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分散泛菌DJL-B醇脱氢酶的重组表达与固定化研究

田红 庞立 杨文韬 陈晓 王婧涵 夏菠 蒋立文

食品工业科技2025,Vol.46Issue(9):176-184,9.
食品工业科技2025,Vol.46Issue(9):176-184,9.DOI:10.13386/j.issn1002-0306.2024060040

分散泛菌DJL-B醇脱氢酶的重组表达与固定化研究

Recombinant Expression and Immobilization of Pantoea dispersa DJL-B Alcohol Dehydrogenase

田红 1庞立 2杨文韬 1陈晓 1王婧涵 1夏菠 1蒋立文1

作者信息

  • 1. 湖南农业大学食品科学技术学院,湖南长沙 410128
  • 2. 湖南农业大学园艺学院,湖南长沙 410128
  • 折叠

摘要

Abstract

To enhance the expression level of recombinant alcohol dehydrogenase in E.coli BL21(DE3),this study investigated the effects of induction temperature,induction time,and IPTG concentration on enzyme expression through one-way experiments.Additionally,the immobilization of recombinant alcohol dehydrogenase using sodium alginate embedding was examined to improve its application in geraniol conversion.The results indicated that the optimal expression conditions for recombinant alcohol dehydrogenase in E.coli BL21(DE3)were an induction temperature of 28 ℃,an induction time of 20 hours,and an IPTG concentration of 0.1 mmol/L.Furthermore,the conditions for immobilization were:immobilization temperature of 20 ℃,sodium alginate concentration of 3.5%,and enzyme addition of 500 μL.Meanwhile,the immobilized enzyme showed good mechanical stability,and the relative enzyme activity was still maintained at about 60%after 5 times of reuse,demonstrating good reusability.The results of the study provide an important theoretical reference for the industrial preparation of geranial using immobilized enzyme catalysis,which has good application prospects.

关键词

醇脱氢酶/异源表达/固定化/香叶醛/生物转化

Key words

alcohol dehydrogenase/heterogeneous expression/immobilization/geranial/bio-transformation

分类

生物科学

引用本文复制引用

田红,庞立,杨文韬,陈晓,王婧涵,夏菠,蒋立文..分散泛菌DJL-B醇脱氢酶的重组表达与固定化研究[J].食品工业科技,2025,46(9):176-184,9.

基金项目

湖南省自然科学基金项目(2022JJ30299、2022JJ30290). (2022JJ30299、2022JJ30290)

食品工业科技

OA北大核心

1002-0306

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