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Title of Journal: Bioprocess Biosyst Eng

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Abbravation: Bioprocess and Biosystems Engineering

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Springer Berlin Heidelberg

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DOI

10.1007/bf00525047

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1615-7605

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Lignocellulose degrading extremozymes produced by

Authors: Burcu Gündüz Ergün Pınar Çalık
Publish Date: 2015/10/23
Volume: 39, Issue: 1, Pages: 1-36
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Abstract

In this review article extremophilic lignocellulosic enzymes with special interest on xylanases βmannanases laccases and finally cellulases namely endoglucanases exoglucanases and βglucosidases 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 sitedirected mutagenesis and amino acid modifications done are also focused Superior enzyme characteristics and improved stability due to the proper posttranslational 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 nonglycosylated 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


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