{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang J"],"funding":["Northeast Agricultural University","National Natural Science Foundation of China","Natural Science Foundation of Heilongjiang Province"],"pagination":["2546-2555"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8693753"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(4)"],"pubmed_abstract":["This study investigated the effects of covalent conjugates combined by glycosylated black bean protein isolate (BBPI-G) and (-)-epigallocatechin-3-gallate (EGCG) on the emulsion stability. Fourier transform infrared (FTIR) spectroscopy showed that covalent binding of EGCG with BBPI-G made the protein molecule unfolded. Besides, the emulsifying properties of BBPI-G were increased after combined with EGCG. BBPI-G-EGCG emulsion had lower mean particle size and higher content of interfacial protein adsorption (AP), which resulted in thicker and more impact oil-water interface. Therefore, the stability of emulsions was significantly improved. Furthermore, the emulsions prepared by BBPI-G-EGCG compounds exhibited considerable stability in storage, oxidation, thermal treatments, freeze-thaw and f"],"journal":["RSC advances"],"pubmed_title":["Improvement of protein emulsion stability through glycosylated black bean protein covalent interaction with (-)-epigallocatechin-3-gallate."],"pmcid":["PMC8693753"],"funding_grant_id":["31901605","19XG27","ZD2019C005"],"pubmed_authors":["Zheng H","Li J","Jin H","Zhu X","Zhang S","Wang J","Xu J"],"additional_accession":[]},"is_claimable":false,"name":"Improvement of protein emulsion stability through glycosylated black bean protein covalent interaction with (-)-epigallocatechin-3-gallate.","description":"This study investigated the effects of covalent conjugates combined by glycosylated black bean protein isolate (BBPI-G) and (-)-epigallocatechin-3-gallate (EGCG) on the emulsion stability. Fourier transform infrared (FTIR) spectroscopy showed that covalent binding of EGCG with BBPI-G made the protein molecule unfolded. Besides, the emulsifying properties of BBPI-G were increased after combined with EGCG. BBPI-G-EGCG emulsion had lower mean particle size and higher content of interfacial protein adsorption (AP), which resulted in thicker and more impact oil-water interface. Therefore, the stability of emulsions was significantly improved. Furthermore, the emulsions prepared by BBPI-G-EGCG compounds exhibited considerable stability in storage, oxidation, thermal treatments, freeze-thaw and f","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jan","modification":"2025-04-04T09:09:50.136Z","creation":"2025-04-04T09:09:50.136Z"},"accession":"S-EPMC8693753","cross_references":{"pubmed":["35424159"],"doi":["10.1039/d0ra08756d"]}}