Residues of acidic chitinase cause chitinolytic activity degrading chitosan in porcine pepsin preparations
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00023884%3A_____%2F19%3A00008551" target="_blank" >RIV/00023884:_____/19:00008551 - isvavai.cz</a>
Result on the web
<a href="https://www.nature.com/articles/s41598-019-52136-2" target="_blank" >https://www.nature.com/articles/s41598-019-52136-2</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41598-019-52136-2" target="_blank" >10.1038/s41598-019-52136-2</a>
Alternative languages
Result language
angličtina
Original language name
Residues of acidic chitinase cause chitinolytic activity degrading chitosan in porcine pepsin preparations
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
30102 - Immunology
Result continuities
Project
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Continuities
N - Vyzkumna aktivita podporovana z neverejnych zdroju
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Scientific Reports
ISSN
2045-2322
e-ISSN
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Volume of the periodical
9
Issue of the periodical within the volume
October
Country of publishing house
GB - UNITED KINGDOM
Number of pages
11
Pages from-to
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UT code for WoS article
000493276600040
EID of the result in the Scopus database
2-s2.0-85074272945