ArticleScientific reports2017
Protease resistance of porcine acidic mammalian chitinase under gastrointestinal conditions implies that chitin-containing organisms can be sustainable dietary resources.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 34 citations in OpenAlex.
- Hologenomic rewiring facilitates dietary adaptation to chitin-rich marine resources in the crab-eating frog.Frontiers in zoology · 2026Article
- Review
- The Biological Functions of Yeast and Yeast Derivatives and Their Application in Swine Production: A Review.Microorganisms · 2025Review
- Hyperactivation of human acidic chitinase (Chia) for potential medical use.The Journal of biological chemistry · 2025Article
- Host gastric corpus microenvironment facilitates Ascaris suum larval hatching and infection in a murine model.PLoS neglected tropical diseases · 2024Article
- The gastric mucosa of Atlantic salmon (Salmo salar) is abundant in highly active chitinases.FEBS open bio · 2024Article
- Endogenous chitinase might lead to differences in growth performance and intestinal health of piglets fed different levels of black soldier fly larva meal.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2023Article
- Evolutionary activation of acidic chitinase in herbivores through the H128R mutation in ruminant livestock.iScience · 2023Article
- Exploring the Differential Expression of a Set of Key Genes Involved in the Regulation and Functioning of the Stomach in the Post-Weaned Pig.Veterinary sciences · 2023Article
- Gene family expansion and functional diversification of chitinase and chitin synthase genes in Atlantic salmon (Salmo salar).G3 (Bethesda, Md.) · 2023Article
- Chitinase-Assisted Bioconversion of Chitinous Waste for Development of Value-Added Chito-Oligosaccharides Products.Biology · 2023Review
- Growth and Welfare of Rainbow Trout (Animals : an open access journal from MDPI · 2022Article
- Crab-Eating Monkey Acidic Chitinase (CHIA) Efficiently Degrades Chitin and Chitosan under Acidic and High-Temperature Conditions.Molecules (Basel, Switzerland) · 2022Article
- Noninsect-Based Diet Leads to Structural and Functional Changes of Acidic Chitinase in Carnivora.Molecular biology and evolution · 2022Article
- Mouse Acidic Chitinase Effectively Degrades Random-Type Chitosan to Chitooligosaccharides of Variable Lengths under Stomach and Lung Tissue pH Conditions.Molecules (Basel, Switzerland) · 2021Article
- Robust chitinolytic activity of crab-eating monkey (Macaca fascicularis) acidic chitinase under a broad pH and temperature range.Scientific reports · 2021Article
- Piglets can secrete acidic mammalian chitinase from the pre weaning stage.Scientific reports · 2021Article
- Residues of acidic chitinase cause chitinolytic activity degrading chitosan in porcine pepsin preparations.Scientific reports · 2019Article
- High expression of acidic chitinase and chitin digestibility in the stomach of common marmoset (Callithrix jacchus), an insectivorous nonhuman primate.Scientific reports · 2019Article
- Acidic mammalian chitinase gene is highly expressed in the special oxyntic glands ofFEBS open bio · 2018Article
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chitin, a polymer of N-acetyl-D-glucosamine (GlcNAc), is a major structural component in chitin-containing organism including crustaceans, insects and fungi. Mammals express two chitinases, chitotriosidase (Chit1) and acidic mammalian chitinase (AMCase). Here, we report that pig AMCase is stable in the presence of other digestive proteases and functions as chitinolytic enzyme under the gastrointestinal conditions. Quantification of chitinases expression in pig tissues using quantitative real-time PCR showed that Chit1 mRNA was highly expressed in eyes, whereas the AMCase mRNA was predominantly expressed in stomach at even higher levels than the housekeeping genes. AMCase purified from pig stomach has highest activity at pH of around 2-4 and remains active at up to pH 7.0. It was resistant to robust proteolytic activities of pepsin at pH 2.0 and trypsin and chymotrypsin at pH 7.6. AMCase degraded polymeric chitin substrates including mealworm shells to GlcNAc dimers. Furthermore, we visualized chitin digestion of fly wings by endogenous AMCase and pepsin in stomach extract. Thus, pig AMCase can function as a protease resistant chitin digestive enzyme at broad pH range present in stomach as well as in the intestine. These results indicate that chitin-containing organisms may be a sustainable feed ingredient in pig diet.
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