Co-Immobilization of Alcalase/Dispase for Production of Selenium-Enriched Peptide from Cardamine violifolia

被引:1
|
作者
Zhu, Shiyu [1 ]
Li, Yuheng [1 ]
Chen, Xu [1 ]
Zhu, Zhenzhou [1 ]
Li, Shuyi [1 ]
Song, Jingxin [2 ]
Zheng, Zhiqiang [2 ]
Cong, Xin [1 ]
Cheng, Shuiyuan [1 ]
机构
[1] Wuhan Polytech Univ, Sch Modern Ind Selenium Sci & Engn, 36 Huanhu Middle Rd, Wuhan 430048, Peoples R China
[2] Syst Engn Inst, Beijing 100010, Peoples R China
关键词
selenium; peptide; co-immobilization; enzyme; Cardamine violifolia; IMMOBILIZED ALCALASE; PROTEIN; ENZYMOLYSIS; HYDROLYSIS; LACCASE;
D O I
10.3390/foods13111753
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Enzymatically derived selenium-enriched peptides from Cardamine violifolia (CV) can serve as valuable selenium supplements. However, the industrial application of free enzyme is impeded by its limited stability and reusability. Herein, this study explores the application of co-immobilized enzymes (Alcalase and Dispase) on amino resin for hydrolyzing CV proteins to produce selenium-enriched peptides. The successful enzyme immobilization was confirmed through scanning electron microscopy (SEM), energy dispersive X-ray (EDX), and Fourier-transform infrared spectroscopy (FTIR). Co-immobilized enzyme at a mass ratio of 5:1 (Alcalase/Dispase) exhibited the smallest pore size (7.065 nm) and highest activity (41 U/mg), resulting in a high degree of hydrolysis of CV protein (27.2%), which was obviously higher than the case of using free enzymes (20.7%) or immobilized Alcalase (25.8%). In addition, after a month of storage, the co-immobilized enzyme still retained a viability level of 41.93%, showing fairly good stability. Encouragingly, the selenium-enriched peptides from co-immobilized enzyme hydrolysis exhibited uniform distribution of selenium forms, complete amino acid fractions and homogeneous distribution of molecular weight, confirming the practicality of using co-immobilized enzymes for CV protein hydrolysis.
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页数:18
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