Heterogeneous Expression and Functional Characterization of Cellulose-Degrading Enzymes from Aspergillus niger for Enzymatic Hydrolysis of Alkali Pretreated Bamboo Biomass

Mol Biotechnol. 2015 Sep;57(9):859-67. doi: 10.1007/s12033-015-9878-x.

Abstract

Enzymatic hydrolysis of cellulosic biomass has caught much attention because of modest reaction conditions and environment friendly conditions. To reduce the cost and to achieve good quantity of cellulases, a heterologous expression system is highly favored. In this study, cellulose-degrading enzymes, GH3 family β-glucosidase (BGL), GH7 family-related cellobiohydrolases (CBHs), and endoglucanase (EG) from a newly isolated Aspergillus niger BE-2 are highly expressed in Pichia pastoris GS115. The strain produced EG, CBHs, and BGL enzymatic concentration of 0.56, 0.11, and 22 IU/mL, respectively. Mode of actions of the recombinant enzymes for substrate specificity and end product analysis are verified and found specific for cellulose degradation. Bamboo biomass saccharification with A. niger cellulase released a high level of fermentable sugars. Hydrolysis parameters are optimized to obtain reducing sugars level of 3.18 g/L. To obtain reducing sugars from a cellulosic biomass, A. niger could be a good candidate for enzymes resource of cellulase to produce reducing sugars from a cellulosic biomass. This study also facilitates the development of highly efficient enzyme cocktails for the bioconversion of lignocellulosic biomass into monosaccharides and oligosaccharides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkalies / chemistry
  • Aspergillus niger / enzymology*
  • Biomass
  • Carbohydrate Metabolism
  • Cellulase / metabolism
  • Cellulose / metabolism*
  • Cellulose 1,4-beta-Cellobiosidase / metabolism
  • beta-Glucosidase / metabolism

Substances

  • Alkalies
  • Cellulose
  • beta-Glucosidase
  • Cellulase
  • Cellulose 1,4-beta-Cellobiosidase