Keyword search (4,163 papers available)

"Basotra N" Authored Publications:

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:Expression of catalytically efficient xylanases from thermophilic fungus Malbranchea cinnamomea for synergistically enhancing hydrolysis of lignocellulosics.
Authors:Basotra N,  Joshi S,  Satyanarayana T,  Pati PK,  Tsang A,  Chadha 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 CTec2;  Enhanced hydrolysis;  Expression;  GH11);  Malbranchea cinnamomea;  Pichia pastoris;  Synergism;  Xylanase (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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