Protective Effect of Selenium-enriched Peptide from Cardamine violifolia on Ethanol-induced L-02 Hepatocyte Injury

Ling, Rongrui; Du, Chaodong; Li, Yue; Wang, Shan; Cong, Xin; Huang, Dejian; Chen, Shangwei; Zhu, Song

doi:10.1007/s12011-024-04159-8

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“…However, once hydrolyzed from macromolecules, they can exert biological activity, including scavenging free radicals, resisting oxidative stress, and other health-related physiological functions [ 13 ]. R. Ling et al [ 14 ] prepared Se-enriched peptides by enzymatic hydrolysis of CV proteins using Alcalase and Dispase, and found that Se-enriched peptides increased mRNA expression of GPX1 and NGFR in ethanol-treated L-02 hepatocytes, confirming their protective effect against ethanol-induced liver injury. Q. Zhao et al [ 15 ] prepared egg yolk Se-enriched peptides using Alcalase and Dispase hydrolysis combined with shear pretreatment, which exhibited excellent immunoassays, including immune organ index, serum levels of immune factors, splenic histopathological changes, and hepatic Se content.…”

Section: Introductionmentioning

confidence: 99%

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

Zhu,

Li,

Chen

et al. 2024

Foods

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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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Section: Introductionmentioning

confidence: 99%