Effective lipase immobilization on crosslinked functional porous polypyrrole aggregates

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F23%3A43927950" target="_blank" >RIV/60461373:22340/23:43927950 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22310/23:43927950

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0927775723004466?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0927775723004466?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.colsurfa.2023.131362" target="_blank" >10.1016/j.colsurfa.2023.131362</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Effective lipase immobilization on crosslinked functional porous polypyrrole aggregates

Popis výsledku v původním jazyce

Enzyme immobilization is an efficient and growing method for the stabilization, separation and reutilization of the expensive and hard-to-extract enzymes used in industrial biocatalysts. A 3D porous functionalized polypyrrole (PPy) material is designed with superior properties for improved performance of covalently immobilized model enzymes. This was uniquely achieved by choosing biodegradable carboxymethylcellulose (CMC) crosslinker of different molecular weights (Mw) to alter the strength of porous aggregates. The ensemble-averaged aggregates radius of gyration 〈Rg〉 increased monotonically almost three-fold with crosslinkers’ Mw along with an open structure formation compared to phytic acid crosslinked aggregates. This improvement was connected with more than a 20-fold increase in adsorbed N2 and a resulting increase in the specific surface area for aggregates crosslinked with CMC compared to phytic acid counterparts. A larger number of COOH groups on the CMC surface combined with optimal pore size achieved with its decreasing Mw facilitated the enzymes’ free diffusion to the functional groups and their retention. The phenomena further allowed a larger fraction of covalent bond formation of enzyme-substrate, resulting in higher specific activity and stability for Candida rugosa and Candida Antarctica, found in commercial biocatalysts, which will guide the formation of improved biocatalysts on porous polymer supports in the future. © 2023 Elsevier B.V.

Název v anglickém jazyce

Effective lipase immobilization on crosslinked functional porous polypyrrole aggregates

Popis výsledku anglicky

Enzyme immobilization is an efficient and growing method for the stabilization, separation and reutilization of the expensive and hard-to-extract enzymes used in industrial biocatalysts. A 3D porous functionalized polypyrrole (PPy) material is designed with superior properties for improved performance of covalently immobilized model enzymes. This was uniquely achieved by choosing biodegradable carboxymethylcellulose (CMC) crosslinker of different molecular weights (Mw) to alter the strength of porous aggregates. The ensemble-averaged aggregates radius of gyration 〈Rg〉 increased monotonically almost three-fold with crosslinkers’ Mw along with an open structure formation compared to phytic acid crosslinked aggregates. This improvement was connected with more than a 20-fold increase in adsorbed N2 and a resulting increase in the specific surface area for aggregates crosslinked with CMC compared to phytic acid counterparts. A larger number of COOH groups on the CMC surface combined with optimal pore size achieved with its decreasing Mw facilitated the enzymes’ free diffusion to the functional groups and their retention. The phenomena further allowed a larger fraction of covalent bond formation of enzyme-substrate, resulting in higher specific activity and stability for Candida rugosa and Candida Antarctica, found in commercial biocatalysts, which will guide the formation of improved biocatalysts on porous polymer supports in the future. © 2023 Elsevier B.V.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

20401 - Chemical engineering (plants, products)

Projekt

—

Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2023

Kód důvěrnosti údajů

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

Název periodika

COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS

ISSN

0927-7757

e-ISSN

1873-4359

Svazek periodika

667

Číslo periodika v rámci svazku

JUN 20 2023

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

13

Strana od-do

—

Kód UT WoS článku

001042106800001

EID výsledku v databázi Scopus

2-s2.0-85151523344