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This study investigated whether the freezing-then-aging treatment of beef affects protein digestibility and release of potentially bioactive peptides using an in vitro infant digestion model. After 28 days of storage, aged-only (AO) and frozen-then-aged (FA) beef exhibited higher α-amino group contents in the 10% trichloroacetic acid-soluble fraction compared to day 0 (P < 0.05). Following in vitro digestion in the infant model, FA showed higher contents of α-amino groups and smaller proteins (<3 and 1 kDa) than day 0 and AO (P < 0.05). Relative contributions of myofibrillar, sarcoplasmic, and stromal proteins to the bioactive peptides released from AO and FA differed from those of day 0. In addition, FA exhibited a higher proportion of potential bioactive peptide sequences. Overall, freezing-then-aging treatment can enhance the potential health benefits of beef to be used as a protein source for complementary foods. • Freezing-then-aging increased beef proteolysis during storage and in vitro digestion. • Alteration in protein digestibility changed peptide profile after in vitro digestion. • Myofibrillar and stromal proteins primarily contributed to peptide release. • Beef protein had ACE, DPP-IV, and α-glucosidase inhibitory and antioxidant activities. • Freezing increased the ratio of released peptides with potential bioactivity. [ABSTRACT FROM AUTHOR]

Beef is an ideal protein source for use as a complementary food in infants. Considering the limited protein-digesting capacity of infants, it is required to enhance protein digestibility while minimizing the deterioration of beef quality. Thus, this study aimed to determine the effects of high-pressure processing (HPP) on the physicochemical properties and in vitro digestibility of beef proteins in an infant digestion model. HPP at 200 and 300 MPa decreased the tryptophan fluorescence intensity of the myosin and actin fractions relative to that at 0.1 MPa (P < 0.05). Compared to treatment at 0.1 and 100 MPa, HPP at 300 MPa decreased α-helix and β-turn contents in the myosin and actin fractions (P < 0.05), whilst increasing the β-sheet content (P < 0.05). Beef actomyosin content decreased (P < 0.05) during HPP at 200 and 300 MPa (c.f., 0.1 and 100 MPa). After in vitro digestion of beef, HPP at 200 and 300 MPa increased the α-amino group content and the abundance of proteins below 3 kDa in the digesta (P < 0.05). However, due to the considerable lipid oxidation at 300 MPa, HPP at 200 MPa is ideal for improving the protein digestibility of beef when incorporated into complementary foods for infants. • The effects of high-pressure processing (HPP) on beef protein quality were studied • HPP at 300 MPa induced conformational changes in the myosin and actin fractions • HPP at 200 and 300 MPa decreased the actomyosin content of beef • HPP at 200 and 300 MPa improved the beef protein digestibility in vitro [ABSTRACT FROM AUTHOR]