{"title":"通过表面包覆无定形 ZIF-67 增强蔗糖磷酸化酶@磁性纳米粒子的催化活性和重复使用性","authors":"Zhendong Liu , Haichang Xu , Bin Wei , Hao Liang","doi":"10.1016/j.bej.2024.109533","DOIUrl":null,"url":null,"abstract":"<div><div>Sucrose phosphorylase (SPase) is a highly efficient glycosyltransferase which has a wide range of substrate specificity and excellent application prospects in the cosmetics, food, and medicine fields. The application of free SPase is limited due to its high cost, poor stability and poor reusability. Immobilization of enzymes can solve these problems. In this study, SPase was firstly immobilized by magnetic nanoparticles (MNPs) and surface-coating amorphous ZIF-67 for enhancing catalytical activity and reusability. ZIF-67@SPase@MNPs with MNPs core and ZIF-67 shell was characterized by TEM, SEM, XRD, FT-IR and VSM. Compared with free SPase, the catalytic activity of ZIF-67@SPase@MNPs increased by 30 %. Coated with amorphous ZIF-67, the immobilized enzyme retained 70 % relative activity after 12 cycles and 80 % relative activity after 15 days of storage. In addition, ZIF-67@SPase@MNPs had strong magnetic properties and the saturation magnetization was 52.07 emu/g. Surface-coating amorphous ZIF-67 on SPase@MNPs is a promising method for immobilizing enzymes, which can improve catalytic activity and reusability, therefore showing great application potential in biocatalysts and product separation. It has a good application prospect in the production of high viscosity glycosides.</div></div>","PeriodicalId":8766,"journal":{"name":"Biochemical Engineering Journal","volume":"212 ","pages":"Article 109533"},"PeriodicalIF":3.7000,"publicationDate":"2024-10-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Enhanced catalytic activity and reusability of sucrose phosphorylase@magnetic nanoparticles by surface-coating amorphous ZIF-67\",\"authors\":\"Zhendong Liu , Haichang Xu , Bin Wei , Hao Liang\",\"doi\":\"10.1016/j.bej.2024.109533\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Sucrose phosphorylase (SPase) is a highly efficient glycosyltransferase which has a wide range of substrate specificity and excellent application prospects in the cosmetics, food, and medicine fields. The application of free SPase is limited due to its high cost, poor stability and poor reusability. Immobilization of enzymes can solve these problems. In this study, SPase was firstly immobilized by magnetic nanoparticles (MNPs) and surface-coating amorphous ZIF-67 for enhancing catalytical activity and reusability. ZIF-67@SPase@MNPs with MNPs core and ZIF-67 shell was characterized by TEM, SEM, XRD, FT-IR and VSM. Compared with free SPase, the catalytic activity of ZIF-67@SPase@MNPs increased by 30 %. Coated with amorphous ZIF-67, the immobilized enzyme retained 70 % relative activity after 12 cycles and 80 % relative activity after 15 days of storage. In addition, ZIF-67@SPase@MNPs had strong magnetic properties and the saturation magnetization was 52.07 emu/g. Surface-coating amorphous ZIF-67 on SPase@MNPs is a promising method for immobilizing enzymes, which can improve catalytic activity and reusability, therefore showing great application potential in biocatalysts and product separation. It has a good application prospect in the production of high viscosity glycosides.</div></div>\",\"PeriodicalId\":8766,\"journal\":{\"name\":\"Biochemical Engineering Journal\",\"volume\":\"212 \",\"pages\":\"Article 109533\"},\"PeriodicalIF\":3.7000,\"publicationDate\":\"2024-10-16\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochemical Engineering Journal\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1369703X24003206\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOTECHNOLOGY & APPLIED MICROBIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemical Engineering Journal","FirstCategoryId":"5","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1369703X24003206","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
Enhanced catalytic activity and reusability of sucrose phosphorylase@magnetic nanoparticles by surface-coating amorphous ZIF-67
Sucrose phosphorylase (SPase) is a highly efficient glycosyltransferase which has a wide range of substrate specificity and excellent application prospects in the cosmetics, food, and medicine fields. The application of free SPase is limited due to its high cost, poor stability and poor reusability. Immobilization of enzymes can solve these problems. In this study, SPase was firstly immobilized by magnetic nanoparticles (MNPs) and surface-coating amorphous ZIF-67 for enhancing catalytical activity and reusability. ZIF-67@SPase@MNPs with MNPs core and ZIF-67 shell was characterized by TEM, SEM, XRD, FT-IR and VSM. Compared with free SPase, the catalytic activity of ZIF-67@SPase@MNPs increased by 30 %. Coated with amorphous ZIF-67, the immobilized enzyme retained 70 % relative activity after 12 cycles and 80 % relative activity after 15 days of storage. In addition, ZIF-67@SPase@MNPs had strong magnetic properties and the saturation magnetization was 52.07 emu/g. Surface-coating amorphous ZIF-67 on SPase@MNPs is a promising method for immobilizing enzymes, which can improve catalytic activity and reusability, therefore showing great application potential in biocatalysts and product separation. It has a good application prospect in the production of high viscosity glycosides.
期刊介绍:
The Biochemical Engineering Journal aims to promote progress in the crucial chemical engineering aspects of the development of biological processes associated with everything from raw materials preparation to product recovery relevant to industries as diverse as medical/healthcare, industrial biotechnology, and environmental biotechnology.
The Journal welcomes full length original research papers, short communications, and review papers* in the following research fields:
Biocatalysis (enzyme or microbial) and biotransformations, including immobilized biocatalyst preparation and kinetics
Biosensors and Biodevices including biofabrication and novel fuel cell development
Bioseparations including scale-up and protein refolding/renaturation
Environmental Bioengineering including bioconversion, bioremediation, and microbial fuel cells
Bioreactor Systems including characterization, optimization and scale-up
Bioresources and Biorefinery Engineering including biomass conversion, biofuels, bioenergy, and optimization
Industrial Biotechnology including specialty chemicals, platform chemicals and neutraceuticals
Biomaterials and Tissue Engineering including bioartificial organs, cell encapsulation, and controlled release
Cell Culture Engineering (plant, animal or insect cells) including viral vectors, monoclonal antibodies, recombinant proteins, vaccines, and secondary metabolites
Cell Therapies and Stem Cells including pluripotent, mesenchymal and hematopoietic stem cells; immunotherapies; tissue-specific differentiation; and cryopreservation
Metabolic Engineering, Systems and Synthetic Biology including OMICS, bioinformatics, in silico biology, and metabolic flux analysis
Protein Engineering including enzyme engineering and directed evolution.