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

Overview

Journal Foods

Specialty Biotechnology

Date 2024 Jun 19

PMID 38890981

Authors

Shiyu Zhu

Yuheng Li

Xu Chen

Zhenzhou Zhu

Shuyi Li

Jingxin Song

Zhiqiang Zheng

Xin Cong

Shuiyuan Cheng

Affiliations

Soon will be listed here.

Abstract

Enzymatically derived selenium-enriched peptides from (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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