Quantitative changes in peptides derived from proteins in beef tenderloin (psoas major muscle) and striploin (longissimus lumborum muscle) during cold storage. (15th February 2021)

• Record Type: Journal Article
• Authors: Kim, Gap-Don; Yun Lee, Seung; Jung, Eun-Young; Song, Sumin; Jin Hur, Sun
• Is Part Of: Food chemistry. Volume 338(2021)
• Publication Date: 2021-02-15
• Subjects: Proteolysis -- Peptide -- Sarcoplasmic protein -- Bovine skeletal muscle; PM psoas major -- LL longissimus lumborum -- LC–MS/MS liquid chromatography-mass spectrometry/mass spectrometry -- CIE Commission Internationale de l'Eclairage -- IHC immunohistochemistry -- LFQ label-free quantification -- MHC myosin heavy chain -- WBSF Warner-Bratzler shear force -- ACTA1 actin alpha skeletal muscle -- AK1 adenylate kinase isoenzyme 1 -- ALDOA fructose-bisphosphate aldolase -- ATP5O ATP synthase subunit O mitochondrial -- BIN1 bridging integrator 1 -- BTBD9 BTB/POZ domain-containing protein 9 -- CAST calpastatin -- CKM creatine kinase M-type -- CKMT2 creatine kinase S-type mitochondrial -- EEF1A1 elongation factor 1-alpha 1 -- DES desmin -- EER1A2 elongation factor 1-alpha 2 -- ENO1 alpha-enolase -- ENO3 beta-enolase -- GAPDH glyceraldehyde-3-phosphate dehydrogenase -- GPD1 glycerol-3-phosphate dehydrogenase [NAD(+)] cytoplasmic -- HBA hemoglobin subunit alpha -- HBB hemoglobin subunit beta -- HSPB1 heat shock 27kDa protein 1 -- HSPB6 heat shock protein beta-6 -- LDB3 LIM domain binding 3 -- MB myoglobin -- MDH2 malate dehydrogenase mitochondrial -- MYH1 myosin-1 -- MYH7 myosin-7 -- MYOT myotilin -- NDUFA4 cytochrome c oxidase subunit NDUFA4 -- NDUFA6 NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 -- NEB nebulin -- PARK7 protein DJ-1 -- PCMT1 protein-l-isoaspartate(d-aspartate) O-methyltransferase -- PDLIM3 PDZ and LIM domain protein 3 -- PDLIM7 isoform 2 of PDZ and LIM domain protein 7 -- PGAM2 phosphoglycerate mutase 2 -- PGK1 phosphoglycerate kinase 1 -- PGK2 phosphoglycerate kinase -- PKM2 pyruvate kinase -- PYGM alpha-1 4 glucan phosphorylase -- S100A10 protein S100-A10 -- SYNPO2 SYNPO2 protein -- TNNC2 fast skeletal troponin C -- TNNI1 slow skeletal troponin I -- TNNT3 troponin T fast skeletal muscle type -- TPI1 triosephosphate isomerase; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2020.128029
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Peptides derived from meat proteins in beef tenderloin and striploin were quantified. 40–43 Proteins were significantly degraded during 21 days of aging. Different muscle fiber composition between the two muscles affected the degradation of glycolytic proteins. Different changes in tenderness and purge loss were observed between the two muscles. Abstract: 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.