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Author: search.filters.author.Chaosap, ChanpornSubject: search.filters.subject.Calpastatin

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    Chemical and fatty acid composition, collagen, calpain and troponin T contents and quality characteristics of five muscle types in native Thai cattle
    (2024-03-01)
    Chaosap, Chanporn
    ;
    Sommart, Kritapon
    ;
    Adeyemi, Kazeem D.
    ;
    Polyorach, Sineenart
    ;
    Lukkananukool, Achara
    In this study, chemical composition, fatty acids, collagen solubility, calpains, and troponin T degradation were investigated in various muscles of native Thai cattle (NTC). Five muscles, namely Bicep femoris, Infraspinatus, Longissimus thoracis, Supraspinatus and Semimembranosus were sampled from five Kho Isaan bulls. Moisture content of Longissimus thoracis was lower (p < 0.05) than others. Protein content of Longissimus thoracis, Bicep femoris and Semimembranosus was higher (p < 0.05) than that of Infraspinatus and Supraspinatus. Infraspinatus and Longissimus thoracis had higher fat content (p < 0.05) than Bicep femoris and Semimembranosus. Muscle pH, color, and drip loss did not differ between muscles. Semimembranosus and Supraspinatus showed higher cook loss (p < 0.05) than Infraspinatus and Longissimus thoracis. Infraspinatus had the lowest Warner–Bratzler shear force (p < 0.05). Supraspinatus, Infraspinatus and Bicep femoris had higher (p < 0.05) soluble, insoluble and total collagen content than Semimembranosus and Longissimus thoracis. Infraspinatus had higher collagen solubility than Semimembranosus and Supraspinatus. Collagen content and solubility were not affected by ageing time. The relative band intensities of intact troponin T and its degradation product at 2- and 14-days postmortem were higher in Longissimus thoracis than in other muscles. Infraspinatus and Supraspinatus had significantly higher expression of m-calpain and calpastatin genes than Longissimus thoracis, Bicep femoris, and Semimembranosus. Total fatty acid was higher while the percentage of C22:6n-3 was lower in Infraspinatus and Longissimus thoracis (p < 0.05) than in other muscles. These results show differences in specific nutritional, technological and eating quality characteristics of NTC muscles and thus provide information for optimizing storage and processing conditions for various NTC muscles.
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    Meat quality, post-mortem proteolytic enzymes, and myosin heavy chain isoforms of different Thai native cattle muscles
    (2021-09-01)
    Chaosap, Chanporn
    ;
    Sivapirunthep, Panneepa
    ;
    Sitthigripong, Ronachai
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    Tavitchasri, Piyada
    ;
    Maduae, Sabaiporn
    Objective: This study investigated the meat quality characteristics, endogenous proteolytic enzymes, collagen content, and myosin heavy chain (MyHC) isoforms of different muscles of Thai native cattle (TNC). Methods: Infraspinatus (IF), Longissimus thoracis (LT), and Supraspinatus (SS) muscles were obtained from two TNC breeds, Kho-Lan (KL, n = 7) and Kho-Isaan (KI, n = 7). The muscle and meat characteristics of TNC breeds and their relationship with MyHC expression were examined. Results: Three MyHC isoforms namely MyHC I, MyHC IIa, and MyHC IIx were detected in the muscles. The KL had higher (p<0.05) MyHC IIx than the KI. The IF muscle had higher (p<0.05) MyHC I compared to other muscles. The LT muscle had the least MyHC I. The LT had higher (p<0.05) MyHC IIx than the IF and SS muscles. The IF presented the least MyHC IIx. The KL had higher (p<0.05) lightness and moisture content and lower crude protein, redness, cooking loss, shear force, and calpastatin than the KI. The glycogen, total collagen, soluble collagen, crude protein, ash contents, and troponin T degradation product of IF and SS were lower (p<0.05) than that of LT. Ether extract in LT was lower (p<0.05) than that of IF and SS. The percentage of MyHC I, MyHC IIa, and MyHC IIx were significantly correlated with muscle and meat characteristics of TNC. Conclusion: These results suggest that the differences in the MyHC isoforms may partly account for the variation in meat quality between breeds and among muscles of TNC.
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    Myosin heavy chain isoforms expression, calpain system and quality characteristics of different muscles in goats
    (2020-08-15)
    Chaosap, Chanporn
    ;
    Sitthigripong, Ronachai
    ;
    Sivapirunthep, Panneepa
    ;
    Pungsuk, Apichaya
    ;
    Adeyemi, Kazeem D.
    Myosin heavy chain (MHC) isoforms in goat muscles and their possible relationships with meat quality have not been fully elucidated. This study characterized the MHC isoforms in different caprine muscles using sodium dodecyl sulphate glycerol gel electrophoresis (SDS-GGE). The relationships between MHC isoforms, calpain systems and meat quality characteristics of different muscles in goats were examined. Four muscles, namely infraspinatus (IF), longissimus dorsi (LD), psoas major (PM) and supraspinatus (SS) were obtained from ten Boer crossbred bucks (7–10 months old; 26.5 ± 3.5 kg, BW). The percentages of MHC I, MHC IIa and MHC IIx in SS, IF, PM and LD were 47.2, 38.3, 32.1, 11.9; 28.0, 42.1, 33.0, 36.4; and 24.8, 19.6, 34.9 and 51.7, respectively. IF and SS had higher levels of calpastatin, total collagen and insoluble collagen contents than did PM and LD. PM had longer sarcomere length than did other muscles. LD had higher collagen solubility, troponin-T degradation products and glycogen content than did other muscles. These results infer that variable fiber-type composition could account partially for the differences in the physicochemical properties of goat muscles.