秦川牛花纹肉剪切力值与胶原蛋白吡啶交联 和热溶解性的关系

doi:10.3864/j.issn.0578-1752.2013.01.015

中国农业科学 ›› 2013, Vol. 46 ›› Issue (1): 130-135.doi: 10.3864/j.issn.0578-1752.2013.01.015

秦川牛花纹肉剪切力值与胶原蛋白吡啶交联和热溶解性的关系

卢桂松, 王复龙, 朱易, 万可慧, 彭增起

南京农业大学农业部农畜产品加工与质量控制重点开放实验室，南京 210095

收稿日期:2012-07-11 出版日期:2013-01-01 发布日期:2012-10-24
通讯作者: 通信作者彭增起，Tel：025-84399028；E-mail：zqpeng@njau.edu.cn
作者简介:卢桂松，Tel：13770501565；E-mail：2010108030@njau.edu.cn
基金资助:
现代农业产业技术体系建设专项资金项目（NYCYTX-38）

Study on the Relationships Between Pyridinoline Cross-Links and Solubility of Collagen and Shear Force of Qinchuan Marbling Beef

LU Gui-Song, WANG Fu-Long, ZHU Yi, WAN Ke-Hui, PENG Zeng-Qi

Key Laboratory of Agricultural and Animal Products Processing and Quality Control, Ministry of Agriculture, Nanjing Agricultural University, Nanjing 210095

Received:2012-07-11 Online:2013-01-01 Published:2012-10-24

摘要/Abstract

摘要： 【目的】通过对花纹肉剪切力值与胶原蛋白吡啶交联含量的对比研究，发掘脂肪沉积改善牛肉嫩度的内在原因。【方法】以秦川公牛花纹肉为试验材料，研究相同年龄不同花纹等级、相同花纹等级不同年龄的牛肉样品剪切力值、胶原蛋白热溶解性以及吡啶交联含量的变化规律。【结果】对花纹等级相同（B级）的西冷来说，随着年龄的增长，羟赖氨酰吡啶嗡（HP）交联逐渐增加，赖氨酰吡啶嗡（LP）交联先增加后减少，胶原蛋白热溶解性下降，牛肉剪切力值增加；对相同年龄的西冷来说（4对永久齿），随着花纹等级的提高，HP交联含量逐渐减少，胶原蛋白热溶解性升高，牛肉剪切力值下降。【结论】脂肪沉积过程中，胶原蛋白中HP交联受抑，胶原蛋白未能形成丰富的成熟交联，加热时更容易形成明胶，使牛肉剪切力值下降，嫩度提高。

关键词: 牛肉 , 大理石纹 , 羟赖氨酰吡啶嗡 , 赖氨酰吡啶嗡 , 嫩度 , 吡啶啉

Abstract: 【Objective】 The objective of this experiment is to study the pyridinoline cross-links of collagen and dissect its relevance to the shear force of beef.【Method】 Samples were divided into two groups. The first group consists of the same marbling with different ages. The second consists of the same age with different marblings. The shear force of beef, solubility and hydroxylysylpyridinium, lysylpyridinium of collagen were measured. 【Result】According to the results of the first group, as bull aged, HP cross-links increased, LP cross-links increased firstly, and then decreased, which was followed by the decreasing of collagen solubility and the increasing of shear force. According to the results of the second group, as fattening, HP cross-links decreased, the solubility of collagen increased, and the shear force of beef decreased. 【Conclusion】In the fattening, the synthesization of HP cross-link was restrained. There are shorts of mature cross-links in collagen, resulting in transition of gelatin more easily. So beef turns tenderer.

Key words: beef , marbling , hydroxylysylpyridinium , lysylpyridinium , tenderness , pyridinoline

卢桂松, 王复龙, 朱易, 万可慧, 彭增起. 秦川牛花纹肉剪切力值与胶原蛋白吡啶交联和热溶解性的关系[J]. 中国农业科学, 2013, 46(1): 130-135.

LU Gui-Song, WANG Fu-Long, ZHU Yi, WAN Ke-Hui, PENG Zeng-Qi. Study on the Relationships Between Pyridinoline Cross-Links and Solubility of Collagen and Shear Force of Qinchuan Marbling Beef[J]. Scientia Agricultura Sinica, 2013, 46(1): 130-135.

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参考文献

[1]NY/T676. 牛肉等级规格. 2010.

NY/T676. Beef Quality Grading. 2010. (in Chinese)

[2]Xiong Y L, Mullins O E, Stika J F, Chen J, Blanchard S P, Moody W G. Tenderness and oxidative stability of post-mortem muscles from mature cows of various ages. Meat Science, 2007, 77(1): 105-113.

[3]Schönfeldt H C, Strydom P E. Effect of age and cut on tenderness of South African beef. Meat Science, 2011, 87(3): 206-218.

[4]Nishimura T, Hattori A, Takahashi K. Structural changes in intramuscular connective tissue during the fattening of Japanese black cattle: effect of marbling on beef tenderization. Journal of Animal Science, 1999, 77(1): 93-104.

[5]李卫林, 曹健. 胶原蛋白结构和稳定性关系研究. 中国皮革, 2005, 34(23): 14-16.

Li W L, Cao J. Study on the structure and stability of collagen. China Leather, 2005, 34(23): 14-16. (in Chinese)

[6]Ranmshaw J A, Shah N K, Brodsky B. Gly-X-Y triple-tide frequencies in collagen: a context for host-guest triple-helical peptide. Journal of Structure Biology, 1998, 23(7): 86-91.

[7]Ngapo T M, Berge P, Culioli J, Dransfield E, De Smet S, Claeys E. Perimysial collagen crosslinking and meat tenderness in Belgian Blue double-muscled cattle. Meat Science, 2002, 61(1): 91-102.

[8]Knott L, Bailey A J. Collagen cross-links in mineralizing tissues: A review of their chemistry, function, and clinical relevance. Bone, 1998, 23(3): 181-187.

[9]Banse X, Devogelaer J P, Lafosse A, Sims T J, Grynpas M, Bailey A J. Cross-link profile of bone collagen correlates with structural organization of trabeculae. Bone, 2002, 31(1): 70-76.

[10]Lepetit J. A theoretical approach of the relationships between collagen content, collagen cross-links and meat tenderness. Meat Science, 2007, 76(1): 147-159.

[11]Atley L M, Mort J S, Lalumiere M, Eyre D R. Proteolysis of human bone collagen by cathepsin K: characterization of the cleavage sites generating the cross-linked N-telopeptide neoepitope. Bone, 2000, 26(3): 241-247.

[12]Bailey A J, Shimokomaki M S. Age related changes in the reducible cross-links of collagen. FEBS Letters, 1971, 16(2): 86-88.

[13]Field R A, McCormick R J, Brown D R, Snowder G D. Collagen crosslinks in longissimus muscle from lambs expressing the callipyge gene. Journal of Animal Science, 1996, 74(12): 2943-2947.

[14]Palka K. The influence of post-mortem ageing and roasting on the microstructure, texture, and collagen solubility of bovine semitendinosus muscle. Meat Science, 2003, 64(2): 191-198.

[15]GB/T9695.23. 肉与肉制品羟脯氨酸含量测定. 2008.

GB/T9695.23. Meat and Meat Products-Determination of Hydroxyproline Content. 2008. (in Chinese)

[16]陈伯华.通过牙齿判断牛的年龄.山西农业, 2002, 1(1): 32-33.

Chen B H. How to know the age of cow by teeth? Shanxi Agriculture, 2002, 1(1):32-33. (in Chinese)

[17]Lepetit J. Collagen contribution to meat toughness: Theoretical aspects. Meat Science, 2008, 80(4): 960-967.

[18]Nishimura T. The role of intramuscular connective tissue in meat texture. Animal Science Journal, 2010, 81(1): 21-27.

[19]Shoulders M D, Raines R T. Collagen structure and stability. Annual Review of Biochemistry, 2009, 78(1): 929-958.

[20]Wang X, Shen X, Li X, Agrawal M. Age-related changes in the collagen network and toughness. Bone, 2002, 31(1): 1-7.

[21]Young O A, Braggins T J. Tenderness of ovine semimembranosus: Is collagen concentration or solubility the critical factor? Meat Science, 1993, 35(2): 213-222.

[22]Avery N C, Sims T J, Warkup C, Bailey A J. Collagen cross-linking in porcine longissimus lumborum: Absence of a relationship with variation in texture at pork weight. Meat Science, 1996, 42(3): 355-369.

[23]Eyre D R, Koob T J, van Ness K P. Quantization of hydroxypyridinium crosslinks in collagen by high-performance liquid chromatography. Analytical Biochemistry, 1984, 137(2): 380-388.

[24]Bosselmann A, Steinhart H, Möller C, Kirchgessner M, Schwarz F J. Pyridinoline cross-links in bovine muscle collagen. Journal of Food Science, 1995, 60(5): 953-957.

[25]Slatter D A, Avery N C, Bailey A J. Collagen in its fibrillar state is protected from glycation. The International Journal of Biochemistry & Cell Biology, 2008, 40(10): 2253-2263.

[26]Eyre D R, Paz M A, Gallop P M. Cross-linking in collagen and elastin. Annual Review of Biochemistry, 1984, 53(1): 717-748.

[27]Reiser K, McCormick R J, Rucker R B. Enzymatic and nonenzymatic cross-linking of collagen and elastin. The FASEB Journal, 1992, 6(7): 2439-2449.

[28]van der Slot A J, Zuurmond A M, van den Bogaerdt A J, Ulrich M M, Middlekoop E, Boers W, Kard Ronday H, DeGroot J, Huizinga T W, Bank R A. Increased formation of pyridinoline cross-links due to higher telopeptide lysyl hydroxylase levels is a general fibrotic phenomenon. Matrix Biology, 2004, 23(4): 251-257.

秦川牛花纹肉剪切力值与胶原蛋白吡啶交联和热溶解性的关系

Study on the Relationships Between Pyridinoline Cross-Links and Solubility of Collagen and Shear Force of Qinchuan Marbling Beef

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秦川牛花纹肉剪切力值与胶原蛋白吡啶交联 和热溶解性的关系

Study on the Relationships Between Pyridinoline Cross-Links and Solubility of Collagen and Shear Force of Qinchuan Marbling Beef

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秦川牛花纹肉剪切力值与胶原蛋白吡啶交联和热溶解性的关系