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

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: Lu Bai, Jonghoon Kim, Kwang-Hee Son, Chung-Wook Chung, Dong-Ha Shin, Bon-Hwan Ku, Do Young Kim, Ho-Yong Park
Formato: article
Lenguaje:EN
Publicado: MDPI AG 2021
Materias:
<i>Cellulosimicrobium funkei</i>
intestinal symbiont
<i>Eisenia fetida</i>
GH19
endo-type chitinase
Microbiology
QR1-502
Acceso en línea:https://doaj.org/article/8cbd2bdeabee41dcbcd20144eb13069a
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spelling oai:doaj.org-article:8cbd2bdeabee41dcbcd20144eb13069a2021-11-25T16:54:39ZNovel Bi-Modular GH19 Chitinase with Broad pH Stability from a Fibrolytic Intestinal Symbiont of <i>Eisenia fetida</i>, <i>Cellulosimicrobium funkei</i> HY-1310.3390/biom111117352218-273Xhttps://doaj.org/article/8cbd2bdeabee41dcbcd20144eb13069a2021-11-01T00:00:00Zhttps://www.mdpi.com/2218-273X/11/11/1735https://doaj.org/toc/2218-273XEndo-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.Lu BaiJonghoon KimKwang-Hee SonChung-Wook ChungDong-Ha ShinBon-Hwan KuDo Young KimHo-Yong ParkMDPI AGarticle<i>Cellulosimicrobium funkei</i>intestinal symbiont<i>Eisenia fetida</i>GH19endo-type chitinaseMicrobiologyQR1-502ENBiomolecules, Vol 11, Iss 1735, p 1735 (2021)
institution DOAJ
collection DOAJ
language EN
topic <i>Cellulosimicrobium funkei</i>
intestinal symbiont
<i>Eisenia fetida</i>
GH19
endo-type chitinase
Microbiology
QR1-502
spellingShingle <i>Cellulosimicrobium funkei</i>
intestinal symbiont
<i>Eisenia fetida</i>
GH19
endo-type chitinase
Microbiology
QR1-502
Lu Bai
Jonghoon Kim
Kwang-Hee Son
Chung-Wook Chung
Dong-Ha Shin
Bon-Hwan Ku
Do Young Kim
Ho-Yong Park
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
description 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.
format article
author Lu Bai
Jonghoon Kim
Kwang-Hee Son
Chung-Wook Chung
Dong-Ha Shin
Bon-Hwan Ku
Do Young Kim
Ho-Yong Park
author_facet Lu Bai
Jonghoon Kim
Kwang-Hee Son
Chung-Wook Chung
Dong-Ha Shin
Bon-Hwan Ku
Do Young Kim
Ho-Yong Park
author_sort Lu Bai
title 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
title_short 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
title_full 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
title_fullStr 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
title_full_unstemmed 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
title_sort 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
publisher MDPI AG
publishDate 2021
url https://doaj.org/article/8cbd2bdeabee41dcbcd20144eb13069a
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