Direct comparison of chitinolytic properties and determination of combinatory effects of mouse chitotriosidase and acidic mammalian chitinase
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články
PubMed
31108147
DOI
10.1016/j.ijbiomac.2019.05.097
PII: S0141-8130(19)31800-8
Knihovny.cz E-zdroje
- Klíčová slova
- Acidic mammalian chitinase, Chitin substrates, Chitotriosidase, Direct comparison, Mutual effects, Serratia marcescens chitinase B,
- MeSH
- bakteriální proteiny chemie genetika MeSH
- chitin chemie MeSH
- chitinasy chemie genetika MeSH
- hexosaminidasy chemie MeSH
- hydrolýza MeSH
- kolorimetrie MeSH
- koncentrace vodíkových iontů MeSH
- molekulová hmotnost MeSH
- myši MeSH
- rekombinantní proteiny MeSH
- substrátová specifita MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- bakteriální proteiny MeSH
- chitin MeSH
- chitinase B, Serratia marcescens MeSH Prohlížeč
- chitinasy MeSH
- chitotriosidase MeSH Prohlížeč
- hexosaminidasy MeSH
- rekombinantní proteiny MeSH
Chitotriosidase (Chit1) and acidic mammalian chitinase (AMCase) have been implicated in food processing and various pathophysiological conditions such as chronic inflammatory diseases. By combination of the colorimetric analysis and fluorophore-assisted carbohydrate electrophoresis (FACE) method, we directly compared the chitinolytic properties of mouse Chit1 and AMCase and determined their combinatory effects in artificial and natural chitin substrates processing. Chit1 and AMCase display different dynamics of chitinolytic properties through acidic to neutral conditions. At pH2.0, the activity of AMCase was higher than that of Chit1 and stronger or comparable with that of Serratia marcescens chitinase B, a well-characterized bacterium chitinase. Changes of degradation products using different substrates indicate that AMCase and Chit1 have diverse properties under various pH conditions. Exposure of the chitin substrates to both Chit1 and AMCase did not indicate any mutual interference of these enzymes and showed no synergistic effect, in contrast to observations regarding some bacterial chitinases. Our results suggest that Chit1 and AMCase have no synergistic effect under physiological conditions.
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