Novel Bi-Modular GH19 Chitinase with Broad pH Stability from a Fibrolytic Intestinal Symbiont of Eisenia fetida, Cellulosimicrobium funkei HY-13
Autor: | Ho-Yong Park, Dong-Ha Shin, Kwang-Hee Son, Jonghoon Kim, Bon-Hwan Ku, Lu Bai, Do Young Kim, Chung-Wook Chung |
---|---|
Jazyk: | angličtina |
Rok vydání: | 2021 |
Předmět: |
Eisenia fetida
Endochitinase activity endo-type chitinase macromolecular substances medicine.disease_cause Biochemistry Microbiology Article Cellulosimicrobium funkei intestinal symbiont GH19 chemistry.chemical_compound Hydrolysis Chitin Enzymatic hydrolysis medicine Animals Oligochaeta Molecular Biology Glycoside hydrolase family 19 biology Chitinases fungi biology.organism_classification QR1-502 Actinobacteria chemistry Diabetes Mellitus Type 2 Chitinase biology.protein |
Zdroj: | Biomolecules; Volume 11; Issue 11; Pages: 1735 Biomolecules, Vol 11, Iss 1735, p 1735 (2021) Biomolecules |
ISSN: | 2218-273X |
DOI: | 10.3390/biom11111735 |
Popis: | Endo-type chitinase is the principal enzyme involved in the breakdown of N-acetyl-d-glucosamine-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-d-chitooligosaccharides 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-d-glucosamine. 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. |
Databáze: | OpenAIRE |
Externí odkaz: |