卤牛肉加工过程中蛋白质组成的变化
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摘要
为探讨蛋白质在卤牛肉品质形成中的作用,研究卤牛肉加工过程中蛋白质组成的变化。碱溶蛋白(NPN)是牛肉中主要的蛋白质组分。腌制过程中,牛肉中NPN含量在0～12h时下降(p<0.05)后有所增大(p>0.05),水溶蛋白和盐溶蛋白的含量均明显下降(p<0.05),碱溶蛋白和碱不溶蛋白的含量均略下降(p>0.05)。出水过程中,牛肉中碱溶蛋白、水溶蛋白和盐溶蛋白的含量及蛋白质总量均显著下降(p<0.05),碱不溶蛋白含量略下降(p>0.05);碱溶蛋白含量在0～6min时明显增大(p<0.05),随后显著降低(p<0.05)。卤制过程中,牛肉中NPN含量明显增大(p<0.05),水溶蛋白、盐溶蛋白、碱溶蛋白的含量及蛋白质总量均明显降低(p<0.05),碱不溶蛋白含量稍下降(p>0.05)。
In order to investigate the role of protein in the quality formation of marinated beef, the change in protein composition during the processing of marinated beef was studied. Alkali-soluble protein(NPN) was the major protein component in beef. During the curing process, the content of NPN in beef decreased from 0 to 12 h(p<0.05) and then increased slightly(p>0.05), and the contents of water-soluble protein and salt-soluble protein decreased significantly(p<0.05), and the contents of alkali-soluble protein and alkali-insoluble protein decreased slightly(p>0.05). During the effluent process, the content of alkali-soluble protein, water-soluble protein and salt-soluble protein and total protein in beef decreased significantly(p<0.05), and the content of alkali-insoluble protein decreased slightly(p>0.05). The content of alkali-soluble protein increased significantly(p<0.05) at 0-6 min, and then decreased significantly(p<0.05). During the marinating process, the content of NPN in beef increased significantly(p<0.05), and the content of water-soluble protein, salt-soluble protein, alkali-soluble protein and total protein all decreased significantly(p<0.05), and the content of alkali-insoluble protein decreased slightly(p<0.05).
In order to investigate the role of protein in the quality formation of marinated beef, the change in protein composition during the processing of marinated beef was studied. Alkali-soluble protein(NPN) was the major protein component in beef. During the curing process, the content of NPN in beef decreased from 0 to 12 h(p<0.05) and then increased slightly(p>0.05), and the contents of water-soluble protein and salt-soluble protein decreased significantly(p<0.05), and the contents of alkali-soluble protein and alkali-insoluble protein decreased slightly(p>0.05). During the effluent process, the content of alkali-soluble protein, water-soluble protein and salt-soluble protein and total protein in beef decreased significantly(p<0.05), and the content of alkali-insoluble protein decreased slightly(p>0.05). The content of alkali-soluble protein increased significantly(p<0.05) at 0-6 min, and then decreased significantly(p<0.05). During the marinating process, the content of NPN in beef increased significantly(p<0.05), and the content of water-soluble protein, salt-soluble protein, alkali-soluble protein and total protein all decreased significantly(p<0.05), and the content of alkali-insoluble protein decreased slightly(p<0.05).
引文
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6 Kanner J, Harel S. Initiation of membranal lipid peroxidation by activated metmyoglobin and methemoglobin. Archives of Biochemistry and Biophysics,1985,(237):314-321
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8 Bertram HC, Engelsen SB, Busk H, Karlsson AH, Andersen HJ. Water properties during cooking of pork studied by low-field NMR reaxation: effects of cuing and the RN--gene. Meat Science,2004,(66):437-446
9 Bertram HC, Kristensen M, Andersen HJ. Functionality of myofibrillar proteins as affected by pH, ionic strenghth and heat treatment—a low-field NMR study. Meat Science,2004,(68):249-256
10 周雪松,赵谋明,林伟锋等.鸡肉蛋白质组成与分离研究[J].食品与发酵工业,2005,31(10):9-12
2 Brunton NP, Lyng JG, Zhang L, Jacquier JC. The use of dielectric properties and other physical analyses for assessing protein denaturation in beefbiceps femoris muscle during cooking from 5 to 85 ℃. Meat Science,2006,(72):236-244
3 Bendall JR, Restall DJ. The cooking of single myofibres, small myofibre bundles and muscle strips fromM. Psoas and M. Sternomandibularis muscle at varying heating rates and temperatures. Meat Science,1983,8(2):93-117
4 Bertram HC, Kristensen M, Ostdal H, Baron CP, Young JF, Andersen HJ.Does oxidation affect the water functionality of myofibrillar proteins. Journal of Agricultural and Food Chemistry,2007,(55):2342-2348
5 Han MY, Zhang YJ, Fei Y, Xu XL, Zhou GH. Effect of micorbial transglutaminase on NMR relaxometry and microstructure of pork myofibrillar protein gel. European Food Research Technology,2009,(228):665-670
6 Kanner J, Harel S. Initiation of membranal lipid peroxidation by activated metmyoglobin and methemoglobin. Archives of Biochemistry and Biophysics,1985,(237):314-321
7 Batifoulier F, Mercier Y, Gatellier P, Renerre M. Influence of vitamin E on lipid and protein oxidation induced by H2O2-activated MetMb in microsomal membranes from turkey muscle. Meat Science,2002,61(4),389-395
8 Bertram HC, Engelsen SB, Busk H, Karlsson AH, Andersen HJ. Water properties during cooking of pork studied by low-field NMR reaxation: effects of cuing and the RN--gene. Meat Science,2004,(66):437-446
9 Bertram HC, Kristensen M, Andersen HJ. Functionality of myofibrillar proteins as affected by pH, ionic strenghth and heat treatment—a low-field NMR study. Meat Science,2004,(68):249-256
10 周雪松,赵谋明,林伟锋等.鸡肉蛋白质组成与分离研究[J].食品与发酵工业,2005,31(10):9-12