4-Methylcatechol (4MC) is a polyphenol with origin in processed food. Proteinpolyphenol
adducts are formed upon covalent bonding between oxidized polyphenols
and proteins. The present study investigated in vitro gastric and intestinal digestion of
a milk protein, beta-lactoglobulin (beta-LG), covalently modified at its nucleophilic amino acid residues by oxidized 4MC, 4-methylbenzoquinone (4MBQ). The present study
characterizes 4MBQ-induced covalent modifications on beta-LG (henceforth beta-LQ) and
their effect on protein digestibility. Significant thiol and amine loss was found in beta-LQ
compared to beta-LG. Site-specific 4MBQ-induced modifications were identified on Cys,
Lys, Arg, His and Trp in beta-LQ. No significant differences between beta-LG and beta-LQ on in vitro digestibility were observed by assessment with SDS-PAGE, degree of hydrolysis
and LC-MS/MS unmodified peptide intensities. Cys-4MC adduct (1.7 ± 0.1 umol/g
protein) was released from beta-LQ after in vitro digestion. Overall, 4MBQ-induced
covalent modifications in beta-LQ did not affect protein digestibility under the present
reaction conditions.
[doi:10.25345/C5JN9F]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: beta-lactoglobulin ; Digestibility ; protein-polyphenol covalent adducts ; 4-methylcatechol ; 4-methylbenzoquinone
Principal Investigators: (in alphabetical order) |
Marianne Nissen Lund, Department of Food Science, University of Copenhagen, Denmark |
Submitting User: | KasperEK |
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