Lignocellulose degrading extremozymes produced by Pichia pastoris: current status and future prospects


Ergun B. G. , ÇALIK P.

BIOPROCESS AND BIOSYSTEMS ENGINEERING, vol.39, no.1, pp.1-36, 2016 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Review
  • Volume: 39 Issue: 1
  • Publication Date: 2016
  • Doi Number: 10.1007/s00449-015-1476-6
  • Title of Journal : BIOPROCESS AND BIOSYSTEMS ENGINEERING
  • Page Numbers: pp.1-36
  • Keywords: Lignocellulose degradation, Pichia pastoris, Extremozymes, Hemicellulases, Laccase, Cellulases, FAMILY 11 XYLANASE, HIGH-LEVEL EXPRESSION, ALKALINE BETA-MANNANASE, PHIALOPHORA SP G5, BISPORA SP MEY-1, RECOMBINANT PROTEIN-PRODUCTION, CARBOHYDRATE-BINDING MODULE, ASPERGILLUS-NIGER-XYLANASE, PENICILLIUM-PINOPHILUM C1, HIGH CATALYTIC EFFICIENCY

Abstract

In this review article, extremophilic lignocellulosic enzymes with special interest on xylanases, beta-mannanases, laccases and finally cellulases, namely, endoglucanases, exoglucanases and beta-glucosidases produced by Pichia pastoris are reviewed for the first time. Recombinant lignocellulosic extremozymes are discussed from the perspectives of their potential application areas; characteristics of recombinant and native enzymes; the effects of P. pastoris expression system on recombinant extremozymes; and their expression levels and applied strategies to increase the enzyme expression yield. Further, effects of enzyme domains on activity and stability, protein engineering via molecular dynamics simulation and computational prediction, and site-directed mutagenesis and amino acid modifications done are also focused. Superior enzyme characteristics and improved stability due to the proper post-translational modifications and better protein folding performed by P. pastoris make this host favourable for extremozyme production. Especially, glycosylation contributes to the structure, function and stability of enzymes, as generally glycosylated enzymes produced by P. pastoris exhibit better thermostability than non-glycosylated enzymes. However, there has been limited study on enzyme engineering to improve catalytic efficiency and stability of lignocellulosic enzymes. Thus, in the future, studies should focus on protein engineering to improve stability and catalytic efficiency via computational modelling, mutations, domain replacements and fusion enzyme technology. Also metagenomic data need to be used more extensively to produce novel enzymes with extreme characteristics and stability.