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Identification of a Novel Chitinase from Bacillus paralicheniformis : Gene Mining, Sequence Analysis, and Enzymatic Characterization.

Authors :
Ma, Xianwen
Zou, Dian
Ji, Anying
Jiang, Cong
Zhao, Ziyue
Ding, Xiaoqi
Han, Zongchen
Bao, Pengfei
Chen, Kang
Ma, Aimin
Wei, Xuetuan
Source :
Foods; Jun2024, Vol. 13 Issue 11, p1777, 14p
Publication Year :
2024

Abstract

In this study, a novel strain for degrading chitin was identified as Bacillus paralicheniformis HL37, and the key chitinase CH1 was firstly mined through recombinant expression in Bacillus amyloliquefaciens HZ12. Subsequently, the sequence composition and catalytic mechanism of CH1 protein were analyzed. The molecular docking indicated that the triplet of Asp526, Asp528, and Glu530 was a catalytic active center. The enzymatic properties analysis revealed that the optimal reaction temperature and pH was 65 °C and 6.0, respectively. Especially, the chitinase activity showed no significant change below 55 °C and it could maintain over 60% activity after exposure to 85 °C for 30 min. Moreover, the optimal host strain and signal peptide were obtained to enhance the expression of chitinase CH1 significantly. As far as we know, it was the first time finding the highly efficient chitin-degrading enzymes in B. paralicheniformis, and detailed explanations were provided on the catalytic mechanism and enzymatic properties on CH1. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
23048158
Volume :
13
Issue :
11
Database :
Complementary Index
Journal :
Foods
Publication Type :
Academic Journal
Accession number :
177854223
Full Text :
https://doi.org/10.3390/foods13111777