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CaCl_2和木瓜蛋白酶处理对羊肉品质的影响 被引量:2

Respective Effects of Calcium Chloride and Papain on Lamb Quality
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摘要 研究不同浓度的CaCl2注射或不同质量浓度的木瓜蛋白酶浸泡处理对云岭黑山羊股二头肌pH值、肉色、蒸煮损失、肌原纤维小片化指数、胶原蛋白、肌浆蛋白和肌原纤维蛋白降解的影响。结果表明:CaCl2注射或木瓜蛋白酶浸泡处理显著提高了肌原纤维小片化指数;0h和6h时对照组出现极限pH值,分别为6.75和6.15,而CaCl2处理组或木瓜蛋白酶处理组到达极限pH值时间为2h和24h,极限pH值分别为6.83、6.29和6.90、5.89,SDS-PAGE分析显示CaCl2和木瓜蛋白酶促使羊肉肌肉中的肌动蛋白、肌球蛋白和连接蛋白发生降解。在0.3mol/LCaCl2或0.002g/100mL木瓜蛋白酶处理时,处理组的肌原纤维小片化指数和胶原蛋白的含量达到最大,蒸煮损失最小,表现出最佳的嫩化效果。 The respective effects of CaCl2 injection at varying concentrations and papain soaking on pH,color,cooking loss,myofibril fragmentation index(MFI),sarcoplasmic protein and myofibrillar protein degradation of Biceps femoris from Yunling black goats were investigated.A significant difference(P0.05) in MFI was observed between the control group and the treatment groups.Ultimate pH was presented in the control group after 0 and 6 h of 4 ℃ storage,which was valued at 6.75 and 6.15,respectively.The lengths of storage time for reaching up to ultimate pH,valued at 6.83 and 6.29 for CaCl2 treatment group and 6.90 and 5.89 for papain treatment group were 2 h and 24 h,respectively.CaCl2 injection or papain soaking could promote the degradation of actin,myosin and myomesin.The samples treated with 0.3 mol/L CaCl2 or 0.002g/100mL papain exhibited the maximum MFI,the highest collagen protein content and minimum cooking loss,indicating perfect tenderization.
出处 《食品科学》 EI CAS CSCD 北大核心 2010年第11期123-127,共5页 Food Science
基金 云南省科技攻关项目(2004NG04)
关键词 羊肉 肌原纤维蛋白 肌浆蛋白 CACL2 木瓜蛋白酶 mutton myofibril sarcoplasmic protein calcium chloride papain
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参考文献14

  • 1SHACKELFORD S D, WHEELER T L, MEADE M K, et al. Consumer impressions of tender select beef[J]. Journal of Animal Science, 2001, 79:2605 -2615. 被引量:1
  • 2LAWRENCE T E, DIKEMAN M E, STEPHENS J W, et al. In situ investigation of the calcium-induced proteolytic and salting in mechanisms causing tenderization in calcium-enhanced muscles[J]. Meat Science, 2003, 66: 69-75. 被引量:1
  • 3吕东坡,胡永金,朱仁俊,葛长荣.宰后肉的嫩化机制及其影响因素[J].食品科学,2008,29(8):704-709. 被引量:21
  • 4FADDA S, SANZ Y, VIGNOLO G, et al. Characterzation of muscle sarcoplasmic and myofibrinar protein hydrolysis caused by Lactobacillus plantarum[J]. Applied and Environmental Microbiology, 1999, 65: 3540-3546. 被引量:1
  • 5DIAZ O, FERNANDEZ M, GARCIA D E, et al. Effect of the addition of papa.in on the dry fermented sausage proteolysis[J]. Journal of the Science of Food and Agriculture, 1996, 71(1): 13-21. 被引量:1
  • 6ASHIE I N A, SORENSEN T L, NIELSEN P M. Effects of papain and a microbial enzyme on meat proteins and beef tenderness[J]. Journal of Food Science, 2002, 67(6): 2138-2142. 被引量:1
  • 7KANG C K, RICE E E. Degeradation of various meat fractions by tendering enaymes[J]. Journal of Food Science, 1970, 35: 563-569. 被引量:1
  • 8汪家政,范明,主编.蛋白质技术手册[M].北京:科学出版社,2001.42-47. 被引量:101
  • 9KONG Fanbin, TANG Juming, LIN Mengshi, et al. Thermal effects on chicken and salmon muscles: Tenderness, cook loss, area shrinkage, collagen solubility and microstructure[J]. LWT - Food Science and Technology, 2008, 41(7): 1210-1222. 被引量:1
  • 10李建武等编..生物化学实验原理和方法[M].北京:北京大学出版社,1994:463.

二级参考文献79

  • 1汪家政,范明,主编.蛋白质技术手册[M].北京:科学出版社,2001.42-47. 被引量:101
  • 2郭尧君.蛋白质电泳实验技术[M].北京:科学出版社,2001:203-208. 被引量:62
  • 3REESA M P, TROUTC G R, WARNERA R D. Effect of calcium infusion on tenderness and ageing rate of pork m. longissimus thoracis et lumborum after accelerated boning [J]. Meat Science, 2002, 61: 169-179. 被引量:1
  • 4GERELT B, IKEUCHI Y, NICHIUMI T, et al. Meat tenderization by calcium chloride after osmotic dehydration[J]. Meat Science, 2002, 60: 237-244. 被引量:1
  • 5NAUSS K M, KITAGAWA S, GERGELY J. Pyrophosphate binding to and adenosine triphosphatase activity of myosin and its proteolytic fragments[J]. J Biol Chem, 1969, 244(3): 755-765. 被引量:1
  • 6HERMANSSON A M, HARBITZ O, LANGTON M. Formation of two types of gels from bovine myosin[J]. J Sci Food Agric, 1986, 37: 69-84. 被引量:1
  • 7WANG S F, SMITH D M. Dynamic rheological properties and secondary structure of chicken breast myoisn as influenced by isothermal heating [J]. J Agric Food Chem, 1994, 42: 1434-1439. 被引量:1
  • 8SPUDICH J A WATT S. The regulation of rabbit skeletal muscle contraction[J]. J Bio Chem, 1971, 246: 4866-4871. 被引量:1
  • 9PERRY S V. The bound nucleotide of the osolated myofibril[J]. Biochemistry, 1952, 51: 495-499. 被引量:1
  • 10LAEMMLI U K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4 [J]. Nature (Lond.), 1970, 227(259): 680-685. 被引量:1

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