解冻方式对鸡腿肉蛋白氧化特性的影响  

Effects of thawing methods on protein oxidation characteristics of chicken thigh meat

作　　者：梁诗惠 冯钰敏 邓华荣 刘巧瑜[1] 白卫东[1] 吴俊师 陈海光[1] LIANG Shihui;FENG Yumin;DENG Huarong;LIU Qiaoyu;BAI Weidong;WU Junshi;CHEN Haiguang(College of Light Industry and Food Sciences,Zhongkai University of Agriculture and Engineering,Guangdong Key Laboratory of Science and Technology of Lingnan Special Food,Key Laboratory of Green Processing and Intelligent Manufacturing of Lingnan Specialty Food,Ministry of Agriculture,Innovation Research Institute of Modern Agricultural Engineering,Guangzhou 510225,China;Shenzhen Jinguyuan Industrial Development Co.Ltd.,Shenzhen 518000,China)

机构地区：[1]仲恺农业工程学院轻工食品学院,广东省岭南特色食品科学与技术重点实验室,农业农村部岭南特色食品绿色加工与智能制造重点实验室,现代农业工程创新研究院,广东广州510225 [2]深圳市金谷园实业发展有限公司,广东深圳518000

出　　处：《食品与发酵工业》2023年第5期223-229,共7页Food and Fermentation Industries

基　　金：广东省重点领域研发计划项目(2019B020212002);2021年广东省现代农业产业技术体系创新团队项目(2021KJ117)。

摘　　要：从蛋白质的氧化、聚集程度、蛋白质结构以及组织学特性方面,探究不同解冻方式(室温解冻、流水解冻、冷藏解冻和微波解冻)对冷冻鸡腿肉肌原纤维蛋白理化性质的影响。结果表明,室温解冻的羰基含量最高,为3.63 nmol/mg,巯基含量和Ca^(2+)-ATPase活性最低,分别为110.55μmol/g和0.72 U/mg,说明室温解冻组的蛋白氧化最为严重;肌球蛋白轻链条带模糊,有轻微降解现象;拉曼光谱结果中β-转角含量(26%)和无规则卷曲含量(31%)相对较高,蛋白质结构的稳定性较差。流水解冻的蛋白氧化程度较轻,具体表现为:其羰基含量和表面疏水性最低,分别为0.97 nmol/mg和10.36μg;Ca^(2+)-ATPase活性最高,为2.95 U/mg;组织结构紧密,α-螺旋含量最高(58%),蛋白质二级结构较为完整。冷藏解冻的巯基损失最小,巯基含量为258.23μmol/g,肌球蛋白轻链条带颜色较深,有聚集现象,组织结构的紧密性与流水解冻组无明显差异。微波解冻的组织结构破坏严重,肌纤维间隙较大,蛋白质二级结构较紊乱,α-螺旋含量最少,为29%。因此,流水解冻可以作为解冻鸡腿肉的主要解冻方式。From the aspects of protein oxidation characteristics, aggregation degree, protein structure, and histological characteristics, the effects of different thawing methods(room temperature thawing, flow thawing, cold storage thawing, and microwave thawing) on the physical and chemical properties of frozen chicken thigh myofibrillar protein were explored. Results showed that the carbonyl content of thawed at room temperature was the highest, 3.63 nmol/mg, and the sulfhydryl content and Ca^(2+)-ATPase activity were the lowest, 110.55 μmol/g and 0.72 U/mg, respectively, indicating that the protein oxidization in the room thawed group was the most severe. The light chain band was fuzzy and slightly degraded. The content of β-turn(26%) and the content of random curl(31%) in the Raman spectroscopy results were relatively high, and the stability of the protein structure was poor. The degree of protein oxidation of hydrolyzed fluid was lighter, which was characterized by its lowest carbonyl content and surface hydrophobicity, 0.97 nmol/mg and 10.36 μg, respectively, and the highest Ca^(2+)-ATPase activity at 2.95 U/mg. At the same time, the tissue structure was tight, the α-helix content was the highest(58%), and the protein secondary structure was relatively complete. The loss of sulfhydryl groups in cold storage and thawing was the smallest, the content of sulfhydryl groups was 258.23 μmol/g, the color of the myosin light chain was darker, there was an aggregation phenomenon, and the tightness of tissue structure was not significantly different from that in the fluid thawing group. The tissue structure of microwave thawing was severely damaged, the muscle fiber gap was large, the protein secondary structure was disordered, and the α-helix content was the least, which was 29%. Therefore, flow thawing could be used as the main thawing method for thawing chicken thigh meat.

关 键 词：解冻方式 鸡腿肉 肌原纤维蛋白 蛋白氧化 蛋白质结构 

分 类 号：TS251.55[轻工技术与工程—农产品加工及贮藏工程]