Novel Bi-Modular GH19 Chitinase with Broad pH Stability from a Fibrolytic Intestinal Symbiont of <i>Eisenia fetida</i>, <i>Cellulosimicrobium funkei</i> HY-13
Endo-type chitinase is the principal enzyme involved in the breakdown of <i>N</i>-acetyl-<span style="font-variant: small-caps;">d</span>-glucosamine-based oligomeric and polymeric materials through hydrolysis. The gene (966-bp) encoding a novel endo-type chitinase...
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| Autores principales: | , , , , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
MDPI AG
2021
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/8cbd2bdeabee41dcbcd20144eb13069a |
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| Sumario: | Endo-type chitinase is the principal enzyme involved in the breakdown of <i>N</i>-acetyl-<span style="font-variant: small-caps;">d</span>-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 <i>Eisenia fetida</i>, <i>Cellulosimicrobium funkei</i> 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 <i>N</i>-acetyl-β-<span style="font-variant: small-caps;">d</span>-chitooligosaccharides with a degree of polymerization from two to six and colloidal shrimp shell chitin yielded primarily <i>N,N</i><i>′</i>-diacetyl-β-<span style="font-variant: small-caps;">d</span>-chitobiose together with a small amount of <i>N</i>-acetyl-<span style="font-variant: small-caps;">d</span>-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 <i>N,N</i><i>′</i>-diacetyl-β-<span style="font-variant: small-caps;">d</span>-chitobiose, which has been shown to alleviate metabolic dysfunction associated with type 2 diabetes. |
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