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 5 publications

(2 citation statements)

References 45 publications

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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%

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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A facile and sustainable preparation of effective biomass macromolecular flame retardants for epoxy resins with improved flame retardation, smoke suppression, and mechanical performance

Ling,

Zhang,

Wang

2024

J of Applied Polymer Sci

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The preparation of biomass flame retardants with efficient flame‐retardant properties is conducive to the realization of sustainable development and is of great practical significance. In this work, a green and sustainable biomass flame retardant PATAPEI was prepared by using phytic acid (PA), tannic acid (TA), and polyethyleneimine (PEI) as reactants via a one‐step method to develop biomass flame retardants that can synchronize enhanced flame retardation, smoke suppression, and mechanical performance of epoxy resin (EP). The EP with only a 3% PATAPEI (EP/3PTP) has a LOI value of 28.5% with a UL‐94 V‐0 classification. The peak heat release rate (PHRR), total heat release (THR), and total smoke release (TSR) of EP/3PTP were decreased by 29.72%, 25.80%, and 21.16%, respectively, in comparison with the ones of pure EP. Additionally, the tensile and impact strengths of EP/3PTP are higher than the ones of pure EP. PATAPEI on heating decomposes to produce phosphorus‐containing acids and biphenyltriol‐containing compounds, which promote to form a good char layer with the aromatic structures during the combustion of EP/3PTP. Therefore, PATAPEI has prospects of wide application in the development of sustainable biomass flame retardant EP.

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Immobilization of alcalase on polydopamine modified magnetic particles

Wang,

Zhou,

et al. 2024

Biochemical Engineering Journal

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

Abstract: Preparation of Se-enriched peptides by enzymatic hydrolysis of Se-enriched protein of CV with immobilized Alcalase.

Cited by 5 publications

References 45 publications

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

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

A facile and sustainable preparation of effective biomass macromolecular flame retardants for epoxy resins with improved flame retardation, smoke suppression, and mechanical performance

Immobilization of alcalase on polydopamine modified magnetic particles

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