<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Wang J</submitter><funding>Northeast Agricultural University</funding><funding>National Natural Science Foundation of China</funding><funding>Natural Science Foundation of Heilongjiang Province</funding><pagination>2546-2555</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8693753</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>11(4)</volume><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</pubmed_abstract><journal>RSC advances</journal><pubmed_title>Improvement of protein emulsion stability through glycosylated black bean protein covalent interaction with (-)-epigallocatechin-3-gallate.</pubmed_title><pmcid>PMC8693753</pmcid><funding_grant_id>31901605</funding_grant_id><funding_grant_id>19XG27</funding_grant_id><funding_grant_id>ZD2019C005</funding_grant_id><pubmed_authors>Zheng H</pubmed_authors><pubmed_authors>Li J</pubmed_authors><pubmed_authors>Jin H</pubmed_authors><pubmed_authors>Zhu X</pubmed_authors><pubmed_authors>Zhang S</pubmed_authors><pubmed_authors>Wang J</pubmed_authors><pubmed_authors>Xu J</pubmed_authors></additional><is_claimable>false</is_claimable><name>Improvement of protein emulsion stability through glycosylated black bean protein covalent interaction with (-)-epigallocatechin-3-gallate.</name><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</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Jan</publication><modification>2025-04-04T09:09:50.136Z</modification><creation>2025-04-04T09:09:50.136Z</creation></dates><accession>S-EPMC8693753</accession><cross_references><pubmed>35424159</pubmed><doi>10.1039/d0ra08756d</doi></cross_references></HashMap>