Xiaolong Sun, Jiahuan Hu, Yufeng Zhou, Xiangyu Zi, Huayue Zhu, Xi Luo, Yongqian Fu
{"title":"Innovative strategy of ZIF-90 for co-immobilization of whole cells and enzymes in biocatalytic D-phenyllactic acid synthesis.","authors":"Xiaolong Sun, Jiahuan Hu, Yufeng Zhou, Xiangyu Zi, Huayue Zhu, Xi Luo, Yongqian Fu","doi":"10.1016/j.ijbiomac.2024.137735","DOIUrl":null,"url":null,"abstract":"<p><p>In this study, we endeavored to catalyze the biosynthesis of D-phenyllactic (D-PLA) from L-Phenylalanine (L-Phe) through a one-pot method. However, the crucial enzymes for the biosynthesis of phenylpyruvate (PPA), amino acid oxidase (L-AAD), is a membrane-bound protein. Herein, we proposed a novel co-immobilization strategy of whole cells and enzymes, integrating them into ZIF-90 to achieve efficient biosynthesis of D-PLA. Consequently, we embarked on integrating both enzyme and E. coli into ZIF-90, ultimately obtaining the novel biocatalyst E. coli/LDH@ZIF-90. This achievement facilitated the cascade reaction between LDH and E. coli, enabling a streamlined one-pot bioconversion process. The morphology and structure of E. coli/LDH@ZIF-90 were thoroughly characterized using a range of methods, including XRD, SEM, FT-IR, CLSM, and XPS, which confirmed that the material had been successfully synthesized. Further activity experiments revealed that E. coli/LDH@ZIF-90 exhibited good stability even under harsh conditions. Additionally, the biocatalyst retained 76 % of its initial catalytic activity after completing six cycles. Moreover, when utilized for the biosynthesis of D-PLA, this system demonstrated an impressive conversion rate of 85.2 % after 12 h. The successful cascade catalysis from L-Phe to D-PLA underscored the potential of the enzyme-cell cascade catalytic system, offering valuable insights for its potential industrial applications.</p>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":" ","pages":"137735"},"PeriodicalIF":7.7000,"publicationDate":"2024-11-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Biological Macromolecules","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1016/j.ijbiomac.2024.137735","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
In this study, we endeavored to catalyze the biosynthesis of D-phenyllactic (D-PLA) from L-Phenylalanine (L-Phe) through a one-pot method. However, the crucial enzymes for the biosynthesis of phenylpyruvate (PPA), amino acid oxidase (L-AAD), is a membrane-bound protein. Herein, we proposed a novel co-immobilization strategy of whole cells and enzymes, integrating them into ZIF-90 to achieve efficient biosynthesis of D-PLA. Consequently, we embarked on integrating both enzyme and E. coli into ZIF-90, ultimately obtaining the novel biocatalyst E. coli/LDH@ZIF-90. This achievement facilitated the cascade reaction between LDH and E. coli, enabling a streamlined one-pot bioconversion process. The morphology and structure of E. coli/LDH@ZIF-90 were thoroughly characterized using a range of methods, including XRD, SEM, FT-IR, CLSM, and XPS, which confirmed that the material had been successfully synthesized. Further activity experiments revealed that E. coli/LDH@ZIF-90 exhibited good stability even under harsh conditions. Additionally, the biocatalyst retained 76 % of its initial catalytic activity after completing six cycles. Moreover, when utilized for the biosynthesis of D-PLA, this system demonstrated an impressive conversion rate of 85.2 % after 12 h. The successful cascade catalysis from L-Phe to D-PLA underscored the potential of the enzyme-cell cascade catalytic system, offering valuable insights for its potential industrial applications.
期刊介绍:
The International Journal of Biological Macromolecules is a well-established international journal dedicated to research on the chemical and biological aspects of natural macromolecules. Focusing on proteins, macromolecular carbohydrates, glycoproteins, proteoglycans, lignins, biological poly-acids, and nucleic acids, the journal presents the latest findings in molecular structure, properties, biological activities, interactions, modifications, and functional properties. Papers must offer new and novel insights, encompassing related model systems, structural conformational studies, theoretical developments, and analytical techniques. Each paper is required to primarily focus on at least one named biological macromolecule, reflected in the title, abstract, and text.