Enhanced saccharification of sugarcane bagasse using soluble cellulase supplemented with immobilized β-glucosidase

Bioresour Technol. 2014 Sep:167:206-13. doi: 10.1016/j.biortech.2014.06.021. Epub 2014 Jun 14.

Abstract

The β-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.

Keywords: Enzyme immobilization; Hydrolysis; Sugarcane bagasse; β-Glucosidase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

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

Substances

  • Enzymes, Immobilized
  • Glyoxylates
  • glyoxyl agarose
  • Cellobiose
  • Cellulose
  • bagasse
  • Sepharose
  • beta-Glucosidase
  • Cellulase