Pseudomonas cepacia lipase immobilized on Zn₂Al layered double hydroxides: Evaluation of different methods of immobilization for the kinetic resolution of (R,S)-1-phenylethanol

IF 1.4 4区生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY

Biocatalysis and Biotransformation Pub Date : 2023-02-27 DOI:10.1080/10242422.2023.2181047

Lilian Fernanda Martins do Amaral, Cristiane Pilissão, Nadia Krieger, Fernando Wypych

{"title":"Pseudomonas cepacia lipase immobilized on Zn2Al layered double hydroxides: Evaluation of different methods of immobilization for the kinetic resolution of (R,S)-1-phenylethanol","authors":"Lilian Fernanda Martins do Amaral, Cristiane Pilissão, Nadia Krieger, Fernando Wypych","doi":"10.1080/10242422.2023.2181047","DOIUrl":null,"url":null,"abstract":"The present work deals with the preparation and characterization of Zn2Al layered double hydroxides (LDHs) intercalated with chloride and dodecyl sulfate ions and their use as supports for the immobilization of Pseudomonas cepacia lipase (LipPS). LipPS was immobilized on LDH by adsorption, in situ entrapment and delamination entrapment methods. The performance of free and immobilized LipPS in the transesterification of (R,S)-1-phenylethanol was compared. The immobilized derivatives prepared by adsorption gave the highest conversions (c = 50%), with an enantiomeric excess of the product (eep) greater than 99% and a high enantiomeric ratio (E > 200). For immobilization by in situ entrapment (coprecipitation), a conversion of 31.5% and E > 200 were obtained. For immobilization by delamination entrapment, a conversion of 36% and E= 155 were obtained. Although the best results were obtained by adsorption, these results show that the delamination entrapment method can also be used to prepare bioinorganic-enzyme materials based on LDH. Our work therefore increases the range of methods that can be used to immobilize lipases for use in the production of optically pure secondary alcohols.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"36 1","pages":"0"},"PeriodicalIF":1.4000,"publicationDate":"2023-02-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biocatalysis and Biotransformation","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/10242422.2023.2181047","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}

引用次数: 1

Abstract

The present work deals with the preparation and characterization of Zn2Al layered double hydroxides (LDHs) intercalated with chloride and dodecyl sulfate ions and their use as supports for the immobilization of Pseudomonas cepacia lipase (LipPS). LipPS was immobilized on LDH by adsorption, in situ entrapment and delamination entrapment methods. The performance of free and immobilized LipPS in the transesterification of (R,S)-1-phenylethanol was compared. The immobilized derivatives prepared by adsorption gave the highest conversions (c = 50%), with an enantiomeric excess of the product (eep) greater than 99% and a high enantiomeric ratio (E > 200). For immobilization by in situ entrapment (coprecipitation), a conversion of 31.5% and E > 200 were obtained. For immobilization by delamination entrapment, a conversion of 36% and E= 155 were obtained. Although the best results were obtained by adsorption, these results show that the delamination entrapment method can also be used to prepare bioinorganic-enzyme materials based on LDH. Our work therefore increases the range of methods that can be used to immobilize lipases for use in the production of optically pure secondary alcohols.

查看原文本刊更多论文

在Zn2Al层状双氢氧化物上固定化洋葱假单胞菌脂肪酶:不同固定化方法对(R,S)-1-苯乙醇动力学分解的评价

本文研究了含氯和十二烷基硫酸盐离子的Zn2Al层状双氢氧化物(LDHs)的制备和表征及其作为固定化洋葱假单胞菌脂肪酶(LipPS)载体的应用。采用吸附法、原位包埋法和分层包埋法将LipPS固定在LDH上。比较了游离和固定化LipPS在(R,S)-1-苯乙醇酯交换反应中的性能。吸附法制备的固定化衍生物转化率最高(c = 50%)，产物的对映体过剩量(eep)大于99%，对映体比高(E > 200)。原位包埋固定(共沉淀法)的转化率为31.5%，E > 200。对于分层夹持固定，转化率为36%，E= 155。虽然吸附法获得的效果最好，但这些结果表明，分层包埋法也可以用于制备基于LDH的生物无机酶材料。因此，我们的工作增加了固定化脂肪酶用于生产光学纯仲醇的方法范围。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文求助全文

来源期刊

Biocatalysis and Biotransformation 生物-生化与分子生物学

CiteScore

4.40

自引率

5.60%

发文量

审稿时长

3 months

期刊介绍： Biocatalysis and Biotransformation publishes high quality research on the application of biological catalysts for the synthesis, interconversion or degradation of chemical species. Papers are published in the areas of: Mechanistic principles Kinetics and thermodynamics of biocatalytic processes Chemical or genetic modification of biocatalysts Developments in biocatalyst''s immobilization Activity and stability of biocatalysts in non-aqueous and multi-phasic environments, including the design of large scale biocatalytic processes Biomimetic systems Environmental applications of biocatalysis Metabolic engineering Types of articles published are; full-length original research articles, reviews, short communications on the application of biotransformations, and preliminary reports of novel catalytic activities.