α-Acetolactatedecarboxylase immobilized onto magnetic polyvinyl alcohol microspheres

QIAN Siriguleng; WANG Hongying; LIU Yang; GENG Jinfeng; ZHU Jingying; CUI Maoxin

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α-Acetolactatedecarboxylase immobilized onto magnetic polyvinyl alcohol microspheres

更新时间：2025-12-10

- α-Acetolactatedecarboxylase immobilized onto magnetic polyvinyl alcohol microspheres
- CIESC Journal Issue 8, Pages: 2062-2066(2007)
- 作者机构：
  
  大连工业大学生物与食品工程学院
- 作者简介：
- 基金信息：
- DOI：
  CLC：
- Online First：05 August 2007，
  
  Published：05 August 2007
- 稿件说明：
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QIAN Siriguleng, WANG Hongying, LIU Yang, et al. α-Acetolactatedecarboxylase immobilized onto magnetic polyvinyl alcohol microspheres[J]. CIESC Journal, 2007, (8): 2062-2066.
DOI：

QIAN Siriguleng, WANG Hongying, LIU Yang, et al. α-Acetolactatedecarboxylase immobilized onto magnetic polyvinyl alcohol microspheres[J]. CIESC Journal, 2007, (8): 2062-2066. DOI：

摘要

采用分散聚合法，用Fe3O4磁流体和PVA分子单体共聚合，制备表面富含羟基和羧基等官能团，粒径分布在8～64µm的磁性聚乙烯醇微球。以CDI为一种PVA的羧基化剂，并通过共价结合固定化法，使ALDC固定到磁性聚乙烯醇微球表面上。结果，固定化ALDC的总活力、蛋白载量、比活和活性回收率分别为65180U/g、74.72mg/g、872.32U/mg和48.71％。固定化ALDC的最适温度和最适pH值分别为50℃和6.0。ALDC被固定化后其热稳定性、操作稳定性、pH稳定性均比自由酶提高。固定化ALDC在４℃、pH 6.0磷酸缓冲液中保存31d，其相对活力仍保持95.7％，这比其自由酶的提高7个百分点。

Abstract

Magnetic polyvinyl alcohol (PVA) microspheres with 8—64 μm in diameter were prepared from PVA by dispersion and copolymerization with Fe3O4 as magnetite.There were more functional groups

such as hydroxyl and carboxyl etc. on the microsphere surface.1

1′-Carbonyldiimidazole (CDI)

a carbonylating agent

was used for the activation of hydroxyl groups of PVA

and α-acetolactatedecarboxylase (ALDC) was immobilized onto the magnetic PVA microspheres by covalent bonding through the amino group.The results showed that total activity

protein binding

specific activity and activity retention of the immobilized enzyme were 63293 U·g-1

72.67 mg·g-1

870.96 U·mg-1and 48.71％

respectively.The optimum temperature of immobilization enzyme was 50℃ and the optimum pH was 6.0.Compared with the free enzyme of ALDC

the thermal

operational and pH stability of the immobilized enzyme were improved.After being stored at 4℃

pH 6.0 for 31 days

the immobilized ALDC retained 95.7% of its initial activity which was 8% higher than the free enzyme.

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