Muscle fiber type-specific proteome distribution and protease activity in relation to proteolysis trends in beef striploin (M. longissimus lumborum) and tenderloin (M. psoas major). (15th December 2022)

• Record Type: Journal Article
• Authors: Song, Sumin; Park, Junyoung; Im, Choeun; Cheng, Huilin; Jung, Eun-Young; Park, Tae Sub; Kim, Gap-Don
• Is Part Of: Lebensmittel-Wissenschaft + Technologie =. Volume 171(2022)
• Publication Date: 2022-12-15
• Subjects: Proteome -- Muscle type -- Muscle fiber composition -- Beef; ALDOA fructose-bisphosphate aldolase -- ANOVA analysis of variance -- BLVRB flavin reductase -- CKM creatine kinase M-type -- CSA cross-sectional area -- ENO3 beta-enolase -- FHL1 four-and-a-half LIM domain 1 -- GAPDH glyceraldehyde-3-phosphate dehydrogenase -- HBA hemoglobin subunit alpha -- HBB hemoglobin subunit beta -- MHC myosin heavy chain -- LCORL ligand dependent nuclear receptor corepressor like -- LDB3 LIM domain binding 3 -- LL longissimus lumborum -- PGK1 phosphoglycerate kinase -- PKM l-lactate dehydrogenase -- PM psoas major; Food industry and trade -- Periodicals; Food -- Composition -- Periodicals; Microbiology -- Periodicals; Nutrition -- Periodicals; 664.005
• DOI: 10.1016/j.lwt.2022.114098
• Languages: English
• ISSNs: 0023-6438

Abstract

Abstract: The muscle fiber type and proteome distributions, protease activity, and protein degradation in bovine M. longissimus lumborum (beef striploin; LL) and M. psoas major (beef tenderloin; PM) were assessed to study muscle type-specific proteolysis. Bovine LL and PM muscle pieces (3 cm thickness) were stored in a refrigerator for 14 days and protein degradation and protease activity were evaluated at 1, 7, and 14 days of storage. Bovine LL included more fast-twitch glycolytic (type IIX) fibers than PM, whereas PM had a higher composition of slow-twitch oxidative (type I) fibers than LL ( P < 0.05). Proteome distribution between these two muscles showed muscle fiber type-specificities: LL showed high intensities of proteins responsible for glycolytic metabolism, while PM showed large distribution of mitochondrial proteins. The activity of proteases, mainly calpain, showed different tendencies between the two muscles during 14 days of cold storage, which resulted in different timing of excessive myofibrillar protein breakdown (myosin heavy chains 1 and 2) between the two muscles. These results provided a detailed understanding of the differences in proteolysis by muscle type resulting in proteolysis-induced changes in meat quality during storage. Highlights: We compared proteome distribution and protease activity in bovine LL and PM. Bovine LL included more type IIX fibers, while PM included more type I fibers. LL included glycolytic metabolism proteins, and PM included mitochondrial proteins. Protease activities differed between the two muscles after 14 days of cold storage. Excessive myofibrillar protein breakdown occurred at different times in LL and PM.