhibit/deactivate cellulase performance
Autor: | Marinda Viljoen-Bloom, Riaan den Haan, Sizwe I. Mhlongo, Willem H. van Zyl |
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Rok vydání: | 2015 |
Předmět: |
Saccharomyces cerevisiae Proteins
Bioengineering macromolecular substances Cellulase Applied Microbiology and Biotechnology Biochemistry Syringaldehyde Lignin Hydrolysate chemistry.chemical_compound Hydrolysis Enzymatic hydrolysis Tannic acid Cellulose 1 4-beta-Cellobiosidase Organic chemistry Cellulases Biomass Enzyme Inhibitors Cellulose biology Beta-glucosidase beta-Glucosidase Glucan 1 3-beta-Glucosidase Kinetics chemistry Coniferyl aldehyde biology.protein Tannins Biotechnology |
Zdroj: | Enzyme and microbial technology. 81 |
ISSN: | 1879-0909 |
Popis: | In this study, we monitored the inhibition and deactivation effects of various compounds associated with lignocellulosic hydrolysates on individual and combinations of cellulases. Tannic acid representing polymeric lignin residues strongly inhibited cellobiohydrolase 1 (CBH1) and β-glucosidase 1 (BGL1), but had a moderate inhibitory effect on endoglucanase 2 (EG2). Individual monomeric lignin residues had little or no inhibitory effect on hydrolytic enzymes. However, coniferyl aldehyde and syringaldehyde substantially decreased the activity of CBH1 and deactivated BGL1. Acetic and formic acids also showed strong inhibition of BGL1 but not CBH1 and EG2, whereas tannic, acetic and formic acid strongly inhibited a combination of CBH1 and EG2 during Avicel hydrolysis. Diminishing enzymatic hydrolysis is largely a function of inhibitor concentration and the enzyme-inhibitor relationship, rather than contact time during the hydrolysis process (i.e. deactivation). This suggests that decreased rates of hydrolysis during the enzymatic depolymerisation of lignocellulosic hydrolysates may be imparted by other factors related to substrate crystallinity and accessibility. |
Databáze: | OpenAIRE |
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