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:Thermostable xylanases from thermophilic fungi and bacteria: Current perspective.
Authors:Chadha BS,  Kaur B,  Basotra N,  Tsang A,  Pandey A
Link:https://www.ncbi.nlm.nih.gov/pubmed/30679061?dopt=Abstract
DOI:10.1016/j.biortech.2019.01.044
Publication:Bioresource technology
Keywords:Enzyme production;  Genomics and metagenomics;  Glycoside hydrolases;  Thermophilic fungi and bacteria;  Thermostable xylanases; 
PMID:30679061 Category:Bioresour Technol Date Added:2019-06-07
Dept Affiliation: CSFG
1 Department of Microbiology, Guru Nanak Dev University, Amritsar 143 005, India. Electronic address: chadhabs@yahoo.com.
2 Department of Microbiology, Guru Nanak Dev University, Amritsar 143 005, India.
3 Center for Structural and Functional Genomics, Concordia University, Sherbrooke Street West, Montreal, Quebec H4B 1R6, Canada. Electronic address: adrian.tsang@concordia.ca.
4 Centre for Innovation and Translational Research, CSIR-Indian Institute of Toxicology Research, Lucknow 226 001, India. Electronic address: ashok.pandey1@iitr.res.in.

Description:

Thermostable xylanases from thermophilic fungi and bacteria: Current perspective.

Bioresour Technol. 2019 Apr;277:195-203

Authors: Chadha BS, Kaur B, Basotra N, Tsang A, Pandey A

Abstract

Thermostable xylanases from thermophilic fungi and bacteria have a wide commercial acceptability in feed, food, paper and pulp and bioconversion of lignocellulosics with an estimated annual market of USD 500 Million. The genome wide analysis of thermophilic fungi clearly shows the presence of elaborate genetic information coding for multiple xylanases primarily coding for GH10, GH11 in addition to GH7 and GH30 xylanases. The transcriptomics and proteome profiling has given insight into the differential expression of these xylanases in some of the thermophilic fungi. Bioprospecting has resulted in identification of novel thermophilic xylanases that have been endorsed by the industrial houses for heterologous over- expression and formulations. The future use of xylanases is expected to increase exponentially for their role in biorefineries. The discovery of new and improvement of existing xylanases using molecular tools such as directed evolution is expected to be the mainstay to meet increasing demand of thermostable xylanases.

PMID: 30679061 [PubMed - in process]




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