Enhanced Stability of Lactobacillus paracasei Aspartate Ammonia-Lyase via Electrospinning for Enzyme Immobilization

利用静电纺丝技术固定化副干酪乳杆菌天冬氨酸氨裂解酶,提高其稳定性

阅读:1

Abstract

This study investigates the immobilization of Lactobacillus paracasei AAL (LpAAL) protein onto polyvinyl alcohol/nylon 6/chitosan nanofiber membranes using dextran polyaldehyde as a biodegradable cross-linker. Immobilization enhanced the enzyme's stability, shifting its optimal reaction conditions from 40 °C to 45 °C and pH from 8.0 to 8.5. While immobilization slightly reduced its catalytic efficiency, it significantly improved enzyme stability and reusability. The immobilized enzyme retained 85% of its initial activity after 7 days of storage at room temperature, compared to 55% for the free enzyme. Reusability tests demonstrated that immobilized LpAAL protein maintained approximately 50% of its activity after six consecutive reaction cycles, highlighting its robustness over repeated use. These results underscore the advantages of nanofiber-based immobilization in enhancing enzyme stability and utility for industrial applications, offering a practical approach to overcoming the limitations associated with free enzyme systems.

特别声明

1、本页面内容包含部分的内容是基于公开信息的合理引用;引用内容仅为补充信息,不代表本站立场。

2、若认为本页面引用内容涉及侵权,请及时与本站联系,我们将第一时间处理。

3、其他媒体/个人如需使用本页面原创内容,需注明“来源:[生知库]”并获得授权;使用引用内容的,需自行联系原作者获得许可。

4、投稿及合作请联系:info@biocloudy.com。