Novel bi-modular GH19 chitinase with broad pH stability from a fibrolytic intestinal symbiont of Eisenia fetida, Cellulosimicrobium funkei HY-13

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Title
Novel bi-modular GH19 chitinase with broad pH stability from a fibrolytic intestinal symbiont of Eisenia fetida, Cellulosimicrobium funkei HY-13
Author(s)
Lu Bai; Jonghoon KimKwang-Hee Son; C W Chung; D H Shin; B H Ku; Do Young KimHo Yong Park
Bibliographic Citation
Biomolecules, vol. 11, no. 11, pp. 1735-1735
Publication Year
2021
Abstract
Endo-type chitinase is the principal enzyme involved in the breakdown of N-acetyl-Dglucosamine-based oligomeric and polymeric materials through hydrolysis. The gene (966-bp) encoding a novel endo-type chitinase (ChiJ), which is comprised of an N-terminal chitin-binding domain type 3 and a C-terminal catalytic glycoside hydrolase family 19 domain, was identified from a fibrolytic intestinal symbiont of the earthworm Eisenia fetida, Cellulosimicrobium funkei HY-13. The highest endochitinase activity of the recombinant enzyme (rChiJ: 30.0 kDa) toward colloidal shrimp shell chitin was found at pH 5.5 and 55 °C and was considerably stable in a wide pH range (3.5-11.0). The enzyme exhibited the highest biocatalytic activity (338.8 U/mg) toward ethylene glycol chitin, preferentially degrading chitin polymers in the following order: ethylene glycol chitin > colloidal shrimp shell chitin > colloidal crab shell chitin. The enzymatic hydrolysis of N-acetyl-β-Dchitooligosaccharides with a degree of polymerization from two to six and colloidal shrimp shell chitin yielded primarily N,N′-diacetyl-β-D-chitobiose together with a small amount of N-acetyl-Dglucosamine. The high chitin-degrading ability of inverting rChiJ with broad pH stability suggests that it can be exploited as a suitable biocatalyst for the preparation of N,N′-diacetyl-β-D-chitobiose, which has been shown to alleviate metabolic dysfunction associated with type 2 diabetes.
Keyword
Cellulosimicrobium funkeiIntestinal symbiontEisenia fetidaGH19Endo-type chitinase
ISSN
2218-273X
Publisher
MDPI
DOI
http://dx.doi.org/10.3390/biom11111735
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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