为探究兔肉在僵直前经不同的超高压处理,对其斩拌肉糜在加热后(20~80 ℃)所形成的凝胶品质的影响。实验以兔肉为主要原料,将僵直前的兔里脊肉在100~300 MPa下分别保压15 s或180 s,再成熟,加盐(质量分数2%)斩拌。对肉糜的储能模量(G′)和相位角等流变特性进行测定和分析,同时测定肉糜的拉曼光谱,计算蛋白的二级结构变化情况。结果表明,对僵直前的兔肉进行超高压处理,会影响其斩拌后蛋白体系中蛋白质的空间构型和理化性质,总体上会使α-螺旋含量降低,β-折叠含量增加,其中以200 MPa-15 s处理组最为显著。这些变化与加热后形成的凝胶功能特性有显著的相关性。
This study aimed to explore the effects of applying different high pressure (HP) treatments to the pre-rigor rabbit meat (PRRM) on the gelling property of its meat batters after heating (20-80 ℃). Rabbit meat was used as raw material, PRRM was subjected to 100-300 MPa HP for 15 s and 180 s, respectively, before aging. The aged meat was chopped with 2% salt. The storage modulus (G′), phase angle, and other rheological properties of meat batters were analyzed. Meanwhile, the Raman spectra were determined and the secondary structural changes of proteins were calculated. The results showed that applying HP treatments to PRRM affected conformations and physicochemical properties of proteins in the batter system, as the content of α-helix reduced and the content of β-sheet enhanced. Samples treated by 200 MPa HP for 15 s exhibited the most significant modifications. These changes had significant correlations with the gelling property of meat batters after heating.
[1] BAJOVIC B, BOLUMAR T, HEINZ V. Quality considerations with high pressure processing of fresh and value added meat products[J]. Meat Science, 2012, 92(3): 280-289.
[2] BUCKOW R, SIKES A, TUME R. Effect of high pressure on physicochemical properties of meat[J]. Critical Reviews in Food Science and Nutrition, 2013, 53(7): 770-786.
[3] HYGREEVA D, PANDEY C. Novel approaches in improving the quality and safety aspects of processed meat products through high pressure processing technology-A review[J]. Trends in Food Science & Technology, 2016, 54: 175-185.
[4] BALDA F, APARICIO B, SAMSON C. Industrial high pressure processing of foods: Review of evolution and emergingtrends[J]. Journal of Food Science and Engineering, 2012, 2(10): 543-549.
[5] MILLER K, ELLIS M, SUTTON D, et al. Effects of live animal sampling procedures and sample storage on the glycolytic potential of porcine longissimus muscle samples[J]. Journal of Muscle Foods, 2000, 11(1): 61-67.
[6] SAMPEDRO F, MCALOON A, YEE W, F et al. Cost analysis and environmental impact of pulsed electric fields and high pressure processing in comparison with thermal pasteurization. Food and Bioprocess Technology, 2014, 7(7): 1 928-1 937.
[7] CHIO Y, KIM B. Muscle fiber characteristics, myofibrillar protein isoforms, and meat quality[J]. Livestock Science, 2009, 122(2): 105-118.
[8] TROY D, KERRY J. Consumer perception and the role of science in the meat industry[J]. Meat Science, 2010, 86(1): 214-226.
[9] Food and agriculture organization of the united nations. Livestock Primary: Production Quantity [DB/OL]. [2017-12-15]. http://www.fao.org/faostat/en/#data/QL.
[10] DALLE A, SZENDRO Z. The role of rabbit meat as functional food[J]. Meat Science, 2011,88(3): 319-331.
[11] XUE Siwen, YANG Huijuan, LIU Rui, et al. Applications of high pressure to pre-rigor rabbit muscles affect the functional properties associated with heat-induced gelation[J]. Meat Science, 2017, 129: 176-184.
[12] XU Xinglian, HAN Minyi, FEI Ying, et al. Raman spectroscopic study of heat-induced gelation of pork myofibrillar proteins and its relationship with textural characteristic[J]. Meat Science, 2011, 87(3): 159-164.
[13] ALIX A, PEDANOU G, BERJOT M. Fast determination of the quantitative secondary structure of proteins by using some parameters of the Raman amide I band[J]. Journal of Molecular Structure, 1988, 174: 159-164.
[14] YANG Huijuan, KHAN M A, YU Xiaobo, et al. Changes in protein structures to improve the rheology and texture of reduced-fat sausages using high pressure processing[J]. Meat Science, 2016,121: 79-87.
[15] LI E, NAKAI S, HIROTSUKA M. Raman Spectroscopy as a Probe of Protein Structure in Food Systems[M]. Boston, MA: Springer US publishing, 1994: 163-197.
[16] HOWELL N K, ARTEAGA G, NAKAI S, et al. Raman spectral analysis in the CH stretching region of proteins and amino acids for investigation of hydrophobic interactions[J]. Journal of Agricultural and Food Chemistry, 1999, 47(3): 924-933.
[17] LIU Ru, ZHAO Siming, XIONG Shanbai, et al. Role of secondary structures in the gelation of porcine myosin at different pH values[J]. Meat Science, 2008, 80(3): 632-639.
[18] HERRERO A M, CARMONA P, LOPEZ I, et al. Raman spectroscopic evaluation of meat batter structural changes induced by thermal treatment and salt addition[J]. Journal of Agricultural and Food Chemistry, 2008, 56(16): 7 119-7 124.
[19] WU Mangang, XIONG Youlin, CHEN Jie. Rheology and microstructure of myofibrillar protein-plant lipid composite gels: Effect of emulsion droplet size and membrane type[J]. Journal of Food Engineering, 2011, 106(4): 318-324.
[20] UPADHYAY R, GHOSAL D, MEHRA A. Characterization of bread dough: Rheological properties and microstructure[J]. Journal of Food Engineering, 2012, 109(1): 104-113.
[21] IKEDA S. Heat-induced gelation of whey proteins observed by rheology, atomic force microscopy, and Raman scattering spectroscopy[J]. Food Hydrocolloids, 2003, 17(4): 399-406.
[22] XUE Siwen, YANG Huijuan, YU Xiaobo, et al. Applications of high pressure to pre-rigor rabbit muscles affect the water characteristics of myosin gels[J]. Food Chemistry, 2018, 240: 59-66.
