Influence of Proteolysis on the Binding Capacity of Flavor Compounds to Myofibrillar Proteins.
Ontology highlight
ABSTRACT: Proteolysis occurs extensively during postmortem aging, enzymatic tenderization and fermentation of meat products, whereas less is understood regarding how proteolysis affects meat flavor. Myofibrillar proteins (MP) were extracted from beef longissimus dorsi muscle and subsequently treated with three commercial proteases. The effect of proteolysis on the interactions between the treated MP and butyraldehyde, 2-pentanone, octanal and 2-octanone was investigated. The progress of proteolysis increased the degree of hydrolysis (DH) and the surface hydrophobicity but decreased the turbidity and particle size. Fluorescence-quenching analysis results indicated that the enzymatic treatment generally increased the quenching constant (Ksv) between the treated MP and ketones but decreased the Ksv bet
SUBMITTER: Li H
PROVIDER: S-EPMC8955031 | biostudies-literature | 2022 Mar
REPOSITORIES: biostudies-literature
ACCESS DATA