Covalent biofunctionalization of chitosan nanofibers with trypsin for high enzyme stability

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216275%3A25310%2F16%3A39901216" target="_blank" >RIV/00216275:25310/16:39901216 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.reactfunctpolym.2016.05.009" target="_blank" >http://dx.doi.org/10.1016/j.reactfunctpolym.2016.05.009</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.reactfunctpolym.2016.05.009" target="_blank" >10.1016/j.reactfunctpolym.2016.05.009</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Covalent biofunctionalization of chitosan nanofibers with trypsin for high enzyme stability

Popis výsledku v původním jazyce

The electrospun chitosan nanofibers provide excellent material for immobilized proteolytic enzymes, and are biocompatible, nontoxic and hydrophilic matrices with large specific area. This paper deals with an application of electrospun chitosan nanofibers and optimizing conditions for their biofunctionalization by model proteolytic enzyme trypsin. Nanofibers fromchitosan were prepared using NanospiderTM technology and covalent immobilization of trypsin followed. Three immobilization techniques preserving biocompatibility and utilizing amine and/or hydroxyl groups of chitosan were optimized and compared to simple adsorption to achieve maximum proteolytic activity per cm2 of the functionalized chitosan nanofibers (Tryp-NF). Significant differences were observed. Trypsin immobilized by the carbodiimide one-step protocol demonstrated the highest activity of the three procedures, ranging from 132 to 210 IU/cm2 (i.e., 548-874 IU/mg of nanofibers), depending on the initial amount of trypsin used. Long-term storage stability together with high reusability of Tryp-NF confirmed advantages of the immobilized enzyme. Tryp-NF showed no cytotoxicity toward growth of HeLa cells. The in vivo tests for irritation and skin sensitization demonstrated no undesirable skin reactions.

Název v anglickém jazyce

Covalent biofunctionalization of chitosan nanofibers with trypsin for high enzyme stability

Popis výsledku anglicky

The electrospun chitosan nanofibers provide excellent material for immobilized proteolytic enzymes, and are biocompatible, nontoxic and hydrophilic matrices with large specific area. This paper deals with an application of electrospun chitosan nanofibers and optimizing conditions for their biofunctionalization by model proteolytic enzyme trypsin. Nanofibers fromchitosan were prepared using NanospiderTM technology and covalent immobilization of trypsin followed. Three immobilization techniques preserving biocompatibility and utilizing amine and/or hydroxyl groups of chitosan were optimized and compared to simple adsorption to achieve maximum proteolytic activity per cm2 of the functionalized chitosan nanofibers (Tryp-NF). Significant differences were observed. Trypsin immobilized by the carbodiimide one-step protocol demonstrated the highest activity of the three procedures, ranging from 132 to 210 IU/cm2 (i.e., 548-874 IU/mg of nanofibers), depending on the initial amount of trypsin used. Long-term storage stability together with high reusability of Tryp-NF confirmed advantages of the immobilized enzyme. Tryp-NF showed no cytotoxicity toward growth of HeLa cells. The in vivo tests for irritation and skin sensitization demonstrated no undesirable skin reactions.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/FR-TI1%2F436" target="_blank" >FR-TI1/436: *Využití nanovlákenných membrán pro řízené uvolňování aktivních látek</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2016

Kód důvěrnosti údajů

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

Název periodika

Reactive and Functional Polymers

ISSN

1381-5148

e-ISSN

—

Svazek periodika

104

Číslo periodika v rámci svazku

květen 2016

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

7

Strana od-do

38-44

Kód UT WoS článku

000379375400006

EID výsledku v databázi Scopus

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