Gastric and intestinal proteases resistance of chicken acidic chitinase nominates chitin-containing organisms for alternative whole edible diets for poultry

Abstract Chitin, a polymer of N-acetyl-D-glucosamine (GlcNAc), functions as a major structural component in crustaceans, insects and fungi and is the second most abundant polysaccharide in the nature. Although these chitin-containing organisms have been suggested as novel animal feed resources, chit...

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Autores principales: Eri Tabata, Akinori Kashimura, Satoshi Wakita, Misa Ohno, Masayoshi Sakaguchi, Yasusato Sugahara, Yoshihiro Kino, Vaclav Matoska, Peter O. Bauer, Fumitaka Oyama
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Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/9c19af425e384cc88b5506bca30a9310
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spelling oai:doaj.org-article:9c19af425e384cc88b5506bca30a93102021-12-02T15:05:33ZGastric and intestinal proteases resistance of chicken acidic chitinase nominates chitin-containing organisms for alternative whole edible diets for poultry10.1038/s41598-017-07146-32045-2322https://doaj.org/article/9c19af425e384cc88b5506bca30a93102017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-07146-3https://doaj.org/toc/2045-2322Abstract Chitin, a polymer of N-acetyl-D-glucosamine (GlcNAc), functions as a major structural component in crustaceans, insects and fungi and is the second most abundant polysaccharide in the nature. Although these chitin-containing organisms have been suggested as novel animal feed resources, chitin has long been considered as indigestible fibers in the animal body. Recently, we reported that acidic chitinase (Chia) is a protease-resistant major glycosidase in mouse gastrointestinal tract (GIT) and that it digests chitin in the mouse stomach. However, the physiological role of Chia in other animals including poultry remains unknown. Here, we report that Chia can function as a digestive enzyme that breaks down chitin-containing organisms in chicken GIT. Chia mRNA is predominantly expressed in the glandular stomach tissue in normal chicken. We also show that chicken Chia has a robust chitinolytic activity at pH 2.0 and is highly resistant to proteolysis by pepsin and trypsin/chymotrypsin under conditions mimicking GIT. Chia degraded shells of mealworm larvae in the presence of digestive proteases and produced (GlcNAc)2. Thus, functional similarity of chicken Chia with the mouse enzyme suggests that chitin-containing organisms can be used for alternative poultry diets not only as whole edible resources but also as enhancers of their nutritional value.Eri TabataAkinori KashimuraSatoshi WakitaMisa OhnoMasayoshi SakaguchiYasusato SugaharaYoshihiro KinoVaclav MatoskaPeter O. BauerFumitaka OyamaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Eri Tabata
Akinori Kashimura
Satoshi Wakita
Misa Ohno
Masayoshi Sakaguchi
Yasusato Sugahara
Yoshihiro Kino
Vaclav Matoska
Peter O. Bauer
Fumitaka Oyama
Gastric and intestinal proteases resistance of chicken acidic chitinase nominates chitin-containing organisms for alternative whole edible diets for poultry
description Abstract Chitin, a polymer of N-acetyl-D-glucosamine (GlcNAc), functions as a major structural component in crustaceans, insects and fungi and is the second most abundant polysaccharide in the nature. Although these chitin-containing organisms have been suggested as novel animal feed resources, chitin has long been considered as indigestible fibers in the animal body. Recently, we reported that acidic chitinase (Chia) is a protease-resistant major glycosidase in mouse gastrointestinal tract (GIT) and that it digests chitin in the mouse stomach. However, the physiological role of Chia in other animals including poultry remains unknown. Here, we report that Chia can function as a digestive enzyme that breaks down chitin-containing organisms in chicken GIT. Chia mRNA is predominantly expressed in the glandular stomach tissue in normal chicken. We also show that chicken Chia has a robust chitinolytic activity at pH 2.0 and is highly resistant to proteolysis by pepsin and trypsin/chymotrypsin under conditions mimicking GIT. Chia degraded shells of mealworm larvae in the presence of digestive proteases and produced (GlcNAc)2. Thus, functional similarity of chicken Chia with the mouse enzyme suggests that chitin-containing organisms can be used for alternative poultry diets not only as whole edible resources but also as enhancers of their nutritional value.
format article
author Eri Tabata
Akinori Kashimura
Satoshi Wakita
Misa Ohno
Masayoshi Sakaguchi
Yasusato Sugahara
Yoshihiro Kino
Vaclav Matoska
Peter O. Bauer
Fumitaka Oyama
author_facet Eri Tabata
Akinori Kashimura
Satoshi Wakita
Misa Ohno
Masayoshi Sakaguchi
Yasusato Sugahara
Yoshihiro Kino
Vaclav Matoska
Peter O. Bauer
Fumitaka Oyama
author_sort Eri Tabata
title Gastric and intestinal proteases resistance of chicken acidic chitinase nominates chitin-containing organisms for alternative whole edible diets for poultry
title_short Gastric and intestinal proteases resistance of chicken acidic chitinase nominates chitin-containing organisms for alternative whole edible diets for poultry
title_full Gastric and intestinal proteases resistance of chicken acidic chitinase nominates chitin-containing organisms for alternative whole edible diets for poultry
title_fullStr Gastric and intestinal proteases resistance of chicken acidic chitinase nominates chitin-containing organisms for alternative whole edible diets for poultry
title_full_unstemmed Gastric and intestinal proteases resistance of chicken acidic chitinase nominates chitin-containing organisms for alternative whole edible diets for poultry
title_sort gastric and intestinal proteases resistance of chicken acidic chitinase nominates chitin-containing organisms for alternative whole edible diets for poultry
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/9c19af425e384cc88b5506bca30a9310
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