Quantitative changes in peptides derived from proteins in beef tenderloin (psoas major muscle) and striploin (longissimus lumborum muscle) during cold storage.

Peptides derived from whole proteins in beef tenderloin (M. psoas major, PM) and striploin (M. longissimus lumborum, LL) associated with meat quality and muscle fiber composition were identified and quantified during 21 days of aging. Peptide quantification revealed 40-43 proteins to be significantly degraded during all aging time, and these were mostly sarcoplasmic proteins. Cooking loss of both muscles was not changed by aging (P > 0.05), whereas Warner-Bratzler shear force and meat color were affected by aging. Sensory tenderness increased in PM after 14 days of aging (P < 0.05). PM had a higher type I fiber content, whereas LL had a higher type IIX fiber content (P < 0.05), resulting in differences in proteolysis during all aging periods tested. These findings improve our understanding of different biochemical and physicochemical changes in aged meat according to the muscle type.