以肉牛蹄皮为试材,分别在75、80、85、90和95 ℃加热30、40、50、60和70 min,分析加热过程中牛蹄皮胶原蛋白含量及热溶解性变化,观察牛蹄皮微观结构的改变,测定其剪切力、蒸煮损失和质构特性变化。结果表明:随加热时间的延长和温度的升高,可溶解胶原蛋白含量和胶原蛋白溶解度逐渐增大(P<0.05),不可溶解胶原蛋白含量整体呈下降趋势,牛皮组织中胶原纤维间距增大,紧密度降低,同时牛蹄皮剪切力、硬度、咀嚼性和黏聚性逐渐减小,蒸煮损失逐渐增大。90～95 ℃加热50～60 min时牛蹄皮胶原蛋白溶解性大,组织松散,剪切力、硬度和咀嚼性均较低,牛蹄皮嫩度较好,该研究可为牛蹄皮加热类菜肴的工业化生产提供科学理论指导。
The effects of heating temperature and time on the connective tissue properties and tenderness of bovine hoof skin were studied to provide technical support and theoretical basis for the comprehensive utilization of bovine hoof. The cattle hoof skin was used as materials, which were heated respectively at 75, 80, 85, 90 and 95 °C for 30, 40, 50, 60 and 70 min to analyze the changes of collagen content and thermal solubility of bovine hoof skin during heating process. The changes in the microstructure of the hoof skin were observed and the shear force, cooking loss, texture characteristics were determined. The study showed that with the prolongation of heating time and temperature, the soluble collagen content and collagen solubility were gradually increased (P<0.05), while the insoluble collagen content was decreased as a whole. Meanwhile, the collagen fiber spacing showed an increase, and the tightness exhibited a decrease. Also, the values of shearing force, hardness, chewiness and cohesiveness were gradually reduced, and the cooking loss was gradually increased. The results indicated that, when heated at 90-95 ℃ for 50-60 min, the bovine hoof skin featured high solubility, loose tissue, low shearing force, hardness and chewiness, which resulted in good tenderness. Therefore, this study provides scientific theoretical guidance for the industrial production of bovine hoof skin hot dishes.
[1] 郭兆斌,余群力.牛副产物—脏器的开发利用现状[J].肉类研究,2011,25(3):35-37.
[2] 卢骁,朱立贤,毛衍伟,等.DFD牛肉研究进展[J].食品科学,2015,36(19):271-276.
[3] CHRISTENSEN L,ERTBJERG P,LØJE H,et al.Relationship between meat toughness and properties of connective tissue from cows and young bulls heat treated at low temperatures for prolonged times[J].Meat Science,2013,93(4):787-795.
[4] 冯宪超,周光宏.快速冷冻工艺对牛肉品质和组织结构的影响[J].食品科学,2016,37(19):1-7.
[5] MILLER M F,CARR M A,RAMSEY C B,et al.Consumer thresholds for establishing the value of beef tenderness[J].Journal of Animal Science,2001,79(12):3 062-3 068.
[6] BOBACK S M,COX C L,OTT B D,et al.Cooking and grinding reduces the cost of meat digestion[J].Comparative Biochemistry and Physiology-Part A: Molecular & Integrative Physiology,2007,148(3):651-656.
[7] GONZALEZ J M,JOHNSON D D,ELZO M A,et al.Effect of brahman genetic influence on collagen enzymatic crosslinking gene expression and meat tenderness[J].Animal Biotechnology,2014,25(3):165-178.
[8] PULGAR J S D,GÁZQUEZ A,RUIZ-CARRASCAL J.Physico-chemical, textural and structural characteristics of sous-vide cooked pork cheeks as affected by vacuum, cooking temperature, and cooking time[J].Meat Science,2012,90(3):828-835.
[9] 常海军.不同加工条件下牛肉肌内胶原蛋白特性变化及其对品质影响研究[D].南京:南京农业大学,2010.
[10] 刘晶晶,雷元华,李海鹏,等.加热温度及时间对牛肉胶原蛋白特性及嫩度的影响[J].中国农业科学,2018,51(5):485-489.
[11] AKTAS N,KAYA M.Influence of weak organic acids and salts on the denaturation characteristics of intramuscular connective tissue: A differential scanning calorimetry study[J].Meat Science,2001,58(4):413-419.
[12] ZUO H,HAN L,YU Q,et al.Proteomic and bioinformatic analysis of proteins on cooking loss in yak longissimus thoracis[J].European Food Research and Technology,2018,244(7):1 211-1 223.
[13] 罗天林.宰后牛胃肠冷藏过程中品质变化规律及其加工适宜性研究[D].兰州:甘肃农业大学,2017.
[14] 陈金伟.超高压改性加工酱卤猪蹄的工艺研究[D].合肥:合肥工业大学,2017.
[15] SCHEIBENZUBER M,W RUß,A GÖRG,et al.Scanning electron microscopic study of high pressure induced microstructural changes of proteins in turkey and pork meat[J].Progress in Biotechnology,2002(2):545-550.
[16] PALKA K.Changes in intramuscular connective tissue and collagen solubility of bovine M.semitendinosus during retorting[J].Meat Science,1999,53(3):189-194.
[17] HUANG F,HUANG M,XU X,et al.Influence of heat on protein degradation, ultrastructure and eating quality indicators of pork[J].Journal of the Science of Food & Agriculture,2011,91(3):443-448.
[18] LEWIE G J,PURSLOW P P.The strength and stiffness of perimysial connective tissue isolated from cooked beef muscle[J]. Meat Science,1989,26(4):255-269.
[19] PALKA K.Changes in intramuscular connective tissue and collagen solubility of bovine M.semitendinosus during retorting[J].Meat Science,1999,53(3):189-194.
[20] CHRISTENSEN L,GUNVIG A,TØRNGREN M A,et al.Sensory characteristics of meat cooked for prolonged times at low temperature[J].Meat Science,2012,90(2):485-489.
[21] TIAN X,WU W,YU Q,et al.Quality and proteome changes of beef M. longissimus dorsi cooked using water bath and ohmic heating process[J].Innovative Food Science & Emerging Technologies,2016,34:259-266.
[22] PALKA K,DAUN H.Changes in texture, cooking losses, and myofibrillar structure of bovine M. semitendinosus during heating[J].Meat Science,1999,51(3):237-243.
[23] YASIN H,BABJI A S,ISMAIL H.Optimization and rheological properties of chicken ball as affected by k-carrageenan, fish gelatin and chicken meat[J].LWT-Food Science and Technology,2016,66(1):79-85.
[24] 董晗,张牧焓,王道营,等.不同加热处理对兔肉超微结构的影响[J].西南农业学报,2012,25(6):2 289-2 293.
[25] 李超,徐为民,王道营,等.加热过程中肉嫩度变化的研究[J].食品科学,2009,30(11):262-265.
[26] NGAPO T M,BERGE P,CULIOLI J,et al.Perimysial collagen crosslinking and meat tenderness in Belgian Blue double-muscled cattle[J].Meat Science,2002,61(1):91-102.
[27] LOUISE M M,MICHAEL B F,SKIBSTED L H,et al.Long-time low-temperature cooking of beef: three dominant time-temperature behaviours of sensory properties[J].Flavour,2015,4(1):2.
[28] WATTANCHANT S,BENJAKKUL S,LEDWARD A.Effect of heat treatment on changes in texture, structure and properties of Thai indigenous chicken muscle[J].Food Chemistry,2005,93(2):337-348.
[29] KIM H W,CHOI Y S,CHOI J H,et al.Tenderization effect of soy sauce on beef M. biceps femoris.[J].Food Chemistry,2013,139(1-4):597-603.
