Optimization of Chitinase Production by the Photobacterium sp. LG-1

被引:0
|
作者
Chen L.-G. [1 ,2 ]
Wu J.-W. [1 ,2 ]
Zhang R. [1 ,2 ]
Zhang Q.F. [1 ,2 ]
Chi N.Y. [1 ,2 ]
Wang X.H. [1 ,2 ]
机构
[1] School of Life Science and Biotechnology, Dalian University, Dalian
[2] Liaoning Marine Microbial Engineering Technology Research Center, Dalian
关键词
chitinase; optimization of fermentation conditions; Photobacterium; response surface methodology;
D O I
10.13386/j.issn1002-0306.2019120161
中图分类号
学科分类号
摘要
To increase chitinase activity, response surface metliodology was used to optimize the fermentation conditions of cold -adapted chitinase by Photobacterium sp.LG-1.The result of Placket-Burman showed that the important factors influencing chitinase production were fermentation temperature, fermentation time and yeast extract. The optimal fermentation conditions were determined as followed: colloidal chitin 12.0 g/L, yeast extract 4.5 g/L, shaking speed 220 r/min, fermentation temperature 20 °C, liquid volume 75 mL/250 mL,inoculums dose 1% " pH7.0"and fermentation time 120 h,respectively. Under these conditions, the max enzyme activity of chitinase was 5.10 U/mL.The maximum theoretic value was consistent with mean value of verification test and the chitinase production was increased by 11.50% comparing to that before optimization.lt provides a reference for the research on the degradation mechanism of low - temperature chitinase and its application in industry. © The Author(s) 2021.
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页码:110 / 114and131
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共 28 条
  • [1] Paszota P, Escalante-Perez M, Thomsen LR, Et al., Secreted major Venus flytrap chitinase enables digestion of arthropod prey [J], Biochim Biophys Acta, 1844, pp. 373-383, (2014)
  • [2] Batista Jtao Adelina B, Gifoni Juliana M, Pereira Mirella L, Et al., New insights into the structure and mode of action of Mo - CBP3, an antifungal chitin - binding protein of Moringa oleifera seeds, PloS One, 9, pp. 1-9, (2014)
  • [3] Gao L, Sun J, Secundo F, Et al., Cloning, characterization and substrate degradation mode of a novel chitinase from Streptomyces albolongus ATCC 27414, Food Chemistry, 261, pp. 329-336, (2018)
  • [4] Wang D, Li A, Han H, Et al., A potent chitinase from, Baciilus ssbtilis, for the efficient bioconversion of chitin-containing wastes [J], International Journal of Biological Macromolecules, (2018)
  • [5] Woltje M, Bobel M, Rheinnecker M, Et al., Transgenic protein production in silkworm silk glands requires cathepsin and chitinase of Autographa California multicapsid nucleopolyhedrovirus [J], Appl Microbiol Biotechnol, 98, pp. 4571-4580, (2014)
  • [6] Shiladitya D S, Capes M D, Ram K, Et al., Amino acid substitutions in cold - adapted proteins from Halorubrum lacusppofondi, an extremely halophilic microbe from Antarctica [J], PLoS ONE, 8, 3, pp. 587-592, (2013)
  • [7] Gurav R, Tang J, Jadhav J., Novel chitinase producer, Bacillus pumilus, RST25 isolated from the shellfish processing industry revealed antifungal potential against phyto - pathogens, International Biodeterioration & Biodegradation, 125, pp. 228-234, (2017)
  • [8] Frederiksen R. F, Paspaliari D. K, Larsen T, Et al., Bacterial chitinases and chitin - binding proteins as virulence factors [J], Microbiology, 159, pp. 833-847, (2013)
  • [9] Nagpure A, Choudhary B, Gupta R K., Chitinases : In agriculture and human healthcare [J], Critical Reviews in Biotechnology, 34, pp. 215-232, (2014)
  • [10] Jankiewicz U, Brzezinska M S., Purification, characterization, and gene cloning of a chitinase from Steptrophomonas maltophilia N4, Journal of Basic Microbiology, 55, 6, pp. 709-717, (2015)