PERFORM Publications

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Title		Authors	PubMed ID
1	Fortifying the Rasamsonia emersonii secretome with recombinant cellobiohydrolase (GH7) for efficient biomass saccharification	Raheja Y; Singh V; Gaur VK; Sharma G; Tsang A; Chadha BS;	40622460 GENOMICS
2	Heterologous Expression of Thermostable Endoglucanases from Rasamsonia emersonii: A Paradigm Shift in Biomass Hydrolysis	Raheja Y; Singh V; Gaur VK; Tsang A; Chadha BS;	40418313 GENOMICS
3	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
4	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
5	Transcriptional and secretome analysis of Rasamsonia emersonii lytic polysaccharide mono-oxygenases	Raheja Y; Singh V; Kumar N; Agrawal D; Sharma G; Di Falco M; Tsang A; Chadha BS;	39167166 CSFG
6	Genome and secretome insights: unravelling the lignocellulolytic potential of Myceliophthora verrucosa for enhanced hydrolysis of lignocellulosic biomass	Sharma G; Kaur B; Singh V; Raheja Y; Falco MD; Tsang A; Chadha BS;	38676717 CSFG
7	A thermostable and inhibitor resistant β-glucosidase from Rasamsonia emersonii for efficient hydrolysis of lignocellulosics biomass	Raheja Y; Singh V; Sharma G; Tsang A; Chadha BS;	38470501 CSFG
8	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
9	Economizing the lignocellulosic hydrolysis process using heterologously expressed auxiliary enzymes feruloyl esterase D (CE1) and β-xylosidase (GH43) derived from thermophilic fungi Scytalidium thermophilum	Agrawal D; Tsang A; Chadha BS;	34293687 CSFG
10	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
11	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
12	Evaluation of secretome of highly efficient lignocellulolytic Penicillium sp. Dal 5 isolated from rhizosphere of conifers.	Rai R, Kaur B, Singh S, Di Falco M, Tsang A, Chadha BS	27341464 CSFG
13	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
14	Thermostable xylanases from thermophilic fungi and bacteria: Current perspective.	Chadha BS, Kaur B, Basotra N, Tsang A, Pandey A	30679061 CSFG
15	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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