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Malbranchea cinnamomea: A thermophilic fungal source of catalytically efficient lignocellulolytic glycosyl hydrolases and metal dependent enzymes.

Author(s): Mahajan C, Basotra N, Singh S, Di Falco M, Tsang A, Chadha BS

Bioresour Technol. 2016 Jan;200:55-63 Authors: Mahajan C, Basotra N, Singh S, Di Falco M, Tsang A, Chadha BS

Article GUID: 26476165
Title:Malbranchea cinnamomea: A thermophilic fungal source of catalytically efficient lignocellulolytic glycosyl hydrolases and metal dependent enzymes.
Authors:Mahajan C,  Basotra N,  Singh S,  Di Falco M,  Tsang A,  Chadha BS
Link:https://www.ncbi.nlm.nih.gov/pubmed/26476165?dopt=Abstract
DOI:10.1016/j.biortech.2015.09.113
Category:Bioresour Technol
PMID:26476165
Dept Affiliation: GENOMICS
1 Department of Microbiology, Guru Nanak Dev University, Amritsar 143005, Punjab, India. Electronic address: chhaviosho@yahoo.com.
2 Department of Microbiology, Guru Nanak Dev University, Amritsar 143005, Punjab, India. Electronic address: nehabasotra506@gmail.com.
3 Division of Microbiology, ICAR-Indian Agricultural Research Institute, New Delhi, India. Electronic address: ssriari@gmail.com.
4 Centre for Structural and Functional Genomics, Concordia University, 7141 Sherbrooke Street West, Montréal, Québec H4B 1R6, Canada. Electronic address: marcos.difalco@concordia.ca.
5 Centre for Structural and Functional Genomics, Concordia University, 7141 Sherbrooke Street West, Montréal, Québec H4B 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:

Malbranchea cinnamomea: A thermophilic fungal source of catalytically efficient lignocellulolytic glycosyl hydrolases and metal dependent enzymes.

Bioresour Technol. 2016 Jan;200:55-63

Authors: Mahajan C, Basotra N, Singh S, Di Falco M, Tsang A, Chadha BS

Abstract

This study reports thermophilic fungus Malbranchea cinnamomea as an important source of lignocellulolytic enzymes. The secretome analysis using LC-MS/MS orbitrap showed that fungus produced a spectrum of glycosyl hydrolases (cellulase/hemicellulase), polysaccharide lyases (PL) and carbohydrate esterases (CE) in addition to cellobiose dehydrogenase (CDH) indicating the presence of functional classical and oxidative cellulolytic mechanisms. The protein fractions in the secretome resolved by ion exchange chromatography were analyzed for ability to hydrolyze alkali treated carrot grass (ATCG) in the presence of Mn(2+)/Cu(2+). This strategy in tandem with peptide mass fingerprinting led to identification of metal dependent protein hydrolases with no apparent hydrolytic activity, however, showed 5.7 folds higher saccharification in presence of Mn(2+). Furthermore, adding different protein fractions to commercial cellulase (Novozymes: Cellic CTec2) resulted in enhanced hydrolysis of ATCG ranging between 1.57 and 3.43 folds indicating the enzymes from M. cinnamomea as catalytically efficient.

PMID: 26476165 [PubMed - indexed for MEDLINE]