Keyword search (4,163 papers available)

"Hydrolysis" Keyword-tagged Publications:

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 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
4 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
5 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
6 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
7 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
8 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
9 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
10 Mycothermus thermophilus (Syn. Scytalidium thermophilum): Repertoire of a diverse array of efficient cellulases and hemicellulases in the secretome revealed Neha Basotra 27744242
CSFG
11 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

 

Title:Expression of catalytically efficient xylanases from thermophilic fungus Malbranchea cinnamomea for synergistically enhancing hydrolysis of lignocellulosics.
Authors:Basotra NJoshi SSatyanarayana TPati PKTsang AChadha BS
Link:https://www.ncbi.nlm.nih.gov/pubmed/29174359?dopt=Abstract
DOI:10.1016/j.ijbiomac.2017.11.131
Publication:International journal of biological macromolecules
Keywords:Cellic CTec2Enhanced hydrolysisExpressionGH11)Malbranchea cinnamomeaPichia pastorisSynergismXylanase (GH10
PMID:29174359 Category:Int J Biol Macromol Date Added:2019-06-07
Dept Affiliation: CSFG
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]





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