Xylanase immobilization onto trichlorotriazine-functionalized polyethylene glycol grafted magnetic nanoparticles: A thermostable and robust nanobiocatalyst for fruit juice clarification

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F20%3A73603067" target="_blank" >RIV/61989592:15310/20:73603067 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0141813020337272" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0141813020337272</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.ijbiomac.2020.06.273" target="_blank" >10.1016/j.ijbiomac.2020.06.273</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Xylanase immobilization onto trichlorotriazine-functionalized polyethylene glycol grafted magnetic nanoparticles: A thermostable and robust nanobiocatalyst for fruit juice clarification

Popis výsledku v původním jazyce

The covalent immobilization of xylanase onto the trichlorotriazine-functionalized polyethylene glycol grafted magnetic nanoparticles was exploited to generate a stabilized xylanase with improved catalytic activity and stability. Several tools were deployed to monitor the synthesis and immobilization processes, the loading capacity of nanocarrier, and the structural/chemical characteristics of the nanobiocatalyst. The optimum immobilization yield of xylanase was 260 mg xylanase/g nanocarrier in 20 mM phosphate buffer, pH 6.5 at 25 degrees C. A forward shift in optimum pH (6.5 to 7.5) and temperature (60 to 70 degrees C) of xylanase was observed after immobilization and the performance of immobilized enzyme was improved at high temperatures and pHs as affirmed by enhancement of v(max) (2.69 to 6.01 U/mL) and decreases of E-a (14.61 to 13.41 kJ/mol). An increase in K-m from 25.51 to 40.42 mg/mL was recorded after immobilization. The obtained results indicated augmented thermal stability of the immobilized xylanase. Notably, it showed good reusability as validated by retention of 50% of its initial activity after nine recycles in enrichment of the pineapple juice clarification after 120 min incubation at 50 degrees C, pH 4.5. The structural analysis revealed some partial changes in the alpha-helix and beta-sheet content of the enzyme after several recycles.

Název v anglickém jazyce

Xylanase immobilization onto trichlorotriazine-functionalized polyethylene glycol grafted magnetic nanoparticles: A thermostable and robust nanobiocatalyst for fruit juice clarification

Popis výsledku anglicky

The covalent immobilization of xylanase onto the trichlorotriazine-functionalized polyethylene glycol grafted magnetic nanoparticles was exploited to generate a stabilized xylanase with improved catalytic activity and stability. Several tools were deployed to monitor the synthesis and immobilization processes, the loading capacity of nanocarrier, and the structural/chemical characteristics of the nanobiocatalyst. The optimum immobilization yield of xylanase was 260 mg xylanase/g nanocarrier in 20 mM phosphate buffer, pH 6.5 at 25 degrees C. A forward shift in optimum pH (6.5 to 7.5) and temperature (60 to 70 degrees C) of xylanase was observed after immobilization and the performance of immobilized enzyme was improved at high temperatures and pHs as affirmed by enhancement of v(max) (2.69 to 6.01 U/mL) and decreases of E-a (14.61 to 13.41 kJ/mol). An increase in K-m from 25.51 to 40.42 mg/mL was recorded after immobilization. The obtained results indicated augmented thermal stability of the immobilized xylanase. Notably, it showed good reusability as validated by retention of 50% of its initial activity after nine recycles in enrichment of the pineapple juice clarification after 120 min incubation at 50 degrees C, pH 4.5. The structural analysis revealed some partial changes in the alpha-helix and beta-sheet content of the enzyme after several recycles.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

—

Návaznosti

N - Vyzkumna aktivita podporovana z neverejnych zdroju

Rok uplatnění

2020

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

163

Číslo periodika v rámci svazku

NOV

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

12

Strana od-do

402-413

Kód UT WoS článku

000579839600042

EID výsledku v databázi Scopus

2-s2.0-85088863211