Direct comparison of chitinolytic properties and determination of combinatory effects of mouse chitotriosidase and acidic mammalian chitinase

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00023884%3A_____%2F19%3A00008253" target="_blank" >RIV/00023884:_____/19:00008253 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0141813019318008" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0141813019318008</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.ijbiomac2019.05.097" target="_blank" >10.1016/j.ijbiomac2019.05.097</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Direct comparison of chitinolytic properties and determination of combinatory effects of mouse chitotriosidase and acidic mammalian chitinase

Popis výsledku v původním jazyce

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 Chitl and AMCase and determined their combinatory effects in artificial and natural chitin substrates processing. Chitl and AMCase display different dynamics of chitinolytic properties through acidic to neutral conditions. At pH 2.0, the activity of AMCase was higher than that of Chitl 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 Chitl 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 Chitl and AMCase have no synergistic effect under physiological conditions. (C) 2019 The Authors. Published by Elsevier B.V.

Název v anglickém jazyce

Direct comparison of chitinolytic properties and determination of combinatory effects of mouse chitotriosidase and acidic mammalian chitinase

Popis výsledku anglicky

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 Chitl and AMCase and determined their combinatory effects in artificial and natural chitin substrates processing. Chitl and AMCase display different dynamics of chitinolytic properties through acidic to neutral conditions. At pH 2.0, the activity of AMCase was higher than that of Chitl 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 Chitl 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 Chitl and AMCase have no synergistic effect under physiological conditions. (C) 2019 The Authors. Published by Elsevier B.V.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

30101 - Human genetics

Projekt

—

Návaznosti

N - Vyzkumna aktivita podporovana z neverejnych zdroju

Rok uplatnění

2019

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

International Journal Of Biological Macromolecules

ISSN

0141-8130

e-ISSN

—

Svazek periodika

134

Číslo periodika v rámci svazku

August

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

882-890

Kód UT WoS článku

000474673600093

EID výsledku v databázi Scopus

2-s2.0-85065870501