Thermostable xylanases from thermophilic fungi and bacteria: Current perspective

被引:105
作者
Chadha, B. S. [1 ]
Kaur, Baljit [1 ]
Basotra, Neha [1 ]
Tsang, Adrian [2 ]
Pandey, Ashok [3 ]
机构
[1] Guru Nanak Dev Univ, Dept Microbiol, Amritsar 143005, Punjab, India
[2] Concordia Univ, Ctr Struct & Funct Genom, Sherbrooke St West, Montreal, PQ H4B 1R6, Canada
[3] Indian Inst Toxicol Res, CSIR, Ctr Innovat & Translat Res, Lucknow 226001, Uttar Pradesh, India
关键词
Thermophilic fungi and bacteria; Thermostable xylanases; Glycoside hydrolases; Genomics and metagenomics; Enzyme production; THERMOMYCES-LANUGINOSUS; MELANOCARPUS-ALBOMYCES; MYCELIOPHTHORA-THERMOPHILA; MALBRANCHEA-CINNAMOMEA; APPLICATION POTENTIALS; CATALYTIC-PROPERTIES; GLYCOSYL HYDROLASES; STRUCTURAL-ANALYSIS; HYPER-PRODUCTION; GH10; XYLANASE;
D O I
10.1016/j.biortech.2019.01.044
中图分类号
S2 [农业工程];
学科分类号
0828 ;
摘要
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.
引用
收藏
页码:195 / 203
页数:9
相关论文
共 105 条
[1]   Effect of Aspergillus niger xylanase on dough characteristics and bread quality attributes [J].
Ahmad, Zulfiqar ;
Butt, Masood Sadiq ;
Ahmed, Anwaar ;
Riaz, Muhammad ;
Sabir, Syed Mubashar ;
Farooq, Umar ;
Rehman, Fazal Ur .
JOURNAL OF FOOD SCIENCE AND TECHNOLOGY-MYSORE, 2014, 51 (10) :2445-2453
[2]   Characterization and high-quality draft genome sequence of Herbivorax saccincola A7, an anaerobic, alkaliphilic, thermophilic, cellulolytic, and xylanolytic bacterium [J].
Aikawa, Shimpei ;
Baramee, Sirilak ;
Sermsathanaswadi, Junjarus ;
Thianheng, Phakhinee ;
Tachaapaikoon, Chakrit ;
Shikata, Ayumi ;
Waeonukul, Rattiya ;
Pason, Patthra ;
Ratanakhanokchai, Khanok ;
Kosugi, Akihiko .
SYSTEMATIC AND APPLIED MICROBIOLOGY, 2018, 41 (04) :261-269
[3]  
AL-Darkazali H, 2017, INT J MICROBIOL, V2017, DOI 10.1155/2017/4018398
[4]   Phylogenetic analysis of β-xylanase SRXL1 of Sporisorium reilianum and its relationship with families (GH10 and GH11) of Ascomycetes and Basidiomycetes [J].
Alvarez-Cervantes, Jorge ;
Diaz-Godinez, Gerardo ;
Mercado-Flores, Yuridia ;
Gupta, Vijai Kumar ;
Anducho-Reyes, Miguel Angel .
SCIENTIFIC REPORTS, 2016, 6
[5]   Characterization of a purified thermostable xylanase from Caldicoprobacter algeriensis sp nov strain TH7C1T [J].
Amel, Bouanane-Darenfed ;
Nawel, Boucherba ;
Khelifa, Bouacem ;
Mohammed, Gagaoua ;
Manon, Joseph ;
Salima, Kebbouche-Gana ;
Farida, Nateche ;
Hocine, Hacene ;
Bernard, Ollivier ;
Jean-Luc, Cayol ;
Marie-Laure, Fardeau .
CARBOHYDRATE RESEARCH, 2016, 419 :60-68
[6]   Characterization of a thermostable, specific GH10 xylanase from Caldicellulosiruptor bescii with high catalytic activity [J].
An, Jiao ;
Xie, Yuan ;
Zhang, Yong ;
Tian, Dongsheng ;
Wang, Shuhao ;
Yang, Guangyu ;
Feng, Yan .
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2015, 117 :13-20
[7]   High stability and low competitive inhibition of thermophilic Thermopolyspora flexuosa GH10 xylanase in biomass-dissolving ionic liquids [J].
Anbarasan, Sasikala ;
Wahlstrom, Ronny ;
Hummel, Michael ;
Ojamo, Heikki ;
Sixta, Herbert ;
Turunen, Ossi .
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2017, 101 (04) :1487-1498
[8]   Production of multiple xylanolytic and cellulolytic enzymes by thermophilic fungus Myceliophthora sp IMI 387099 [J].
Badhan, A. K. ;
Chadha, B. S. ;
Kaur, Jatinder ;
Saini, H. S. ;
Bhat, M. K. .
BIORESOURCE TECHNOLOGY, 2007, 98 (03) :504-510
[9]   Functionally diverse multiple xylanases of thermophilic fungus Myceliophthora sp IMI 387099 [J].
Badhan, AK ;
Chadha, BS ;
Sonia, KG ;
Saini, HS ;
Bhat, MK .
ENZYME AND MICROBIAL TECHNOLOGY, 2004, 35 (05) :460-466
[10]   A new crystal form of XT6 enables a significant improvement of its diffraction quality and resolution [J].
Bar, M ;
Golan, G ;
Nechama, MA ;
Zolotnitsky, G ;
Shoham, Y ;
Shoham, G .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2004, 60 :545-549