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Bioresour Technol ; 167: 206-13, 2014 Sep.
Article in English | MEDLINE | ID: mdl-24983691

ABSTRACT

The ß-glucosidase (BG) enzyme plays a vital role in the hydrolysis of lignocellulosic biomass. Supplementation of the hydrolysis reaction medium with BG can reduce inhibitory effects, leading to greater conversion. In addition, the inclusion of immobilized BG can be a useful way of increasing enzyme stability and recyclability. BG was adsorbed on polyacrylic resin activated by carboxyl groups (BG-PC) and covalently attached to glyoxyl-agarose (BG-GA). BG-PC exhibited similar behavior to soluble BG in the hydrolysis of cellobiose, while BG-GA hydrolyzed the same substrate at a lower rate. However, the thermal stability of BG-GA was higher than that of free BG. Hydrolysis of pretreated sugarcane bagasse catalyzed by soluble cellulase supplemented with immobilized BG improved the conversion by up to 40% after 96 h of reaction. Both derivatives remained stable up to the third cycle and losses of activity were less than 50% after five cycles.


Subject(s)
Biotechnology/methods , Carbohydrate Metabolism , Cellulase/metabolism , Cellulose/metabolism , Enzymes, Immobilized/metabolism , Saccharum/metabolism , beta-Glucosidase/metabolism , Adsorption , Cellobiose , Enzyme Stability , Glyoxylates/chemistry , Hydrogen-Ion Concentration , Hydrolysis , Sepharose/chemistry , Solubility , Temperature , Trichoderma/enzymology
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