Preparation of immobilized pepsin for extraction of collagen from bovine hide

Duan, Youdan; Cheng, Haiming

doi:10.1039/d2ra05744a

Cited by 3 publications

(2 citation statements)

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“…Herein, BSA (2 mL, 5 mg/mL) was used as the substrate to measure enzyme activity [ 31 ]. The performance of immobilized enzymes, referred to as matrix activity, was documented per milligram of matrix for easy comparison.…”

Section: Methodsmentioning

confidence: 99%

“…where the protein concentrations (mg/mL) in the initial solution and washing solution are represented by C 0 and C W , respectively, and the volumes (mL) of the initial solution and washing solution are denoted by V 0 and V W , respectively. Herein, BSA (2 mL, 5 mg/mL) was used as the substrate to measure enzyme activity [31]. The performance of immobilized enzymes, referred to as matrix activity, was documented per milligram of matrix for easy comparison.…”

Section: Determination Of the Optimal Alcalase/resin Ratiomentioning

confidence: 99%

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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: Methodsmentioning

confidence: 99%

Section: Determination Of the Optimal Alcalase/resin Ratiomentioning

confidence: 99%