摘要
本研究以两岁龄西门塔尔杂种牛半腱肌为材料,分别用2%、4%、6%的NaCl、1%、3%、5%的焦磷酸二氢二钠(DSPP)、三聚磷酸钠(STPP)、焦磷酸钠(TSPP)和六偏磷酸钠(HMP)溶液在4℃下浸渍1、2、3天,研究这些盐对牛肉的嫩化作用。主要研究结果如下:
1.氯化钠和多聚磷酸盐均能降低牛肉半腱肌的剪切力,而且剪切力随浓度的提高和浸渍时间的延长而降低。各自适宜的嫩化条件为:4%NaCl浸渍2天、5%DSPP、3%STPP、3%TSPP、3%HMP在4℃下浸渍3天。
2.不同浓度的NaCl、STPP、TSPP、HMP浸渍不同时间后都比对照肉重净增百分率高,DSPP处理只有浓度为5%处理3天的样品比对照肉重略有增加,而1%、3%的DSPP不同时间处理后,肉重净增百分率与对照相比则均有所下降。
3.与对照相比,DSPP只有在浓度为5%时蒸煮损失稍有下降,在其它浓度对蒸煮损失没有降低作用,而另外几种盐则不同程度地降低了蒸煮损失。
4.NaCl处理肉样的pH值与对照差异不显著(P>0.05),DSPP处理的肉样pH值比对照低,STPP、TSPP、HMP三种磷酸盐提高了肉的pH值(P<0.05)。
5.经NaCl、STPP、TSPP和HMP处理后,肉样的剪切力均与净增百分率成负相关,与蒸煮损失成正相关,与pH值成负相关,且相关性显著(P<0.01)。而DSPP与净增百分率成负相关,与蒸煮损失成正相关,与pH值成正相关,相关性显著(P<0.01)。
6.经4%NaCl、5%DSPP、3%STPP、3%TSPP、3%HMP处理的肉样,显著提高了胶原蛋白的热溶解度(P<0.01),其中DSPP的效果最明显。NaCl与STPP处理间以及STPP与HMP处理间差异不显著(P>0.05)。
7.在不同温度下测定了剪切力的变化,各种处理的趋势大致相同,都是60℃和80℃各出现一个高峰,90℃时略有下降。
8.对照和DSPP处理样品的肌原纤维结构完好,肌节轮廓完整、清晰可见。NaCl处理的肉样肌节基本上保持原有轮廓,只是稍微模糊,且在Z盘处出现轻微弱化。STPP和TSPP处理的肉样肌节结构受到了破坏,Z盘处发生弱化,甚至出现断裂。肉样经HMP处理后,肌节基本上保持原有结构,只是Z盘处稍有弱化发生。
9.对照样品中肌束膜中胶原纤维结构没有被破坏,呈致密的缆状。NaCl和TSPP处理的样品,胶原纤维分散成更细的原胶原纤维,好像散乱的丝线,且彼此很分散。DSPP处理对胶原纤维的影响不大,结构基本上与对照接近,只是稍稍发生松动。STPP和HMP处理的样品,胶原纤维也分散为原胶原纤维,但原胶原纤维仍彼此很接近。
Semitendinosus muscle obtained from 2-year-old beef carcasses was treated with sodium chloride solutions of 2%,4%,6%,and desodium pyrophosphate, sodium tripolyphosphate, tetrasodium pyrophosphate and hexametaphosphate solutions of 1%,3%,5% respectively, the marinating periods was 1d,2d,3 d. The tenderization of these salts on beef semitendinosus muscle was studied. The main results were given as followed.
l.NaCl and polyphosphates decreased the shear force of semitendinosus muscle, the shear force decreased with increse of concentration of salts and prolongation of marinating time.The moderate conditions of each salt was that 4% NaCl,5%DSPP,3%STPP,3%TSPP,3%HMP marinade 3days at 4 .respectively.
2. Compared with control, NaCI, STPP, TSPP, HMP increased the percentage net weight increase at different concentration and different marinating time, DSPP solution of 5% increased the meat weight slightly after marinating 3 days, the samples treated with the DSPP solutions of 1% and 3% had lower meat weight than the control, irrespective of marinating time.
3. DSPP solution decreased the cooking loss at the concentration of 5% and had no impact on cooking loss at other concentration, but other salts decreased the cooking loss at different concentration.
4. Compared with control, the pH of meat samples treated with NaCI solution had no distinct difference (P>0.05). The meat samples treated with DSPP had lower pH than the control. The solution of STPP, TSPP, HMP increased the pH of beef (P<0.05).
5. After the semitendinosus muscle treated with NaCI,STPP,TSPP and HMP respectively, the shear force had negative correlation with the percentage net weight increase and pH value, had positive correlation with cooking loss (P<0.01). the shear force of the samples treated with DSPP had negative correlation with percentage net weight increase, had positive correlation with cooking loss and pH value (P<0.01).
6. The samples treated with NaCl solution of 4%, DSPP solution of 5%, STPP,TSPP.HMP solution of 3% respectively, the collagen solubility of these samples was markedly raised (P<0.01). No significant difference between NaCl treatment and STPP treatment as well as between STPP treatment and HMP treatment (P>0.05).
7. The changes of shear force at various temperature was determined, the curves trend of
all treatments was similar. There were two peaks at 60 and 80 in every curve, and the curves slightly declined at 90 .
8. The myofibrils of control and DSPP treatments remained integrity, the structure of sarcomere was intact and clear. The sarcomere of NaCl treatment remained original structure basically except that it seemed less pronounced and had slightly weakening at Z disk. The structure of STPP treatmenet and TSPP tueatment was disrupted and the weakening occurred at Z disk ,even the rupture was found. The sarcomere struture of HMP also remained basic structure except the weakening at Z disk.
9. The structure of collagen fibrils in the perimysium of control had no obvious alteration, it seemed like as compact rope. The collagen fibrils of NaCl and STPP treatments disassociated more thinner tropocollagen fibrils which liked disordered silk thread and separated from each other. Except that the fibrils occurred loose, the structure of DSPP treatment had no distinct alteration and was similar with control. The collagen fibrils of STPP treatment and HMP treatmen disassociated tropocollagen fibrils, but they closed with each other.
引文
[1] Hostertker R, Landmann W, Link B, et al. Influence of carcass position during rigor mortis on tenderness of beef muscles: Coparison of two treatments[J]. Journal of Animal Science, 1970, 31(1):47~50.
[2] Takahashi G, Wang S M, Lochner J V, et al. Effects of 2-Hz and 60-Hz electuical stimulation on the micro-structure of beetf[J]. Meat Science, 1987,19(1):65~76.
[3] Ho C, Stromer M H, Robson R M. Effects of electrical stimulation and postmortem storage on changes in Titin, Nebulin, Desmin, Troponin-T and muscle ultrastructure in Bos indicus crossbred cattle[J]. Journal of Animal Science, 1996, 74(7): 1563~1575.
[4] Dransfield E, Etherington D J, Taylor M A J. Modeling post-mortem tenderisation-Ⅱ :enzyme changes during storage of electrically stimulated and non-stimulated beef[J]. Meat Science, 1992, 31(1)75~84.
[5] Ducastaing A, valin C, Schollmeyer J, et al. Effects of electrical stimulation on post-mortem changes in the activities of two Ca dependent neutral proteases and their inhibitor inhibitor in beef muscle[J]. Meat Science, 1985, 15(2):193~202.
[6] Wheeler T L, Savell J W, Cross H R, et al. Effects of Postmortem treatments on the tenderness of meat from hereford, Brahman and Brahman-cross beef cattle[J]. Journal of Animal Science, 1990b, 68(11):3677~3686.
[7] Ferguson D M, Jiang S T, Heamshaw H, et al. Effect of electrical stimulation on protease activity and tenderness of M. Longissimus from cattle with different proportions of Bos indicus content[J].Meat Science, 2000, 55(3):265~272.
[8] 晋艳曦.肉类嫩化新技术—声波嫩化[J].肉品卫生,1999,6,24~25.
[9] Ceftel J c, Culioli J. Effect of high pressure on meat: a review[j]. Meat Science, 1997, 46, (3):211~236.
[10] Homma N, Ikeuchi Y, Suzuki A. Effects of high pressure treatment on the proteolysis enzymes in meat[J]. Meat Science, 1994, 38(3):219~228.
[11] Elgasim E A, Kennick W H, Effects of high pressure on meat microstructure[J], food microstrcture, 1982, 1, 223~245.
[12] Beilken S L, MacFarlane j J, Jones p N. Effect of high pressure during heat treatment on the Warner-Bratzler shear force values of selected beef muscles[j]. Journal of
Food Science, 1990, 55(1)15~18.
[13] MacFarlane J J, Mckenzie I J, Turner R H. Pressure treatment of meat: effects on thermal transitions and shear values[j]. Meat Science, 1980, 5(3):307~317.
[14] Jung S, Ghoul M, Lamballerie-Anton M. Changes in lysosomal enzyme activities and shear values of high pressure treated meat during aging[J].
[15] Koohmaraie M, Whipple G, Crouse J D. Acceleration of post mortem tenderization in lamb and Trahman-cross beef carcasses through infusion of calcium chloride[j]. Journal of Animal Science, 1990, 68(5):1278~1293.
[16] Morgan J B, Miller R K, Mendez F M, et al. Using calcium chloride injection to improve tenderness of beef from mature cows[J]. Journal of Animal Science, 1991, 69(12):4469~4476.
[17] Wheeler T L, Koohmaraie M, Crouse J D. Effects ofcalciu chloride injection and hot boning on the tenderness of round muscles[J]. Joumal of Animal Science, 1991, 69(12):4871~4875.
[18] Hamm R. Post mortem breakdown of ATP and glycogen in ground muscle: a review[J]. Meat Science, 1977, 1(1): 15~39.
[19] Whipple G, Koohmaraie M. Calcium chloride marination effect on beef steak tenderness and calpain proteolytic activity[J]. Meat Science, 1993,33(3):265~275.
[20] Wheeler T L, Kooharaie M, Lansdell J J, et al. Effect of postmortem injiection time, injection level, and concentration of calcium chloride on beef quality traits[J]. Journal of Animal Science, 1993,71(11):2965~2974.
[21] Koohmaraie M, Babiker A S, Schroeder A L, et al. Acceleration of postmortem tenderization in ovine carcasses through activation of Ca~(2+)-dependent protease[J]. Journal of Food Science, 1988b, 53(6):1638~1641.
[22] Polidori P, Marinucci M T, Fantuz F, et al. Tenderization of wether lams meat through pri-rigor infusion of calcium ions[J]. Meat Science, 2000, 55(2):197~200.
[23] Takahashi K, Nakamura F, Hattori A., et al. Paratropomyosin: a new myofibrillar protein that modify characterization[J]. Journal of Biochemestry, 1985, (97): 1039~1043
[24] Lee S, Stevenson-Barry J M, Kauffman R G, et al. Effect of ion fluid injection on
beef tenderness in association with calpain activity[J]. Meat Science, 2000, 56(3):301~310.
[25] Kotula K L, Thelappurath R. Microbiological and sensory attributes of retail cuts of beef treated with acetic and lactic acid solutions[J]. Journal of Food Protection, 1994, 57(5): 665~470.
[26] Wenham I M, Locker R H. The effect of marinading on beef[J]. Journal of the Science of Food and Agriculture, 1976, 27(7):1079~1084.
[27] Eilers J D, Morgan J B, Martin A M, et al. Evaluation of calcium chloride and lactic acid injection on chemical, microbiological and descriptive attributes of mature cow beef[J]. Meat Science, 1994, 38(4):443~451.
[28] Ertbjerg P, Mielche M M, Larsen L M, et al. Relationship between proteolytic changes and tenderness in prerigor lactic acid marinated beef[J]. Journal of the Science of Food and Agriculture, 1999, 79(7):970~978.
[29] Berge P, Ertbjerg P, Larsen L M, et al. Tenderization of beef by lactic acid injected at diferent times post mortem[J]. Meat Science, 2001, 57(4):347~357.
[30] Aktas N, Kaya M. Influence of weak organic acid and salts on the denaturation characteristics of intramuscular connective tissue. A differential scanning calorimetry study[J]. Meat Science, 2001, 58(4):413~419.
[31] Horgan D J, Kurth L B, Kuypers R. pH effect on thermal transition temperature of collagen[J]. Journal of Food Science, 1991, 56(5):1203~1208.
[32] Gault N F S. The relationship between water-holding capcity and cooked meat tenderness in some beef muscles as influenced by acidic conditions below the ultimate pH[J]. Meat Science, 1985, 15(1): 15~30.
[33] Rao M V, Gault N f S. Acetic acid marinating-the rheological characteristics of some raw and cooked beef muscles which contribute to changes in meat tenderness[J]. Journal of Texture Studies, 1990, 21, 455~477.
[34] Oreskovich D C, Bechtel P J, Mckeith F K, et al. Marinade pH affects textural properties of beef[J]. Journal of Food Science, 1992, 57(2):305~311.
[35] Stanton C, Light N D. The effects of conditioning on meat collagen—Part 4. The use of Pre-rigor lactic acid injection to accelerate conditioning in bovine meat[J]. Meat
Science, 1990, 27(2): 141~159.
[36] Maldonado F, Almela F, Casta-Lopez J. The binding of anionic and nonionic surfactants to collagen through the hydrophobic effect[J]. Journal of Protein chemistry, 1991, 10(2): 189~192.
[37] Kawazoye S, Tian S F, Toda S, et al. The mechanism of interaction of sodium dodecyl sulfate with elastic fibers[J]. Journal of Biochemisry, 1995, 117(6):1254~1260.
[38] Mori K, Nishimura T, Yasukawa T, et al. Tenderization of heated sliced beef by succinylated glycerol monostearate, a novel meat tenderizer[J]. Journal of Food Science, 2001, 66(4):524~529.
[39] Kooharaie M, Babiker A S, Merker R A, et al. Role of Ca~(++)-dependent proteases and lysosomal enzymes in postmortem changes in bovine skeletal muuscle[J]. Journal of Food Science, 1988, 53(6): 1253~1257.
[40] Koohmaraie M. Inhibition of postmortem tendeization in ovine carcasses through infusion of zinc[J]. Journal of Animal Science, 1990, 68(5): 1476~1483.
[41] Mestres Prates J A, Ribeire A M, Dias correia A D. Role of cystein endopeptidase in rabbit meat tenderisation and some related changes[J]. Meat Science, 2001, 57(3):283~290.
[42] Bohem M L, Kendall T L, Thompson V F, et al. Changes in the calpains and calpastatin during postmortem storage of bovine muscle[J]. Jorunal of Animal Science, 1998, 76(9):2415~2434.
[43] Huff-Lonergan E, Mitsuhashi T, Beekman D D, et al. Proteolysis of specific muscle structural proteins by μ-caipain at low pH and temperature is similar to degradation in postmortem bovine muscle[J]. Journal of Animal Science, 1996, 74(5):993~1008.
[44] Geesink G H, Koohmaraie M. Effect of calpastain on degradation of myofibrillar proteins by μ-calpain under postmortem conditions[J]. Journal of Animal Science, 1999, 77(10):2685~2692.
[45] 张英君,陈有量.内源蛋白酶在肉成熟嫩化中的作用机理. 肉类工业,2000,(8):31~36.
[46] 杜敏,朱美君.内源蛋白酶与肉的嫩化.肉类研究,1994,(3):13~14,21.
[47] 黄明,罗欣.内源蛋白酶在肉嫩化中作用.肉类研究,1999,(2):9~11.
[48] Kang C K, Warner W D. Tenderization of meat with papaya Latex proteases[J]. Journal of Food Sciene, 1974, 39(4):812~818.
[49] Brooks B A, Klasing K C, regenstein J M. Effects of antemortem injected crude papain in chicken muscle[J]. Journal of Food Science, 1985, 50(6):1370~1374.
[50] Gerelt B, Ikeuchi Y, Suzuki A. Meat Tenderization by proteolytic enzymes after osmotic dehydration[J]. Meat Science, 2000, 56(3):311~318.
[51] Takahashi K. Structural weakening of skeletal muscle tissue during post-mortem aging of meat: the non enzymatic mechanism of meat tenderization[J].Meat Science, 1996, 43(1):67~80.
[52] Dransfield E, Rhodes D N. Effect of Post-rigor muscle length on the texture of meat[J]. Journal of Science of Food and Agriculture, 1976, 27(5):483~486.
[53] Bouton P E, Harris P V, Macfarlane J J. Pressure-heat treatment of meat: effect of prior aging treatments on shear properties[J]. Journal of Food Science, 1980, 45(2):276~278.
[54] Willems M E T, Purslow P P. Effect of post-rigor sarcomere length on mechanical and structural characteristics of raw and heat-denatured single porcine muscle fibres[J]. Journal of Texture Studies, 1996,27,217~233.
[55] Rowe R W D. Collagen fibre arrangement in intramuscular connective tissue. Changes associated with muscle shortening and their possible relevance to raw neat toughness measurements[J]. Journal of Food Tdechnology, 1974, 9, 501~508.
[56] Rowe R W D. The efect of pre-rigor stretch and contractions on the post-rigor geometry of meat samples in relation to meat toughness[J]. Meat Science, 1977,1(2):205~218.
[57] Lepetit J, Grajales A, Favier R. Modelling the effect of sarcoere length on collagen thermal shortening in cooked meat: Consequence on meat toughness[J]. Meat Science, 2000, 54(3):239~250.
[58] Light N, Champion A E, Voyle C et al. The Role of epimysial, perimysial and endomysial collagen in determining texture in six bovine muscles[J]. Meat Science, 1985, 13(2):137~149.
[59] Tornberg E. Biophysical aspects of meat tenderness[J]. Meat Sciene, 1996, 43(S):S175-S191.
[60] Asghar A, Bhatti A R. Endogenous enzymes in skeketal muscle: dtheir significance in muscle physiology and during post mortem aging events in carcasses[J]. Advances in Food Research, 1987, 31, 343~351.
[61] Ouali A. Meat tenderization: possible causes and mechanisms. A review[J]. Journal of Muscle Foods, 1990,1,129~165.
[62] 刘希良,葛长荣.肉品工艺学[M].昆明:云南科技出版社,1997,112~113.
[63] 刘丽,周光宏,王丽哲等.宰后成熟时间对牛肉品质的影响[J].食品科学,2002,23(1):33~36.
[64] McCormick R J. Extracellular modifications to muscle collagen: Inplications for meat quality. Poultry Science, 1999, 78(5):785~791.
[65] Bosselmann A, Moiler C, Steinhan H, et al. Pyridinoline cross-links in bovine muscle collagen. Journal of Food Science, 1995, 60(5):953~958.
[66] 周光宏,徐幸莲.肉品学[M].北京:中国农业科技出版社,1999.
[67] Rowe R W D. Morphology of perimysial and endomysial connective tissue in skeletal musce[J]. Tissue Cell, 1981, 13:681~690.
[68] Nishimura T K, Ojima A, Liu A, et al. Structural changes in the intramuscular connective tissue during development of bovine semitendinosus muscle[J]. Tissue Cell, 1996, 28:527~536.
[69] Davey C L, Gilbert K V. Temperature-dependent cooking toughness in beef[J]. Journal of Science of Food and Agriculture, 1974, 25(7):931~938.
[70] Bouton P E, Harris P V. The effect of cooking temperature and time on some mechanical properties of meat[J]. Journal of Food Science, 1972, 37(1): 140~144.
[71] Lewis G J, Purslow P P. The sturength and stiffness of perimysial connective tissue isolated from cooked beef muscle[J]. Meat Science, 1989, 26(?):255~269.
[72] Lewis G J, Purslow P P, Rice A E. The effect of conditioning on the strength of perimysial connective tissue dissected from cooked meat[J]. Meat Science, 1991, 30(1):1~12.
[73] Mutungi G. Purslow P P, Waukup C. Structural and mechanical changes in raw and
cooked single porcine muscle fibres extended to fracture[J]. Meat Science, 1995, 40(3):217~234.
[74] Mutungi G, Purslow P P, Warkup C. Influence of temperature, fibre diameter and conditioning of the mechanical properties of single muscle fibres extended to fracture[J]. Journal of Science of Food and Agriculture, 1996, 720():359~366.
[75] 钱毅,赵国君.食品分析法[M].上海:上海科学普及出版社,1990.
[76] Bergman I, Loxley R. Two improved and simplified methods for the spectrophotometrie determination of hydroxyproline. Analytical Chemistry, 1963, 35, 1961~1965.
[77] 陈力.电子显微技术教程[M].北京:北京师范大学出版社,1998.
[78] Stanton C, Light N D. The effects of conditioning on meat collagen: Part 1-evidence for gross in situ proteolysis[J]. Meat Science, 1987, 21(4):249~265.
[79] 林杰斌,陈湘,刘明德.SPSS 11统计分析实务设计宝典[M].北京:中国铁道出版社.
[80] Offer G, Knight P. The Structural basis of water-holding in meat. Part 1: general principles and water uptake in meat processing. Developments in Meat Science, 1988, 4, 63~172.
[81] Medynski A, Pospiech E, Kniat R. Effect of various concentrations of lactic acid and sodium chloride on selected physico-chemical meat traits. Meat Science, 2000, 55(3): 285~290.
[82] Hamm R. Biochemistry of meat hydration. Advances in Food Research, 1960, 10, 355~463.
[83] Judge M D, Aberle E D. Effect of chronological age and postmortem aging on thermal shrinkage temperature of bovine intramusclular collagen. Journal of Animal Science, 54(1)68~71.
[84] Lwescher M, Ruege M, Schindler P. Effect of hydration upon the thermal stability of tropocollagen and its dependence of the presence of neutral salts. Biopolymers, 1974, 13, 2489~2492.
[85] Zheng M, Detienne N A, Bames B W, et al. Tenderness and yields of poultry breast are influenced by phosphate type and concentration of marinade. Journal of the Science of Food and Agriculture. 2000, 81, 82~87.