Synthesis of lipase-hydrogel microspheres and their application in deacidification of high-acid rice bran oil

Yin, Yawen; Fei, Xu; Tian, Jing; Xu, Ling; Li, Yao; Wang, Yi

doi:10.1039/d2nj03761k

Cited by 2 publications

(2 citation statements)

References 62 publications

(72 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This could be attributed to enzyme molecules adsorbing onto the pores and surface of the resin, forming new irregular voids, especially within the mesopore range, during the co-immobilization process [ 45 ]. Meanwhile, when the ratio of the two enzymes was 5:1, the smallest pore size of the immobilized enzyme was measured at 7.065 nm, indicating effective adsorption of enzyme molecules at this point [ 46 ].…”

Section: Resultsmentioning

confidence: 99%

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

Zhu,

Li,

Chen

et al. 2024

Foods

View full text Add to dashboard Cite

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.

show abstract

Section: Resultsmentioning

confidence: 99%

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

Zhu,

Li,

Chen

et al. 2024

Foods

View full text Add to dashboard Cite

show abstract

“…Lipase is a family of enzymes that catalyzes the hydrolysis of fats. As efficient and “green” biocatalysts, 1 lipases have been widely used in hydrolysis, 2 alcoholysis, 3 esterification 4 and transesterification reactions, 5 and are considered to be the most valuable enzymes in the biological-production industry. 6 Due to the special structure of lipases, a relatively hydrophobic α-helix “lid” covers the central surface of the catalytic active site and has a protective role.…”

Section: Introductionmentioning

confidence: 99%

Lipase/tannic acid magnetic hydrogel microspheres and their continuous catalytic application

Ji,

Li,

Wang

et al. 2023

New J. Chem.

Self Cite

View full text Add to dashboard Cite

show abstract

Synthesis of lipase-hydrogel microspheres and their application in deacidification of high-acid rice bran oil

Abstract: The main challenge of rice bran oil (RBO) as a highly nutritional edible oil is the high content of free fatty acids.

Cited by 2 publications

References 62 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

Lipase/tannic acid magnetic hydrogel microspheres and their continuous catalytic application

Contact Info

Product

Resources

About