氧化锌盐作为洋葱假单胞菌脂肪酶固定化的新载体

IF 1.4 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
Glauco Silva Dias, David Alexander Mitchell, Fernando Wypych, Nadia Krieger
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引用次数: 0

摘要

层状双氢氧化物(LDHs)是一种类似水镁石的纳米材料,已被用于固定化多种酶。然而,层状氢氧化物盐(lhs),另一组类似水镁石的纳米材料,尚未用于酶固定化。本文制备了两种层状氢氧化锌盐:硝酸氢氧化锌(ZHN: Zn5(OH)8(NO3)2.2H2O)和氯化锌(ZHC: Zn5(OH)8Cl2.H2O),并将其用于固定化洋葱假单胞菌脂肪酶(LipPS)。zn和ZHC的最佳蛋白负荷均为162.5 mg g−1,在有机培养基中具有较高的三聚烯烃水解活性(LipPS-ZHN为103 U g−1,LipPS-ZHC为105 U g−1),固定化效率在90%以上,活性保留率在170%以上。在(R,S)-1-苯乙醇的动力学拆分方面,LipPS-ZHN具有较好的效果,2 h内转化率达到50%,转化率达到99%。LipPS-ZHC在2 h的转化率为40%,ees较低,仅为73%。两种固定化材料的eep均大于99%,E均大于200。在连续的2 h动力学分辨率下,固定材料在重复使用5次后是稳定的。这些结果表明,层状氢氧化盐ZHN和ZHC作为固定化脂肪酶的载体具有良好的潜力。关键词:洋葱假单胞菌脂酶固定化层状氢氧盐酶动力学分解作者对本研究的构思和设计均有贡献。材料准备、数据收集和分析由Glauco Silva Dias完成。Nadia Krieger和Fernando Wypych直接监督这项工作。手稿的初稿是由Glauco Silva Dias撰写的,所有作者都对手稿的初稿和后续版本进行了评论。所有作者都阅读并批准了最终的手稿。披露声明作者声明,他们没有已知的竞争经济利益或个人关系,可能会影响本文所报道的工作。虽然资金来自不同的研究资助机构(列在致谢部分),但没有一个资助机构参与研究的设计、执行或报告。本研究由巴西政府高等教育人才发展机构CAPES (codena ode aperfeiamento de Pessoal de Nível Superior)和巴西-阿根廷生物技术中心(CBAB/CABBIO)资助、CNPq (Conselho Nacional de Desenvolvimento Científico e Tecnológico)管理的一个项目资助(财务代码001)。巴西政府科技促进机构(项目441015/2016-6)。研究奖学金由CAPES授予Glauco Silva Dias,由CNPq授予David Alexander Mitchell, Fernando Wypych和Nadia Krieger。这些资助机构没有参与工作的设计、执行或报告。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Zinc hydroxide salts as new supports for the immobilization of Pseudomonas cepacia lipase
AbstractLayered double hydroxides (LDHs) are brucite-like nanomaterials that have been used to immobilize several enzymes. However, layered hydroxide salts (LHSs), another group of brucite-like nanomaterials, have not yet been used for enzyme immobilization. In this work, we prepared two types of layered hydroxide salts, zinc hydroxide nitrate (ZHN: Zn5(OH)8(NO3)2.2H2O) and zinc hydroxide chloride (ZHC: Zn5(OH)8Cl2.H2O) and used them to immobilize Pseudomonas cepacia lipase (LipPS). The best protein loading for both ZHN and ZHC was 162.5 mg g−1 of LHS, which gave high values of triolein-hydrolyzing activity in organic medium (103 U g−1 for LipPS-ZHN and 105 U g−1 for LipPS-ZHC), immobilization efficiencies above 90% and activity retentions above 170%. In the kinetic resolution of (R,S)-1-phenylethanol, LipPS-ZHN gave better results, with 50% conversion being obtained in 2 h and an ees of 99%. With LipPS-ZHC, the conversion at 2 h was 40% and the ees, was lower, only 73%. For both immobilized materials, the eep was higher than 99% and E was higher than 200. The immobilized materials were stable after 5 cycles of reuse in successive 2-h kinetic resolutions. These results demonstrate that the layered hydroxide salts ZHN and ZHC have good potential as supports for the immobilization of lipases.Keywords: Pseudomonas cepacia lipaseimmobilizationlayered hydroxide saltsenzymatic kinetic resolution Authors’ contributionsAll authors contributed to the conception and design of the study. Material preparation, data collection and analysis were performed by Glauco Silva Dias. Nadia Krieger and Fernando Wypych directly supervised the work. The first draft of the manuscript was written by Glauco Silva Dias and all authors commented on this first draft and subsequent versions of the manuscript. All authors read and approved the final manuscript.Disclosure statementThe authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. Although funding was received from various research funding agencies (listed in the acknowledgements section), none of the funding agencies were involved in the design, execution or reporting of the work.Additional informationFundingThis study was financed (Finance Code 001) by CAPES (Coordenação de Aperfeiçoamento de Pessoal de Nível Superior), a Brazilian government agency for the development of personnel in higher education and by a project financed by the Brazilian-Argentine Biotechnology Center (CBAB/CABBIO) and administered by CNPq (Conselho Nacional de Desenvolvimento Científico e Tecnológico), a Brazilian government agency for the advancement of science and technology (Project 441015/2016-6). Research scholarships were granted to Glauco Silva Dias by CAPES and to David Alexander Mitchell, Fernando Wypych and Nadia Krieger by CNPq. These funding agencies were not involved in the design, execution or reporting of the work.
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来源期刊
Biocatalysis and Biotransformation
Biocatalysis and Biotransformation 生物-生化与分子生物学
CiteScore
4.40
自引率
5.60%
发文量
37
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.
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