{"title":"Activity of enzymes immobilized on plasma treated polyester","authors":"Arfaoui Mohamed , Behary Nemeshwaree , Mutel Brigitte , Perwuelz Anne , Belhacene Kalim , Dhulster Pascal , Mamede Anne-Sophie , Froidevaux Rénato","doi":"10.1016/j.molcatb.2016.09.015","DOIUrl":null,"url":null,"abstract":"<div><p>The aim of this study was to investigate the effect of 3 different surface plasma treatments on the immobilization of β-galactosidase on a fibrous PET nonwoven membrane. Two methods 1. Entrapment in a thin calcium alginate coating and 2. Direct sorption, were used to immobilize the enzyme. The three different plasma treatments for surface activation of PET nonwovens were: 1. Air atmospheric DBD plasma, 2. Cold remote plasma-CRP with 100% N<sub>2</sub> and 3.- CRP with a mixture of N<sub>2</sub>/O<sub>2</sub> gases. Plasma treatment of the PET fiber surface increased the quantity of immobilized enzyme using the entrapment method, and the degree of alginate film cross-linking highly influenced the enzyme activity. Highest enzyme activity was reached for the PET treated with air atmospheric plasma and cross-linked with 0.25<!--> <!-->g/l of CaCl<sub>2</sub>. With the direct sorption method, greater amounts of enzyme were immobilized as compared to the entrapment method, but a considerable proportion of enzyme lost their catalytic activity. Only with the CRP N<sub>2</sub>/O<sub>2</sub> plasma treatment, up to 90% of sorbed enzyme maintained their activity. Reusability study showed that for the optimized entrapment method, a progressive decrease in activity was observed after each use cycle. With the optimized sorption method using N<sub>2</sub>/O<sub>2</sub> CRP plasma, no decrease in enzyme activity was detected, and the immobilized enzyme could be used over more than 15 cycles.</p></div>","PeriodicalId":16416,"journal":{"name":"Journal of Molecular Catalysis B-enzymatic","volume":"134 ","pages":"Pages 261-272"},"PeriodicalIF":0.0000,"publicationDate":"2016-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.molcatb.2016.09.015","citationCount":"15","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Molecular Catalysis B-enzymatic","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1381117716301898","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"Chemical Engineering","Score":null,"Total":0}
引用次数: 15
Abstract
The aim of this study was to investigate the effect of 3 different surface plasma treatments on the immobilization of β-galactosidase on a fibrous PET nonwoven membrane. Two methods 1. Entrapment in a thin calcium alginate coating and 2. Direct sorption, were used to immobilize the enzyme. The three different plasma treatments for surface activation of PET nonwovens were: 1. Air atmospheric DBD plasma, 2. Cold remote plasma-CRP with 100% N2 and 3.- CRP with a mixture of N2/O2 gases. Plasma treatment of the PET fiber surface increased the quantity of immobilized enzyme using the entrapment method, and the degree of alginate film cross-linking highly influenced the enzyme activity. Highest enzyme activity was reached for the PET treated with air atmospheric plasma and cross-linked with 0.25 g/l of CaCl2. With the direct sorption method, greater amounts of enzyme were immobilized as compared to the entrapment method, but a considerable proportion of enzyme lost their catalytic activity. Only with the CRP N2/O2 plasma treatment, up to 90% of sorbed enzyme maintained their activity. Reusability study showed that for the optimized entrapment method, a progressive decrease in activity was observed after each use cycle. With the optimized sorption method using N2/O2 CRP plasma, no decrease in enzyme activity was detected, and the immobilized enzyme could be used over more than 15 cycles.
期刊介绍:
Journal of Molecular Catalysis B: Enzymatic is an international forum for researchers and product developers in the applications of whole-cell and cell-free enzymes as catalysts in organic synthesis. Emphasis is on mechanistic and synthetic aspects of the biocatalytic transformation.
Papers should report novel and significant advances in one or more of the following topics;
Applied and fundamental studies of enzymes used for biocatalysis;
Industrial applications of enzymatic processes, e.g. in fine chemical synthesis;
Chemo-, regio- and enantioselective transformations;
Screening for biocatalysts;
Integration of biocatalytic and chemical steps in organic syntheses;
Novel biocatalysts, e.g. enzymes from extremophiles and catalytic antibodies;
Enzyme immobilization and stabilization, particularly in non-conventional media;
Bioprocess engineering aspects, e.g. membrane bioreactors;
Improvement of catalytic performance of enzymes, e.g. by protein engineering or chemical modification;
Structural studies, including computer simulation, relating to substrate specificity and reaction selectivity;
Biomimetic studies related to enzymatic transformations.