Protein solubility is related to myosin isoforms, muscle fiber types, meat quality traits, and postmortem protein changes in porcine longissimus dorsi muscle

Choi, Young Min; Lee, S.H.; Choe, Jae Gol; Rhee, Min Suk; Lee, S.K.; Joo, Seon-Tea; Kim, B.C.

doi:10.1016/j.livsci.2009.09.009

Cited by 62 publications

(41 citation statements)

References 55 publications

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“…A 56-kDa fragment of the globular head domain of MHC was identified to increase in abundance during postmortem aging in whole-muscle pork samples (Lametsch et al, 2003). Pork LM with low total protein solubility and low pH at 45 min postmortem also resulted in degradation of MHC (Choi et al, 2010). Degradation of MHC during postmortem aging could influence the migration pattern of MHC isoforms.…”

Section: Discussionmentioning

confidence: 98%

Postmortem protein degradation is a key contributor to fresh pork loin tenderness

Carlson¹,

Prusa²,

Fedler³

et al. 2017

Journal of Animal Science

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The objective of this study was to determine factors that influence tenderness independent of variation in pH, color, or marbling. To achieve the objective, 2 sample groups were chosen from a population of 159 pork loins aged 11 to 16 d. Predetermined ranges (ultimate pH, 5.54 to 5.86; marbling score, 1.0 to 3.0; percent total lipid, 1.61 to 3.37%) were defined for inclusion of individual loins in the study. The pork loins with the greatest (n = 12) and least (n = 12) Instron star probe values were assigned to 2 classification groups. The high star probe group had an average star probe that was 2.8 kg greater than the low star probe group (7.75 vs. 4.95 kg). Pork quality and sensory characteristics of pH, subjective and instrumental color values, cook loss, sensory tenderness, chewiness, juiciness, pork flavor, and off flavor were determined on fresh, never frozen pork chops. Lipid content, sarcomere length, myosin heavy-chain profile, and calpain autolysis were determined. Degradation of troponin-T, desmin, filamin, and titin were evaluated on the protein extracts from each sample. Pork loin pH, subjective color scores, Minolta L values, sarcomere length, and myosin heavychain composition were not different across groups. Chops from the low star probe group had a significantly greater marbling score (2.3 vs. 1.9) and lipid content (2.61 vs. 2.23%). Calpain-1 was completely autolyzed in both high and low star probe samples, demonstrating that calpain-1 potentially had been active in all samples. Low star probe whole-muscle protein extracts had more troponin-T (P < 0.01), desmin (P < 0.01), and filamin degradation (P < 0.01) than high star probe samples. Both classification groups showed degradation of titin. Remarkably, some high star probe samples still had observable intact bands of titin on SDS-PAGE gels. These results demonstrate that significant variation in instrumental tenderness is observed within a moderate pH range. Lipid content and proteolysis both appear to contribute to this variation.

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Section: Discussionmentioning

confidence: 98%

Postmortem protein degradation is a key contributor to fresh pork loin tenderness

Carlson¹,

Prusa²,

Fedler³

et al. 2017

Journal of Animal Science

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“…However, the oxygen-enrichment atmosphere inevitably accelerated oxidative reactions in meat which have been shown for lipids to cause rancidity in meat (Kim et al, 2010) and flavors deterioration (Jongberg et al 2014) through the breakdown of lipid hydroperoxides into volatile ketones and aldehydes (Ladikos and Lougovois 1990). Oxidation of lipids, which results in the production of free radicals, has been extensively studied and widely believed as a promoter of protein oxidation.…”

Section: Introductionmentioning

confidence: 99%

Effects of High Oxygen Packaging on Tenderness and Water Holding Capacity of Pork Through Protein Oxidation

Lin

Zhou

Zhang

2015

Food Bioprocess Technol

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The objective of this study was to investigate the biochemical difference of pork under high oxygen modified atmosphere packaging and their contribution to meat tenderness and water holding capacity of pork during postmortem storage. Twelve longissimus dorsi muscles were randomly assigned to either high oxygen modified atmosphere packaging or vacuum packaging and stored for 1, 4, and 6 days at 4°C. The carbonyl content, protein surface hydrophobicity, protein solubility, calpain activity, desmin degradation, tenderness, and water loss of pork were determined. Results showed that carbonyl content, protein surface hydrophobicity, and protein solubility were significantly affected (P < 0.05) by packaging method, while storage time did not significantly influence protein surface hydrophobicity and the solubility of sarcoplasmic protein (P > 0.05). Samples from high oxygen modified atmosphere packaging at 1 day showed greater intensity of intact 80 KDa calpain and lower intensity of autolyzed 76 KDa calpain product compared to samples from vacuum packaging (P < 0.05). Desmin degradation was significantly affected (P < 0.05) by packaging method and storage time, while their interaction presented no significance (P > 0.05). Higher intensity of intact desmin was observed in samples from high oxygen modified atmosphere packaging than vacuum packaging samples from 1 day of postmortem storage. Both packaging method and storage time showed significant effects (P < 0.05) on tenderness and water loss of pork muscle during postmortem storage. Changes in protein oxidation, calpain activation, and protein proteolysis of postmortem pork under high oxygen modified atmosphere packaging could help to explain decreased meat tenderness and increased centrifuge loss of pork. Keywords High oxygen modified atmosphere packaging . Pork muscle . Protein oxidation . Calpain . Tenderness . Water holding capacity Abbreviations HiOx High oxygen modified atmosphere packaging VP Vacuum packaging WHC Water holding capacity WBSF Warner-Bratzler shear force LD Longissimus dorsi PM Packaging method ST Storage time PM × ST Interaction of packaging method and storage time LF-NMR Low-field nuclear magnetic resonance DNPH 2,4-Dinitrophenylhydrazine BPB Bromophenol blue

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“…W przeciwieństwie do pierwszej fazy, enzymy uczestniczące w drugiej fazie glikolizy (5 z 6) zostały w więk-szości zidentyfikowane jako wiarygodne markery kruchości. Należą do nich: dehydrogenaza aldehydu 3-fosfoglicerolowego, kinaza fosfoglicerynianowa [33], enolaza (hydrataza fosfo(enolo)pirogronianowa), kinaza pirogronianowa i dehydrogenaza mleczanowa [12,48,66]. Innym potencjalnym markerem jest dehydrogenaza aldehydowa [33].…”

Section: Potencjalne Markery Kruchości Mięsaunclassified

Theories concerning natural tenderization processes in post mortem meat

Florek¹,

Domaradzki²,

Litwińczuk³

2016

zntj

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S t r e s z c z e n i eSpośród różnych właściwości mięsa wpływających na jego jakość, dla konsumenta najważniejsza jest kruchość. W czasie pośmiertnej konwersji mięśni do mięsa zachodzi złożony proces tenderyzacji. Od dawna mechanizm tenderyzacji mięsa był przedmiotem szczególnego zainteresowania badaczy z tego obszaru wiedzy. Pomimo intensywnych badań istota tych procesów nie została dokładnie poznana. W pracy przedstawiono główne teorie dotyczące mechanizmów tenderyzacji mięsa, zarówno nieenzymatyczne (wapniowa teoria kruszenia mięsa, wpływ ciśnienia osmotycznego), jak i enzymatyczne (procesy z udziałem proteolitycznych enzymów endogennych: kalpain i kalpastatyny, kaspaz, katepsyn, proteasomów, macierzy metaloproteaz). Wymienione enzymy prawdopodobnie uczestniczą w pośmiertnej proteolizie białek mięśniowych. Dokonano ponadto omówienia potencjalnych markerów z różnych szlaków metabolicznych, biorących udział w kształtowaniu kruchości mięsa post mortem.Słowa kluczowe: mięso, tenderyzacja, teorie, kruchość, markery kruchości WprowadzenieBezpośrednio po uboju zwierząt tkanka mięśniowa stanowi niepełnowartościowy surowiec zarówno do spożycia, jak i przetwórstwa. Jest twarda, gumowata, niesoczysta i ciężkostrawna, a składniki odżywcze są słabo przyswajalne. Podczas dojrzewania, tj. gdy tusze po ustąpieniu fazy rigor mortis przechowuje się w temperaturze wyższej od punktu zamarzania, zachodzą złożone procesy biochemiczne prowadzące do wykształ-cenia cech typowych dla mięsa kulinarnego. Do tych zmian należą [30]: 1) stopniowe wyczerpywanie się dostępnej energii, Dr hab. inż. M. Florek, dr inż. P. Domaradzki, Katedra Towaroznawstwa i Przetwórstwa Surowców Zwierzęcych, prof. dr hab.

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Protein solubility is related to myosin isoforms, muscle fiber types, meat quality traits, and postmortem protein changes in porcine longissimus dorsi muscle

Cited by 62 publications

References 55 publications

Postmortem protein degradation is a key contributor to fresh pork loin tenderness

Postmortem protein degradation is a key contributor to fresh pork loin tenderness

Effects of High Oxygen Packaging on Tenderness and Water Holding Capacity of Pork Through Protein Oxidation

Theories concerning natural tenderization processes in post mortem meat

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