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中国精品科技期刊2020
孟嘉珺,许树荣,邓莎,等. 食盐腌制对鸡肉品质、肌原纤维蛋白结构和功能特性的影响[J]. 食品工业科技,2022,43(24):45−53. doi: 10.13386/j.issn1002-0306.2022020270.
引用本文: 孟嘉珺,许树荣,邓莎,等. 食盐腌制对鸡肉品质、肌原纤维蛋白结构和功能特性的影响[J]. 食品工业科技,2022,43(24):45−53. doi: 10.13386/j.issn1002-0306.2022020270.
MENG Jiajun, XU Shurong, DENG Sha, et al. Effects of Salt Marinating on Chicken Quality and Structure Characteristics, Function Characteristics of Chicken Myofibrin Protein[J]. Science and Technology of Food Industry, 2022, 43(24): 45−53. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2022020270.
Citation: MENG Jiajun, XU Shurong, DENG Sha, et al. Effects of Salt Marinating on Chicken Quality and Structure Characteristics, Function Characteristics of Chicken Myofibrin Protein[J]. Science and Technology of Food Industry, 2022, 43(24): 45−53. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2022020270.

食盐腌制对鸡肉品质、肌原纤维蛋白结构和功能特性的影响

Effects of Salt Marinating on Chicken Quality and Structure Characteristics, Function Characteristics of Chicken Myofibrin Protein

  • 摘要: 为探究食盐浓度对冷藏腌制过程中鸡肉品质和肌原纤维蛋白的影响,将鸡肉置于不同浓度(0%、1.6%、3.2%、4.8%、6.4%、8.0%)的食盐腌制液中,进行不同时间(0.2、1、2、3、4 d)的冷藏腌制后,测定鸡肉的水分含量、持水性以及肌原纤维蛋白的溶解度、表面疏水性、羰基、巯基、二聚酪氨酸含量等。结果表明:经过不同浓度食盐液的腌制,鸡肉的持水性和肌原纤维蛋白表面疏水性发生变化,随着腌制时间的延长羰基含量和二聚酪氨酸含量增大,肌原纤维蛋白的溶解度、热稳定性、巯基含量降低,部分α-螺旋转化为β-折叠。随着食盐液浓度增大羰基和二聚酪氨酸含量先增加后减小,巯基含量不断增大,并且食盐液浓度范围为3.2%~4.8%时肌原纤维蛋白各特性指标变化较大。综上,食盐腌制能促使鸡肉肌原纤维蛋白结构和功能发生改变,此研究结果可为控制腌制过程中鸡肉品质变化和其肌原纤维蛋白氧化提供理论依据。

     

    Abstract: This study was conducted to investigate the effect of salt on the quality and myofibrillar protein during cold storage of chicken breast. After the low-temperature curing with different salt concentration (0.0%, 1.6%, 3.2%, 4.8%, 6.4% and 8.0%) for different times (0.2, 1, 2, 3, 4 d), the chicken samples were used to meaure the water content, water holding capacity, olubility, surface hydrophobicity, carbonyl content, sulfhydryl content, and dimer tyrosine content. Results showed that water holding capacity and surface hydrophobicity were changed after brining, the brining time positively affected carbonyl content and dimer tyrosine content while negatively affected sulfhydryl group content, thermal stability, and solubility. In addition, salt treatments could change the structure of samples from α-helix to β-fold. With the increasing of salt concentration, the contents of carbonyl and dimer tyrosine increased firstly and then decreased, and the content of sulfhydryl increased continuously. When the salt concentrations ranged from 3.2% to 4.8%, the characteristic indexes of myofibrillar protein changed obviously. In conclusion, the structure and function of myofibrillar protein in chicken were affected by salination. These results would provide theoretical data for controlling the changes of chicken quality and oxidation of myofibrillar protein during the brining process.

     

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