Enzymatic and molecular characterization of an acidic and thermostable chitinase 1 from <i>Streptomyces thermodiastaticus</i> HF 3-3-Reference-Cited by-同舟云学术

Enzymatic and molecular characterization of an acidic and thermostable chitinase 1 from Streptomyces thermodiastaticus HF 3-3

Published:2018 Issue:4 Volume:64 Page:190-197
ISSN:0022-1260
Container-title:The Journal of General and Applied Microbiology
language:en
Short-container-title:J. Gen. Appl. Microbiol.

Author:

Take Keitaro¹,Fujiki Hidehisa¹,Suyotha Wasana²,Hayashi Junji¹,Takagi Kazuyoshi³,Yano Shigekazu⁴,Wakayama Mamoru¹

Affiliation:

1. Department of Biotechnology, Faculty of Life Sciences, Ritsumeikan University

2. Biotechnology for Bioresource Utilization Laboratory, Department of Industrial Biotechnology, Faculty of Agro-industry, Prince of Songkla University

3. Department of Applied Chemistry, Faculty of Life Sciences, Ritsumeikan University

4. Department of Biochemical Engineering, Graduate School of Sciences and Engineering, Yamagata University

Publisher

Microbiology Research Foundation

Subject

Applied Microbiology and Biotechnology,Microbiology

Link

https://www.jstage.jst.go.jp/article/jgam/64/4/64_2017.12.002/_pdf

Reference23 articles.

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2. Dahiya, N., Tewari, R., and Hoondal, G. S. (2006) Biotechnological aspects of chitinolytic enzymes: a review. Appl. Microbiol. Biotechnol., 71, 773–782.

3. Han, Y., Yang, B., Zhang, F., Miao, X., and Li, Z. (2009) Characterization of antifungal chitinase from marine Streptomyces sp. DA11 associated with South China Sea sponge Craniella australiensis. Mar. Biotechnol., 11, 132–140.

4. Hobel, C. F., Hreggvidsson, G. O., Marteinsson, V. T., Bahrani-Mougeot, F., Einarsson, J. M. et al. (2005) Cloning, expression, and characterization of a highly thermostable family 18 chitinase from Rhodothermus marinus. Extremophiles, 9, 53–64.

5. Kawase, T., Yokokawa, S., Saito, A., Fujii, T., Nikaidou, N. et al. (2006) Comparison of enzymatic and antifungal properties between family 18 and 19 chitinases from S. coelicolor A3(2). Biosci. Biotechnol. Biochem., 70, 988–998.

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