PERFORM Publications

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Title		Authors	PubMed ID
1	Retraction notice to "Thermostable xylanases from thermophilic fungi and bacteria: Current perspective" [Bioresour. Technol. 277 (2019) 195-203]	Chadha BS; Kaur B; Basotra N; Tsang A; Pandey A;	39447502 CSFG
2	Developing endophytic Penicillium oxalicum as a source of lignocellulolytic enzymes for enhanced hydrolysis of biorefinery relevant pretreated rice straw	Sharma G; Kaur B; Raheja Y; Kaur A; Singh V; Basotra N; Di Falco M; Tsang A; Chadha BS;	39249151 CSFG
3	CRISPR/Cas9 mediated gene editing of transcription factor ACE1 for enhanced cellulase production in thermophilic fungus Rasamsonia emersonii	Singh V; Raheja Y; Basotra N; Sharma G; Tsang A; Chadha BS;	37658430 CSFG
4	Lignocellulolytic enzymes from Aspergillus allahabadii for efficient bioconversion of rice straw into fermentable sugars and biogas	Sharma G; Kaur B; Raheja Y; Agrawal D; Basotra N; Di Falco M; Tsang A; Singh Chadha B;	35753566 CSFG
5	Combination of system biology and classical approaches for developing biorefinery relevant lignocellulolytic Rasamsonia emersonii strain	Raheja Y; Singh V; Kaur B; Basotra N; Di Falco M; Tsang A; Singh Chadha B;	35318142 CSFG
6	Discovery and Expression of Thermostable LPMOs from Thermophilic Fungi for Producing Efficient Lignocellulolytic Enzyme Cocktails.	Agrawal D, Basotra N, Balan V, Tsang A, Chadha BS	31792786 CSFG
7	Malbranchea cinnamomea: A thermophilic fungal source of catalytically efficient lignocellulolytic glycosyl hydrolases and metal dependent enzymes.	Mahajan C, Basotra N, Singh S, Di Falco M, Tsang A, Chadha BS	26476165 CSFG
8	Expression of catalytically efficient xylanases from thermophilic fungus Malbranchea cinnamomea for synergistically enhancing hydrolysis of lignocellulosics.	Basotra N, Joshi S, Satyanarayana T, Pati PK, Tsang A, Chadha BS	29174359 CSFG
9	Thermostable xylanases from thermophilic fungi and bacteria: Current perspective.	Chadha BS, Kaur B, Basotra N, Tsang A, Pandey A	30679061 CSFG
10	Characterization of a novel Lytic Polysaccharide Monooxygenase from Malbranchea cinnamomea exhibiting dual catalytic behavior	Basotra N; Dhiman SS; Agrawal D; Sani RK; Tsang A; Chadha BS;	31054382 ENCS

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
Publication:	Bioresource technology
Keywords:	Cellobiose dehydrogenase; Glycosyl hydrolases; Ion exchange chromatography; M cinnamomea; Secretome;
PMID:	26476165	Category:	Bioresour Technol	Date Added:	2019-06-07
Dept Affiliation:	CSFG 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]

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