Applications of Microbial β-Mannanases.
作者： Aneesa Dawood , Kesen Ma
DOI: 10.3389/FBIOE.2020.598630
关键词: Pulp (paper) 、 Animal feed 、 Pulp and paper industry 、 Biorefinery 、 Chemistry 、 Bacteria 、 Hemicellulose
摘要: Mannans are main components of hemicellulosic fraction softwoods and they present widely in plant tissues. β-mannanases the major mannan-degrading enzymes produced by different plants, animals, actinomycetes, fungi, bacteria. These can function under conditions wide range pH temperature. Applications have therefore, been found industries such as animal feed, food, biorefinery, textile, detergent, paper pulp. This review summarizes most recent studies reported on potential applications bioengineering to modify optimize their key catalytic properties cater growing demands commercial sectors.
frontiersin.org
sci-hub.st 参考文章(114)
Carl J. Yeoman, Yejun Han, Dylan Dodd, Charles M. Schroeder, Roderick I. Mackie, Isaac K.O. Cann, Thermostable Enzymes as Biocatalysts in the Biofuel Industry Advances in Applied Microbiology. ,vol. 70, pp. 1- 55 ,(2010) , 10.1016/S0065-2164(10)70001-0
Yang Wang, Shoaib Azhar, Rosaria Gandini, Christina Divne, Ines Ezcurra, Henrik Aspeborg, Biochemical characterization of the novel endo-β-mannanase AtMan5-2 from Arabidopsis thaliana. Plant Science. ,vol. 241, pp. 151- 163 ,(2015) , 10.1016/J.PLANTSCI.2015.10.002
Haoyu Zang, Shanshan Xie, Huijun Wu, Weiduo Wang, Xiankun Shao, Liming Wu, Faheem Uddin Rajer, Xuewen Gao, A novel thermostable GH5_7 β-mannanase from Bacillus pumilus GBSW19 and its application in manno-oligosaccharides (MOS) production. Enzyme and Microbial Technology. ,vol. 78, pp. 1- 9 ,(2015) , 10.1016/J.ENZMICTEC.2015.06.007
Samkelo Malgas, J. Susan van Dyk, Brett I. Pletschke, A review of the enzymatic hydrolysis of mannans and synergistic interactions between β-mannanase, β-mannosidase and α-galactosidase. World Journal of Microbiology & Biotechnology. ,vol. 31, pp. 1167- 1175 ,(2015) , 10.1007/S11274-015-1878-2
Jia You, Jin-Feng Liu, Shi-Zhong Yang, Bo-Zhong Mu, Low-temperature-active and salt-tolerant β-mannanase from a newly isolated Enterobacter sp. strain N18. Journal of Bioscience and Bioengineering. ,vol. 121, pp. 140- 146 ,(2016) , 10.1016/J.JBIOSC.2015.06.001
Philip J. Harris, Bruce A. Stone, Chemistry and Molecular Organization of Plant Cell Walls Biomass Recalcitrance. pp. 61- 93 ,(2009) , 10.1002/9781444305418.CH4
Ayuub A. Ayoola, Ramon D. Malheiros, Jesse L. Grimes, Peter R. Ferket, Effect of Dietary Exogenous Enzyme Supplementation on Enteric Mucosal Morphological Development and Adherent Mucin Thickness in Turkeys. Frontiers in Veterinary Science. ,vol. 2, pp. 45- 45 ,(2015) , 10.3389/FVETS.2015.00045
L. R. S. Moreira, E. X. F. Filho, An overview of mannan structure and mannan-degrading enzyme systems Applied Microbiology and Biotechnology. ,vol. 79, pp. 165- 178 ,(2008) , 10.1007/S00253-008-1423-4
Hui Zhang, Qing Sang, Production and extraction optimization of xylanase and β-mannanase by Penicillium chrysogenum QML-2 and primary application in saccharification of corn cob Biochemical Engineering Journal. ,vol. 97, pp. 101- 110 ,(2015) , 10.1016/J.BEJ.2015.02.014
Hong Yang, Pengjun Shi, Haiqiang Lu, Huimin Wang, Huiying Luo, Huoqing Huang, Peilong Yang, Bin Yao, None, A thermophilic β-mannanase from Neosartorya fischeri P1 with broad pH stability and significant hydrolysis ability of various mannan polymers Food Chemistry. ,vol. 173, pp. 283- 289 ,(2015) , 10.1016/J.FOODCHEM.2014.10.022