差示扫描量热法检测猪、牛、羊肉加热终点温度

doi:10.3864/j.issn.0578-1752.2015.06.14

摘要/Abstract

摘要： 【目的】利用差示扫描量热法（differential scanning calorimetry，DSC）对猪肉、牛肉和羊肉样进行扫描，寻找其热处理温度与热相图之间的关系，探究一种灵敏、高效的EPT检测方法，为肉制品在实际生产流通中的EPT检测提供理论依据。【方法】将一定体积（2.0 cm×1.0 cm×1.0 cm）的猪肉、牛肉、羊肉块分别进行不同温度（猪肉、羊肉：50℃、60℃、70℃和75℃；牛肉50℃、55℃、65℃、70℃和75℃）的热处理，当达到相应的中心温度时停止加热，冷却至中心温度为4℃，从中心取约100.0 mg肉样（以生肉样为对照）于热分析铝坩埚中，将肉样在坩埚底部压实，并加盖密封，以空坩埚作为参比，4℃条件下隔夜平衡。从40℃加热到80℃，升温速率为1℃/min，样品室氮气流量20 mL·min^-1，保护气流量60 mL·min^-1，进行DSC扫描，由此获得不同温度热处理肉样的DSC热相图。【结果】未经热处理的生猪肉、羊肉、牛肉样经扫描分别得到3个峰，对应不同的起始温度（猪肉：50.83℃、60.54℃、71.02℃；羊肉：50.76℃、59.82℃、70.46℃；牛肉：50.25℃、56.29℃、71.92℃）和变性焓（猪肉：0.4656 J·g^-1、0.1394 J·g^-1、0.2053 J·g^-1; 羊肉：0.0899 J·g^-1、0.3116 J·g^-1、0.3842 J·g^-1；牛肉：0.1078 J·g^-1、0.4151 J·g^-1、0.3662 J·g^-1）。当热处理温度为50℃时，3种肉样的热相图与未经热处理生肉样相比，未出现显著变化；当热处理为60℃（牛肉为55℃）时，3种肉热相图中第1个峰消失，第1个峰和第2个峰的起始温度变化不显著（P＞0.05），但变性焓显著降低（P＜0.05）；当热处理为70℃（牛肉为65℃和70℃）时，3种肉热相图中第2个峰也消失，第3个峰起始温度变化不显著（P＞0.05），变性焓显著降低（P＜0.05）；当热处理温度达到75℃时，猪、牛、羊肉样的3个峰完全消失。可以发现，随着热处理温度的升高，肉样峰对应的变性焓值逐渐降低，不同温度热处理肉样的热相图差异明显，本研究对不同温度热处理肉样检测成功。【结论】通过不同温度处理后肉样的DSC变性峰和变性焓，可知3种肉的热变性程度对温度有特异性。因此，可采用DSC法判定畜肉的热变性程度，从而应用于肉制品加工过程中EPT的检测。

关键词: 猪肉, 牛肉, 羊肉, 差示扫描量热法, 加热终点温度

Abstract: 【Objective】The Differential Scanning Calorimetry (DSC) was used in this test to scan the meat samples of pork, beef and mutton with different heat treatment temperatures. The purpose of this experiment is to study the relationship between the DSC thermogram and the heat treatment temperature of meat samples, to explore a sensitive and high-efficiency method to detect the EPT, in the hope of providing theoretical foundation for EPT detection during the actual production and circulation.【Method】Different heat treatments (for pork and mutton: 50℃, 60℃, 70℃, and 75℃; for beef: 50℃, 55℃, 65℃, 70℃, and 75℃）were carried out on a certain volume (2.0 cm×1.0 cm×1.0 cm) of meat cuboids. The meat cuboids were cooled to 4℃ after the center temperature reached to the aim temperature. The meat samples at 100.0 mg (the raw samples as control) taken from the center of meat cuboid were put into the thermoanalysis aluminium crucible. The crucible was sealed with lid and then balanced for a night at 4℃. A thermal scan was conducted from 40 to 80℃ at a constant heating rate of 1℃/min. The nitrogen flow was 20 mL·min^-1 and the shielding gas flow was 60 mL·min^-1. Finally, DSC thermograms of the meat samples with different center temperatures were obtained.【Result】The result showed that three peaks which had initial temperatures (pork: 50.83℃, 60.54℃, and 71.02℃; mutton: 50.76℃, 59.82℃, and 70.46℃; beef: 50.25℃, 56.29℃, and 71.92℃) and enthalpy of denaturation (pork: 0.4656 J·g^-1, 0.1394 J·g^-1, and 0.2053 J·g^-1; mutton: 0.0899 J·g^-1, 0.3116 J·g^-1, and 0.3842 J·g^-1; beef: 0.1078 J·g^-1, 0.4151 J·g^-1, and 0.3662 J·g^-1), respectively, were obtained from the raw pork, beef and mutton meat samples. The DSC thermograms of the three kinds of meat showed no significant changes when the heat treatment reached 50℃. The first peek vanished when the heat treatment reached 60℃ (for beef it reached 55℃), while, there were no obvious changes (P＞0.05) in the initial temperatures of the second and third peek but the enthalpy of that changed distinctly (P＜0.05). The second peek also disappeared when the heat treatment reached 70℃ (for beef it reached 65℃ and 70℃) and the initial temperatures of the last peeks changed slightly (P＞0.05), but the relevant enthalpy changed significantly (P＜0.05). All the three peaks of pork, beef and mutton meat samples vanished when the heat treatment temperature reached 75℃. It was concluded that the enthalpy of denaturation of the above meat samples gradually decreased and there were significant differences among the DSC thermograms of meat samples dealing with different temperatures. In this study, a success in EPT detection of the meat samples of different heat treatment temperatures was achieved.【Conclusion】Accordingly, the present study demonstrates that the denaturation of the above three kinds of meat has specificity to temperature and DSC can be used in the detection of EPT.

Key words: pork, beef, mutton, differential scanning calorimetry, endpoint temperature

刘功明，孙京新，徐幸莲，黄明，李鹏. 差示扫描量热法检测猪、牛、羊肉加热终点温度[J]. 中国农业科学, 2015, 48(6): 1186-1194.

LIU Gong-ming, SUN Jing-xin, XU Xing-lian, HUANG Ming, LI Peng. Detection of Endpoint Temperature of Pork, Beef and Mutton by Differential Scanning Calorimetry[J]. Scientia Agricultura Sinica, 2015, 48(6): 1186-1194.

0
/ / 推荐

导出引用管理器 EndNote|Reference Manager|ProCite|BibTeX|RefWorks

链接本文: https://www.chinaagrisci.com/CN/10.3864/j.issn.0578-1752.2015.06.14

https://www.chinaagrisci.com/CN/Y2015/V48/I6/1186

参考文献

[1] Musleh U, Shoichiro I, Munehiko T. Coagulation test for determining endpoint temperature of heated blue marlin meat. Fisheries Science, 2000, 66(1): 153-160.

[2] Holownia K, Chinnan M S, Reynolds A E, Davis J W. Relating induced in situ conditions of raw chicken breast meat to pinking. Poultry Science, 2004, 83(1): 109-118.

[3] Tatjana S, Marija J, Tojagic S. Effects of nutrition and heat treatment methods on sensory traits of chicken meat. Acta Agriculturae Serbica, 2006, 21: 11-18.

[4] Sharen S C, Jimmy T K, Smith S B. Lactate dehydrogenase activity in bovine muscle as a means of determining heating endpoint. Journal of Food Science, 1991, 56(4): 895-898.

[5] Ellekjare M R, Isaksson T. Assessments of maximum cooking temperatures in previously heat treated beef. Part 1: Near infrared spectroscopy. Journal of the Science of Food and Agriculture, 1992, 59(3): 335-343.

[6] Thyholt K, Enersen G, Isaksson T. Determination of endpoint temperatures in previously heat treated beef using reflectance spectroscopy. Meat Science, 1998, 48(1): 49-63.

[7] Hsieh Y H P, Zhang S, Chen F C, Sheu S C. Monoclonal antibody- based ELISA for assessment of endpoint heating temperature of ground pork and beef. Journal of Food Science, 2002, 67(3): 1149-1154.

[8] 韩伟, 顾鸣, 杨捷琳, 张柳, 杨峥嵘. 蛋白芯片检测法验证热加工肉及含肉食品的加热效果. 检验检疫科学, 2008, 18(3): 22-24.

Han W, Gu M, Yang J L, Zhang L, Yang Z R. Heating effect validation in processed meat and meat products by automatic protein chip method. Inspection and Quarantine Science, 2008, 18(3): 22-24. (in Chinese)

[9] 毛毛, 高宏伟, 梁成珠, 汪东风. SDS-PAGE电泳法检测鱼肉热处理终点温度. 中国食品学报, 2009, 9(6): 164-169.

Mao M, Gao H W, Liang C Z, Wang D F. Detection of heating endpoint temperature for fish by SDS-PAGE method. Journal of Chinese Institute of Food Science and Technology, 2009, 9(6): 164-169. (in Chinese)

[10] 毛毛, 高宏伟, 梁成珠, 汪东风. 微流芯片分离技术检测烘烤鸡肉源食品热处理终点温度. 食品工业科技, 2009, 30(10): 101-106.

Mao M, Gao H W, Liang C Z, Wang D F. Study on detecting the heating endpoint temperature of the denatured protein in roasted chicken by microfluidic technology. Science and Technology of Food Industry, 2009, 30(10): 101-106. (in Chinese)

[11] 董佩谕, 孙京新, 徐幸莲, 黄明, 冯婷, 王翠燕. SDS-PAGE电泳法检测动物鸡肉蛋白质加热终点温度的研究. 食品工业科技, 2011, 11(32): 65-71.

Dong P Y, Sun J X, Xu X L, Huang M, Feng T, Wang C Y. Research on identification of the endpoint temperature of animal tissue protein through sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Science and Technology of Food Industry, 2011, 11(32): 65-71. (in Chinese)

[12] Hanne C B, Wu Z Y, Frans V B, Henrik J A. NMR relaxometry and differential scanning calorimetry during meat cooking. Meat Science, 2006, 74(4): 684-689.

[13] Svein K S, Agnar H S, Karsten H D, Dagbjorn S. Endpoint temperature of heat-treated surimi can be measured by visible spectroscopy. Food Control, 2012, 26(1): 92-97.

[14] 董佩谕. 动物源性食品加热终点温度检测方法的研究[D]. 青岛: 青岛农业大学, 2011.

Dong P Y. Research on methods for detection of the endpoint temperature of animal origin food [D]. Qingdao: Qingdao Agricultural University, 2011. (in Chinese)

[15] Zhang Z S, Li D, Zhang L X, Liu L Y, Wang X D. Heating effect on the DSC melting curve of flaxseed oil. Journal of Thermal Analysis and Calorimetry, 2014, 115(3): 2129-2135.

[16] 吴海波, 齐宝坤, 江连洲, 李杨, 冯红霞, 曹亮, 马文君, 丁俭, 王瑞. 大豆分离蛋白热性质及其空间构象对表面疏水性的影响. 中国粮油学报, 2014, 29(10): 42-46.

Wu H B, Qi B K, Jiang L Z, Li Y, Feng H X, Cao L, Ma W J, Ding J, Wang R. Effect of thermal properties and spatial conformation of soybean protein isolate on surface hydrophobicity. Journal of the Chinese Cereals and Oils Association, 2014, 29(10): 42-46. (in Chinese)

[17] 乔宁, 张坤生, 任云霞. 超高压对绿豆中4种蛋白质性质的影响. 食品与发酵工业, 2014, 40(10): 83-89.

Qiao N, Zhang K S, Ren Y X. Effects of high pressure on the characteristics of four mung bean proteins. Food and Fermentation Industries, 2014, 40(10): 83-89. (in Chinese)

[18] Shon S R; Chin K B. Evaluation of rheological properties of pork myofibrillar protein with tapioca starch and its utilization to the pork model sausages. Korean Journal for Food Science of Animal Resources, 2012, 32(3): 323-329.

[19] Miyaguchi Y, Hayashi Y, Sakamoto T. Physicochemical properties of the thermal gel of water-washed meat in the presence of the more soluble fraction of porcine sarcoplasmic protein. Animal Science Journal, 2007, 78(1): 77.

[20] Fernández-Martín F, López-López I, Cofrades S, Colmenero F Jiménez. Influence of adding Sea Spaghetti seaweed and replacing the animal fat with olive oil or a konjac gel on pork meat batter gelation. Potential protein/alginate association. Meat Science, 2009, 83(2): 209-217.

[21] Hong I-K, Seung Y. Textural properties and water-holding capacity of broiler breast meat cooked to various internal endpoint temperatures. Food Science and Biotechnology, 2012, 21(5): 1497-1499.

[22] Qiu C J, Xia W S, Jiang Q X. Pressure-induced changes of silver carp (Hypophthalmichthys molitrix) myofibrillar protein structure. European Food Research and Technology, 2014, 83(2): 209-217.

[23] Holownia K, Chinnan M S, Reynolds A E. Cooked chicken breast meat conditions related to simulated pink defect. Food Chemistry and Toxicology, 2004, 69(3): 194-199.

[24] Senter D S, Townsend W E, Searcy G K. Variablility in residual myoglobin content and glutamic oxaloacetic transaminase (GOT) activity in cooked bovine cooking media above endpoint temperature and sample size. Journal of Food Protection, 1994, 57(6): 502-504.

[25] Wang C H, Pestka J J, Booren A M, Smith D M. Lactate dehydrogenase, serum protein, and immunoglobulin G content of uncured turkey thigh rolls as influenced by endpoint cooking temperature. Journal of Agriculture and Food Chemistry, 1994, 42(8): 1829-1833.

[26] Hsiesh C S, Keeton J T, Smith S B. Lactate dehydrogenase activity in bovine muscles as a potential heating endpoint indicator. Journal of Agricultural and Food Chemistry, 1991, 39(7): 1294-1297.

[27] Parsons S E, Patterson R L S. Assessment of the previous heat treatment given to meat products in the temperature range 40–90°C. Part 2: differential scanning calorimetry, a preliminary study. Journal of Food Technology, 1986, 21: 123-131.

[28] Brunton N P, Lyng J G, Zhang L, Jacquier J C. The use of dielectric properties and other physical analyses for assessing protein denaturation in beef biceps femoris muscle during cooking from 5 to 85℃. Meat Science, 2006, 72(2): 236-244.

[29] Bendall J R, Restall D J. The cooking of single myofibres, small myofibre bundles and muscle strips from beef M. Psoas and M. Sternomandibularis muscles at varying heating rates and temperatures. Meat Science, 1983, 8(2): 93-117.

[30] Sims T J, Bailey A J. Structural aspects of cooked meat. In Johnston D E, Knight M K, Ledward D A (eds). The chemistry of muscle based foods. Cambridge: The Royal Society of Chemistry, 1992: 106-127.

[31] Stabursvik E, Martens H. Thermal denaturation of proteins in post rigor muscle tissue as studied by differential scanning calorimetry. Journal of the Science of Food and Agriculture, 1980, 31(10): 1034-1042.

[32] Li C, Wang D Y, Dong H, Xu W, Gao F, Zhou G, Zhang M. Effects of different cooking regimes on the microstructure and tenderness of duck breast muscle. Journal of Food Agriculture and Environment, 2013, 93(8): 1979-1985.