Effective lipase immobilization on crosslinked functional porous polypyrrole aggregates
The result's identifiers
Result code in 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>
Alternative codes found
RIV/60461373:22310/23:43927950
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Effective lipase immobilization on crosslinked functional porous polypyrrole aggregates
Original language description
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.
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
20401 - Chemical engineering (plants, products)
Result continuities
Project
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Continuities
S - Specificky vyzkum na vysokych skolach
Others
Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS
ISSN
0927-7757
e-ISSN
1873-4359
Volume of the periodical
667
Issue of the periodical within the volume
JUN 20 2023
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
13
Pages from-to
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UT code for WoS article
001042106800001
EID of the result in the Scopus database
2-s2.0-85151523344