Immobilization of ligninolytic enzymes from white-rot fungi in cross-linked aggregates

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62156489%3A43210%2F18%3A43913602" target="_blank" >RIV/62156489:43210/18:43913602 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216305:26620/18:PU127926

Výsledek na webu

<a href="https://doi.org/10.1016/j.chemosphere.2018.03.088" target="_blank" >https://doi.org/10.1016/j.chemosphere.2018.03.088</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.chemosphere.2018.03.088" target="_blank" >10.1016/j.chemosphere.2018.03.088</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Immobilization of ligninolytic enzymes from white-rot fungi in cross-linked aggregates

Popis výsledku v původním jazyce

Ligninolytic enzymes from white-rot fungi are widely used in biotechnological processes. However, the application of these enzymes as free enzymes is limited due to their instability and lack of reusability. Enzyme stabilization is therefore a major challenge in biocatalytic process research, and immobilization methods are desirable. Using cross-linked enzyme aggregates (CLEAs) such as magnetic CLEAs, porous-CLEAs and combi-CLEAs is a promising technique for overcoming these issues. Cross-linking methods can stabilize and immobilize enzymes by interconnecting enzyme molecules via multiple bonds using cross-linking agents such as glutaraldehyde. The high catalyst density and microporous assembly of CLEAs guarantee high catalyst activity, which, together with their long shelf life, operational stability, and reusability, provide a cost-efficient alternative to matrix-assisted immobilization approaches. Here, we review current progress in ligninolytic enzyme immobilization and provide a comprehensive review of CLEAs. Moreover, we summarize the use of these CLEAs for biocatalysis processes, bioremediation such as dye decolourization, wastewater treatment or pharmaceutically active compound elimination.

Název v anglickém jazyce

Immobilization of ligninolytic enzymes from white-rot fungi in cross-linked aggregates

Popis výsledku anglicky

Ligninolytic enzymes from white-rot fungi are widely used in biotechnological processes. However, the application of these enzymes as free enzymes is limited due to their instability and lack of reusability. Enzyme stabilization is therefore a major challenge in biocatalytic process research, and immobilization methods are desirable. Using cross-linked enzyme aggregates (CLEAs) such as magnetic CLEAs, porous-CLEAs and combi-CLEAs is a promising technique for overcoming these issues. Cross-linking methods can stabilize and immobilize enzymes by interconnecting enzyme molecules via multiple bonds using cross-linking agents such as glutaraldehyde. The high catalyst density and microporous assembly of CLEAs guarantee high catalyst activity, which, together with their long shelf life, operational stability, and reusability, provide a cost-efficient alternative to matrix-assisted immobilization approaches. Here, we review current progress in ligninolytic enzyme immobilization and provide a comprehensive review of CLEAs. Moreover, we summarize the use of these CLEAs for biocatalysis processes, bioremediation such as dye decolourization, wastewater treatment or pharmaceutically active compound elimination.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LQ1601" target="_blank" >LQ1601: CEITEC 2020</a><br>

Návaznosti

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

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

Chemosphere

ISSN

0045-6535

e-ISSN

—

Svazek periodika

202

Číslo periodika v rámci svazku

July

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

14

Strana od-do

694-707

Kód UT WoS článku

000430882700079

EID výsledku v databázi Scopus

2-s2.0-85044482895