Production of Cardamine violifolia selenium-enriched peptide using immobilized Alcalase on Fe3O4 modified by tannic acid and polyethyleneimine

Zhu, Shiyu; Cong, Xin; Sun, Zhuangzhi; Chen, Zhe; Chen, Xu; Zhu, Zhenzhou; Li, Shuyi; Cheng, Shuiyuan

doi:10.1039/d2ra03765c

Cited by 4 publications

(2 citation statements)

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“…This was primarily attributed to the resin carrier having an appropriate porous structure, preventing the clogging of substrate diffusion channels after enzyme molecule adsorption. Additionally, in comparison to our previous research [35], the DH of CV protein significantly increased (from 23.2% to 27.2%). Compared to other studies, the co-immobilized enzyme achieved a higher DH within a short period of time, which was attributed to the enrichment of substrates by the porous structure of the resin, and showed the promising application of the co-immobilized enzyme prepared in this study.…”

Section: Comparison Of the Efficiency Of Different Immobilized Enzymescontrasting

confidence: 85%

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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: Comparison Of the Efficiency Of Different Immobilized Enzymescontrasting

confidence: 85%

“…First, we precipitated the unreacted protein from the enzymatic solution with an excess of TCA. Total Se and inorganic Se content were calculated by atomic fluorescence spectrometry according to the method of Shiyu Zhu et al [ 35 ]. The content of organic Se was determined by subtracting the inorganic Se from the total Se.…”

Section: Methodsmentioning

confidence: 99%