ArticleScientific reports2019
Residues of acidic chitinase cause chitinolytic activity degrading chitosan in porcine pepsin preparations.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Heterogeneously deacetylated chitosans possess an unexpected regular pattern favoring acetylation at every third position.Nature communications · 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
- Gene family expansion and functional diversification of chitinase and chitin synthase genes in Atlantic salmon (Salmo salar).G3 (Bethesda, Md.) · 2023Article
- Irreversible evolutionary loss of chitin-degrading ability in the chitinase-like protein Ym1 under positive selection in rodents.Protein science : a publication of the Protein Society · 2023Article
- Chitinase-Assisted Bioconversion of Chitinous Waste for Development of Value-Added Chito-Oligosaccharides Products.Biology · 2023Review
- 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
- The Antifungal Action Mode ofMolecules (Basel, Switzerland) · 2021Article
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7 authors.
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Abstract
Commercially available porcine pepsin preparations have been used for the production of chitooligosaccharides with various biomedical activities. However, the origin of this activity is not well understood. Here we show that the chitosan-degrading activity is conferred by residues with chitinolytic activity of truncated forms of acidic chitinase (Chia) persisting in the pepsin preparation. Chia is an acid-stable and pepsin-resistant enzyme that degrades chitin to produce N-acetyl-D-glucosamine dimer. We found that Chia can be truncated by pepsin under stomach-like conditions while maintaining its enzymatic activity. Similarly to the full-length protein, truncated Chia as well as the pepsin preparations digested chitosan with different degrees of deacetylation (DD: 69-84%) with comparable degradation products. The efficiency was DD-dependent with a marked decrease with higher DD, indicating that the chitosan-degrading activity in the pepsin preparation is due to the chitinolytic activity rather than chitosanolytic activity. We suggest that natural or recombinant porcine Chia are suitable for producing chitooligosaccharides for biomedical purposes.
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