极限pH对羊肉宰后成熟过程中肌原纤维蛋白特型的影响
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摘要
为了研究羊肉宰后成熟过程中极限pH对肌原纤维蛋白特型即肌联蛋白、伴肌动蛋白、肌间线蛋白和肌钙蛋白-T降解及肌原纤维小片化指数的影响。本文选取50只羊的右侧背最长肌,贮存于4℃条件下,在宰后时间点分别为1 h、1、2、3、5 d和7 d时,测定其pH。按照宰后2 d的pH将肉样分成三组:高极限pH组(5.72±0.03),中极限pH组(5.54±0.01)和低极限pH组(5.40±0.02)。在每个宰后时间点,测定肌联蛋白、伴肌动蛋白、肌间线蛋白、肌钙蛋白-T降解程度和肌原纤维小片化指数(MFI)。结果表明:肌联蛋白在高极限pH组中宰后1 d开始降解;在宰后1 d时,高极限pH组肌间线蛋白相对灰度值显著低于中极限pH组和低极限p H组(p <0.05);肌钙蛋白-T在高极限pH组中,宰后1 d已出现降解条带。而伴肌动蛋白在中极限pH组中降解较快,在宰后1 d开始降解。另外在宰后1、2、3、5、7 d时,高极限pH组和中极限pH组的肌原纤维小片化指数显著高于低极限pH组的肌原纤维小片化指数(p <0.05)。极限pH通过影响这些肌原纤维蛋白降解来促进宰后肌肉成熟过程并且肌联蛋白、肌间线蛋白和肌钙蛋白-T的降解,加快了宰后前期嫩化过程。这为揭示宰后肉嫩度形成机理提供理论基础。
This study was aimed to investigate effects of muscle ultimate p H( pH_u) on titin,nebulin,desmin,troponin-T degradation and myofibril fragmentation index( MFI) in ovine muscle. After 50 animals were slaughtered,the right longissimus lumborum( LL) muscles were stored at 4 ℃ for 7 d.Based on muscle the p H at post-mortem 2 d,muscles were classified into three groups: the high pH_u( 5.72 ± 0.03),intermediate pH_u( 5.54 ± 0.01) and low pH_u( 5.40 ± 0.02) muscles.Muscle pH,MFI and degradation of titin,nebulin,desmin and troponin-T were measured at 1 h,1,2,3,5 and 7 days postmortem. The data obtained showed that titin started to the degradation in the high pH_u muscles on day 1 postmortem. On day 1 postmortem,the intensity of desmin was lowest in the high pH_u muscles than that that in intermediate and low pH_u( p < 0.05).Degradation of troponin-T occurred on day 1 postmortem in the high pH_u muscles. But degradation of nebulin was observed on day 1postmortem in the intermediate pH_u muscles.At the same time,meat in high and intermediate pH_u groups had higher MFI than that in low pH_u group at 1,2,3,5 and 7 days postmortem( p < 0.05).The study showed that muscle ultimate pH influenced the degradation of these myofibrillar proteins postmortem and thus meat tenderization.Degradation of titin,desmin and troponin-T improved directly meat tenderness in early stage of ageing. This provided a theoretical basis for mechanisms involved in tenderization of meat.
This study was aimed to investigate effects of muscle ultimate p H( pH_u) on titin,nebulin,desmin,troponin-T degradation and myofibril fragmentation index( MFI) in ovine muscle. After 50 animals were slaughtered,the right longissimus lumborum( LL) muscles were stored at 4 ℃ for 7 d.Based on muscle the p H at post-mortem 2 d,muscles were classified into three groups: the high pH_u( 5.72 ± 0.03),intermediate pH_u( 5.54 ± 0.01) and low pH_u( 5.40 ± 0.02) muscles.Muscle pH,MFI and degradation of titin,nebulin,desmin and troponin-T were measured at 1 h,1,2,3,5 and 7 days postmortem. The data obtained showed that titin started to the degradation in the high pH_u muscles on day 1 postmortem. On day 1 postmortem,the intensity of desmin was lowest in the high pH_u muscles than that that in intermediate and low pH_u( p < 0.05).Degradation of troponin-T occurred on day 1 postmortem in the high pH_u muscles. But degradation of nebulin was observed on day 1postmortem in the intermediate pH_u muscles.At the same time,meat in high and intermediate pH_u groups had higher MFI than that in low pH_u group at 1,2,3,5 and 7 days postmortem( p < 0.05).The study showed that muscle ultimate pH influenced the degradation of these myofibrillar proteins postmortem and thus meat tenderization.Degradation of titin,desmin and troponin-T improved directly meat tenderness in early stage of ageing. This provided a theoretical basis for mechanisms involved in tenderization of meat.
引文
[1]吴菊清,李春保,周光宏,等.宰后成熟过程中冷却牛肉、猪肉色泽和嫩度的变化[J].食品科学,2008,29(10):136-139.
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[9]Huff-Lonergan E,Zhang W,Lonergan S M.Biochemistry of postmortem muscle-lessons on mechanisms of meat tenderization[J].Meat Science,2010,86(1):184-195.
[10]杜雪莉,蔡秋凤,蔡阳鹏,等.黄鳍鲷肌肉中肌联蛋白的纯化、抗体制备与性质分析[J].食品科学,2006,27(12):463-466.
[11]Tomaszewska-Gras J,Schreurs F J,Kijowski J.Post mortem development of meat quality as related to changes in cytoskeletal proteins of chicken muscles[J]. British Poultry Science,2011,52(2):189-201.
[12]李桂霞,李欣,李铮,等.宰后僵直及成熟过程中羊背最长肌理化性质的变化[J].食品科学,2017,38(21):112-118.
[13]Lokman N S,Sabow A B,Abubakar A A,et al.Comparison of carcass and meat quality in goats subjected to preslaughter headonly electrical stunning or slaughtered without stunning[J].CyTA-Journal of Food,2017,15(1):1-6.
[14]Rajagopal K,Oommen G T.Myofibril fragmentation index as an immediate postmortem predictor of buffalo meat tenderness[J]. Journal of Food Procesing&Preservation,2014,39(6):1-8.
[15]高星,李欣,李铮,等.宰后肌肉中肌球蛋白磷酸化调控激动求蛋白解离作用机制[J].中国农业科学,2016,49(16):3199-3207.
[16]Wang Y,Li X,Li Z,et al. Changes in degradation and phosphorylation level of titin in three ovine muscles during postmortem[J]. International Journal of Food Science&Technology,2018,53:913-920.
[17]Li Z,Li X,Gao X,et al. Phosphorylation prevents in vitro myofibrillar proteins degradation by μ-calpain[J]. Food Chemistry,2017,218:455-462.
[18]Rajagopal K,Oommen G T.Myofibril fragmentation index as an immediate postmortem predictor of buffalo meat tenderness[J]. Journal of Food Processing&Preservation,2014,39(6):1-8.
[19]王永辉,马俪珍,张建荣,等.特种野猪和普通家猪宰后pH变化分析[J].肉类研究,2006(4):40-43.
[20]Bouton P E,Harris P V,Shorthose W R. The Effects of ultimate pH on ovine muscle:water-holding capacity[J]. Journal of Food Science,2010,37(3):351-355.
[21]Honikel K O.Chemical and physical characteristics of meat pH measurement[J]. Encyclopedia of Meat Science,2014:262-266.
[22]王强,吴建平,张玉斌,等.钙蛋白酶的活性调节及其与肉嫩度的关系[J].食品科技,2007(12):115-118.
[23]Du M,Li X,Li Z,et al.Phosphorylation inhibits the activity of μ-calpain at different incubation temperatures and Ca~(2+) concentrations in vitro[J].Food Chemistry,2017,228:649-655.
[24]Koohmaraie M,Geesink G H. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system[J].Meat Science,2006,74(1):34-43.
[25]陈琳,唐玮,徐幸莲,等.溶酶体中的组织蛋白酶及其在肌肉成熟中的作用[J].江西农业学报,2008,20(2):72-75.
[26]Sentandreu E,Carbonell J V,Sendra J M. Monitoring of chemical and enzymatic hydrolysis of water-soluble proteins using flow-injection analysis with fluorescence detection and an aqueous eluant containing 2-p-toluidinylnaphthalene-6-sulfonate as the fluorescent probe[J]. Biotechnology&Bioengineering,2002,78(7):829-883.
[27]王莉,王玉涛,郭丽君,等.电刺激对宰后牦牛肉成熟过程中肌钙蛋白-T和肌间线蛋白及嫩度的影响[J].食品工业科技,2017,38(11):65-75.
[28]Li Z,Li X,Gao X,et al.Effect of inhibition ofμ-calpain on the myofibril structure and myofibrillar protein degradation in postmortem ovine muscle[J]. Journal of the Science of Food&Agriculture,2016,97(7):2122-2131.
[29]Marino R,Albenzio M,Malva A,et al.Proteolytic pattern of myofibrillar protein and meat tenderness as affected by breed and aging time[J].Meat Science,2013,95(2):281-287.
[2]曹宪福,杨志成,姜廷波,等.肌肉嫩度的影响因素分析[J].黑龙江畜牧兽医,2016(11):60-63.
[3]Silva J A,Patarata L,Martins C.Influence of ultimate pH on bovine meat tenderness during ageing[J].Meat Science,1999,52(4):453-459.
[4]Purchas R W,Yan X,Hartley D G.The influence of a period of ageing on the relationship between ultimate pH and shearvalues of beef M. longissimus thoracis[J]. Meat Science,1999,51(2):135-141.
[5]JeleníkováJ,Pipek P,Staruch L. The influence of antemortem treatment on relationship between pH and tenderness of beef[J].Meat Science,2008,80(3):870-874.
[6]Pulford D J,Vazquez S,Frost D F,et al. The intracellular distribution of small heat shock proteins in post-mortem beef is determined by ultimate pH[J]. Meat Science,2008,79(4):623-630.
[7]Wu G,Farouk M M,Clerens S,et al.Effect of beef ultimate pH and large structural changes with aging on meat tenderness[J]. Meat Science,2014,98(4):637-645.
[8]Lomiwes D,Farouk M M,Wu G,et al. The development of meat tenderness is likely to be compartmentalised by ultimate pH[J].Meat Science,2014,96(1):646-651.
[9]Huff-Lonergan E,Zhang W,Lonergan S M.Biochemistry of postmortem muscle-lessons on mechanisms of meat tenderization[J].Meat Science,2010,86(1):184-195.
[10]杜雪莉,蔡秋凤,蔡阳鹏,等.黄鳍鲷肌肉中肌联蛋白的纯化、抗体制备与性质分析[J].食品科学,2006,27(12):463-466.
[11]Tomaszewska-Gras J,Schreurs F J,Kijowski J.Post mortem development of meat quality as related to changes in cytoskeletal proteins of chicken muscles[J]. British Poultry Science,2011,52(2):189-201.
[12]李桂霞,李欣,李铮,等.宰后僵直及成熟过程中羊背最长肌理化性质的变化[J].食品科学,2017,38(21):112-118.
[13]Lokman N S,Sabow A B,Abubakar A A,et al.Comparison of carcass and meat quality in goats subjected to preslaughter headonly electrical stunning or slaughtered without stunning[J].CyTA-Journal of Food,2017,15(1):1-6.
[14]Rajagopal K,Oommen G T.Myofibril fragmentation index as an immediate postmortem predictor of buffalo meat tenderness[J]. Journal of Food Procesing&Preservation,2014,39(6):1-8.
[15]高星,李欣,李铮,等.宰后肌肉中肌球蛋白磷酸化调控激动求蛋白解离作用机制[J].中国农业科学,2016,49(16):3199-3207.
[16]Wang Y,Li X,Li Z,et al. Changes in degradation and phosphorylation level of titin in three ovine muscles during postmortem[J]. International Journal of Food Science&Technology,2018,53:913-920.
[17]Li Z,Li X,Gao X,et al. Phosphorylation prevents in vitro myofibrillar proteins degradation by μ-calpain[J]. Food Chemistry,2017,218:455-462.
[18]Rajagopal K,Oommen G T.Myofibril fragmentation index as an immediate postmortem predictor of buffalo meat tenderness[J]. Journal of Food Processing&Preservation,2014,39(6):1-8.
[19]王永辉,马俪珍,张建荣,等.特种野猪和普通家猪宰后pH变化分析[J].肉类研究,2006(4):40-43.
[20]Bouton P E,Harris P V,Shorthose W R. The Effects of ultimate pH on ovine muscle:water-holding capacity[J]. Journal of Food Science,2010,37(3):351-355.
[21]Honikel K O.Chemical and physical characteristics of meat pH measurement[J]. Encyclopedia of Meat Science,2014:262-266.
[22]王强,吴建平,张玉斌,等.钙蛋白酶的活性调节及其与肉嫩度的关系[J].食品科技,2007(12):115-118.
[23]Du M,Li X,Li Z,et al.Phosphorylation inhibits the activity of μ-calpain at different incubation temperatures and Ca~(2+) concentrations in vitro[J].Food Chemistry,2017,228:649-655.
[24]Koohmaraie M,Geesink G H. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system[J].Meat Science,2006,74(1):34-43.
[25]陈琳,唐玮,徐幸莲,等.溶酶体中的组织蛋白酶及其在肌肉成熟中的作用[J].江西农业学报,2008,20(2):72-75.
[26]Sentandreu E,Carbonell J V,Sendra J M. Monitoring of chemical and enzymatic hydrolysis of water-soluble proteins using flow-injection analysis with fluorescence detection and an aqueous eluant containing 2-p-toluidinylnaphthalene-6-sulfonate as the fluorescent probe[J]. Biotechnology&Bioengineering,2002,78(7):829-883.
[27]王莉,王玉涛,郭丽君,等.电刺激对宰后牦牛肉成熟过程中肌钙蛋白-T和肌间线蛋白及嫩度的影响[J].食品工业科技,2017,38(11):65-75.
[28]Li Z,Li X,Gao X,et al.Effect of inhibition ofμ-calpain on the myofibril structure and myofibrillar protein degradation in postmortem ovine muscle[J]. Journal of the Science of Food&Agriculture,2016,97(7):2122-2131.
[29]Marino R,Albenzio M,Malva A,et al.Proteolytic pattern of myofibrillar protein and meat tenderness as affected by breed and aging time[J].Meat Science,2013,95(2):281-287.