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Expression of catalytically efficient xylanases from thermophilic fungus Malbranchea cinnamomea for synergistically enhancing hydrolysis of lignocellulosics.

Author(s): Basotra N, Joshi S, Satyanarayana T, Pati PK, Tsang A, Chadha BS

Int J Biol Macromol. 2018 Mar;108:185-192 Authors: Basotra N, Joshi S, Satyanarayana T, Pati PK, Tsang A, Chadha BS

Article GUID: 29174359
Title:Expression of catalytically efficient xylanases from thermophilic fungus Malbranchea cinnamomea for synergistically enhancing hydrolysis of lignocellulosics.
Authors:Basotra N,  Joshi S,  Satyanarayana T,  Pati PK,  Tsang A,  Chadha BS
Link:https://www.ncbi.nlm.nih.gov/pubmed/29174359?dopt=Abstract
DOI:10.1016/j.ijbiomac.2017.11.131
Category:Int J Biol Macromol
PMID:29174359
Dept Affiliation: GENOMICS
1 Department of Microbiology, Guru Nanak Dev University, Amritsar, 143005, Punjab, India. Electronic address: nehabasotra506@gmail.com.
2 Central University of Gujarat, Gandhinagar, Gujarat, India. Electronic address: swati.joshi.aj@gmail.com.
3 Division of Biological Sciences & Engineering, Netaji Subhas Institute of Technology, Azad Hind Fauz Marg, Dwarka, New Delhi,110078, India. Electronic address: tsnarayana@gmail.com.
4 Department of Biotechnology, Guru Nanak Dev University, Amritsar, 143005, Punjab, India. Electronic address: pkpati@yahoo.com.
5 Center for Structural and Functional Genomics, Concordia University, 7141 Sherbrooke Street West, Montreal, Quebec H4 B 1R6, Canada. Electronic address: adrian.tsang@concordia.ca.
6 Department of Microbiology, Guru Nanak Dev University, Amritsar, 143005, Punjab, India. Electronic address: chadhabs@yahoo.com.

Description:

Expression of catalytically efficient xylanases from thermophilic fungus Malbranchea cinnamomea for synergistically enhancing hydrolysis of lignocellulosics.

Int J Biol Macromol. 2018 Mar;108:185-192

Authors: Basotra N, Joshi S, Satyanarayana T, Pati PK, Tsang A, Chadha BS

Abstract

In this study, two xylanase genes (GH10 and GH11) derived from Malbranchea cinnamomea, designated as XYN10A_MALCI and XYN11A_MALCI, respectively, were expressed in Pichia pastoris X33. The maximum level of xylanase expression was found to be 24.3U/ml for rXYN10A_MALCI and 573.32U/ml for rXYN11A_MALCI. The purified recombinant rXYN11A_MALCI was stable at 70°C and catalytically active against a variety of substituted (arabinoxylans) as well as unsubstituted xylans. The hydrolytic potential of recombinant xylanases for enhancing the hydrolysis of acid/alkali pretreated lignocellulosics (rice straw and bagasse) by the commercial cellulase Cellic CTec2 was assessed which revealed that both rXYN10A_MALCI and rXYN11A_MALCI act synergistically with commercial cellulases and resulted in 1.54 and 1.58 folds improved hydrolysis of acid treated rice straw and alkali treated rice straw using cocktail comprising of Cellic CTec2 and XYN11A_MALCI (8:2 ratio) when compared to Cellic CTec2 alone at same protein loading rate of (~5.7mg/g biomass).

PMID: 29174359 [PubMed - indexed for MEDLINE]