Study on Stability of Catalase Immobilized by Metal-Polyphenol Coordination Polymers
10.19756/j.issn.0253-3820.251090
- VernacularTitle:金属-多酚配位聚合物固定化过氧化氢酶的稳定性研究
- Author:
Qin LIU
1
;
Yuan LIN
;
Zhao-Hui SU
Author Information
1. 中国科学院长春应用化学研究所,高分子物理与化学国家重点实验室,长春 130022;中国科学技术大学应用化学与工程学院,合肥 230026
- Keywords:
Enzyme;
Immobilization;
Stability;
Tannic acid;
Ferric ions
- From:
Chinese Journal of Analytical Chemistry
2025;53(6):1019-1027
- CountryChina
- Language:Chinese
-
Abstract:
The thermal sensitivity of enzymes is a key bottleneck that restricts their practical application,and the development of efficient enzyme stability enhancement technology has important application value.Based on the principle of metal-polyphenol coordination chemistry,this study used tannic acid-ferric ion(TA-FeⅢ)coordination polymer to nano-encapsulate catalase(CAT)and systematically explored its stability enhancement effect.The catalytic activity retention rate of the immobilized enzyme in extreme environments(High temperature,organic solvents,denaturants and pH 3-11)was significantly improved compared with that of the free enzyme,proving that the TA-FeⅢ nanoshell had a significant environmental barrier effect.In the long-term stability test,the immobilized enzyme retained 20％activity after a 30-d storage at room temperature,and its effective activity was prolonged to 8 times that of the free enzyme in the accelerated inactivation test at 37 ℃.In addition,several cyclic catalytic experiments demonstrated that the immobilized enzyme exhibited good reusability,thus broadening its practical application.
