兔肉胶原蛋白特性及评定方法研究被引量：9

Characteristics and evaluation method of collagen from rabbit meat

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摘要胶原蛋白是一种生物性高分子物质,是动物细胞外基质中最重要的组成部分。兔肉作为一种营养美味的食材,其食用和加工品质与肌内胶原蛋白的变化息息相关。通过总结不同兔品种、生长时期、生长部位及加工条件等因素对兔肉肌内胶原蛋白特性的影响,介绍兔肉肌内胶原蛋白的评定方法,以期为兔肉及其高附加值产品的研发提供理论依据和创新基础。 Collagen is a kind of biological polymer,and it is the most important part of the animal extracellular matrix. The rabbit meat as nutritious and delicious ingredients,its dietary and processing quality are closely related to the changes of intramuscular collagen. Reviewed the effect of different rabbit species ,growth period, growth location and processing conditions on rabbit intramuscular collagen characteristics ,and introduced the evaluation method of the rabbit intramuscular collagen,so as to provide a theoretical basis and innovation foundation for the research and development of rabbit meat,as well as its high value-added products.

作者薛山贺稚非李洪军

机构地区西南大学食品科学学院

出处《食品工业科技》 CAS CSCD 北大核心 2013年第4期372-377,共6页 Science and Technology of Food Industry

基金国家兔产业技术体系肉加工与综合利用(CARS-44-D-1)

关键词兔肉胶原蛋白特性评定 rabbit meahcollagen characteristics evaluation

分类号 TS251.1 [轻工技术与工程—农产品加工及贮藏工程]

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1陈丽清,韩佳冬,马良,张宇昊.兔肉品质及其影响因素研究进展[J].食品科学,2011,32(19):298-301. 被引量：20
2ZOTTE A D. Perception of rabbit meat and major tactors influencing the rabbit carcass and meat quality[J].Livestock Production Science,2002,(01):11-32.
3PASCUAL M,PLA M. Changes in collagen,texture and sensory properties of meat when selecting rabbits for growth rate[J].Meat Science,2008,(04):375-380.doi:10.1016/j.meatsci.2007.07.009.
4LI C,ZHOU G,XU X. Comparisons of meat quality characteristics and intramuscular connective tissue between beef longissimus dorsi and semitendinosus muscles from Chinese yellow bulls[J].Journal of Muscle Foods,2007,(02):143-161.
5CORREA J A,FAUCITANO L,LAFOREST J P. Effects of slaughter weight on carcass composition and meat quality in pigs of two different growth rates[J].Meat Science,2006,(01):91-99.
6SAKAKIBARA K,TABATA S,SHIBA N. Myofibre composition and total collagen content in M.iliotibialis lateralis and M.pectoralis of silkie and white leghorn chickens[J].British Poultry Science,2000,(05):570-574.doi:10.1080/713654983.
7YUNOKIA S,SUZUKIB T,TAKAIA M. Stabilization of low denaturation temperature collagen from fish by physical cross-linking methods[J].Journal of Bioscience and Bioengineering,2003,(06):575-577.doi:10.1016/S1389-1723(04)70152-8.
8ALBERTS B,JOHNSON A,LEWIS J. Molecular biology of the cell[M].New York:Garland Publishing,Inc,2000.1097-1097.
9LAREU R R,ZEUGOLIS D I,ABU-RUB M. Essential modification of the Sircol Collagen Assay for the accurate quantification of collagen content in complex protein solutions[J].Acta Biomaterialia,2010,(06):3146-3151.
10BAILEY A J,ETHERINGTON D J. Metabolism of collagen and elastin[J].Comprehensive Biochemistry,1980.299-460.