title: Malbranchea cinnamomea: A thermophilic fungal source of catalytically efficient lignocellulolytic glycosyl hydrolases and metal dependent enzymes.
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.
authors.affiliation: Department of Microbiology, Guru Nanak Dev University, Amritsar 143005, Punjab, India. Electronic address: chhaviosho@yahoo.com.
authors.forename: Chhavi
authors.initials: C
authors.lastname: Mahajan
authors.affiliation: Department of Microbiology, Guru Nanak Dev University, Amritsar 143005, Punjab, India. Electronic address: nehabasotra506@gmail.com.
authors.forename: Neha
authors.initials: N
authors.lastname: Basotra
authors.affiliation: Division of Microbiology, ICAR-Indian Agricultural Research Institute, New Delhi, India. Electronic address: ssriari@gmail.com.
authors.forename: Surender
authors.initials: S
authors.lastname: Singh
authors.affiliation: Centre for Structural and Functional Genomics, Concordia University, 7141 Sherbrooke Street West, Montréal, Québec H4B 1R6, Canada. Electronic address: marcos.difalco@concordia.ca.
authors.forename: Marcos
authors.initials: M
authors.lastname: Di Falco
authors.affiliation: Centre for Structural and Functional Genomics, Concordia University, 7141 Sherbrooke Street West, Montréal, Québec H4B 1R6, Canada. Electronic address: adrian.tsang@concordia.ca.
authors.forename: Adrian
authors.initials: A
authors.lastname: Tsang
authors.affiliation: Department of Microbiology, Guru Nanak Dev University, Amritsar 143005, Punjab, India. Electronic address: chadhabs@yahoo.com.
authors.forename: B S
authors.initials: BS
authors.lastname: Chadha
mesh_terms: D019659:Asteraceae / Q000737:chemistry / Q000378:metabolism*; D002237:Carbohydrate Dehydrogenases / Q000737:chemistry / Q000378:metabolism; D002384:Catalysis; D002480:Cellulase / Q000737:chemistry / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000378:metabolism*; D006868:Hydrolysis; D008670:Metals / Q000378:metabolism; D020036:Onygenales / Q000201:enzymology*; D057685:Plant Weeds / Q000737:chemistry / Q000378:metabolism; D053719:Tandem Mass Spectrometry
chemical_list: D005656:Fungal Proteins; D008670:Metals; D002237:Carbohydrate Dehydrogenases; C019859:cellobiose-quinone oxidoreductase; D006026:Glycoside Hydrolases; C023305:hemicellulase; D002480:Cellulase
keywords: Cellobiose dehydrogenase; Glycosyl hydrolases; Ion exchange chromatography; M. cinnamomea; Secretome