食品科学 ›› 2018, Vol. 39 ›› Issue (3): 28-33.doi: 10.7506/spkx1002-6630-201803005

• 基础研究 • 上一篇    下一篇

迷迭香提取物与NaCl协同改善肌原纤维蛋白凝胶特性

贾 娜,谢振峰,李儒仁*,邵俊花,刘登勇,刘裕慧   

  1. 渤海大学食品科学与工程学院,辽宁省食品安全重点实验室,生鲜农产品贮藏加工及安全控制技术国家地方联合工程研究中心,辽宁 锦州 121013
  • 出版日期:2018-02-15 发布日期:2018-01-30
  • 基金资助:
    国家自然科学基金青年科学基金项目(31301509;31601489)

Synergistic Improvement of Myofibrillar Protein Gel Properties by Combination of Rosemary Extract and NaCl

JIA Na, XIE Zhenfeng, LI Ruren*, SHAO Junhua, LIU Dengyong, LIU Yuhui   

  1. National & Local Joint Engineering Research Center of Storage, Processing and Safety Control Technology for Fresh Agricultural and Aquatic Products, Food Safety Key Laboratory of Liaoning Province, College of Food Science and Engineering, Bohai University, Jinzhou 121013, China
  • Online:2018-02-15 Published:2018-01-30

摘要: 本研究以猪背最长肌肌原纤维蛋白为对象,通过测定内源荧光强度、巯基含量、流变特性、凝胶强度、 保水性,探讨不同NaCl浓度条件下,迷迭香提取物(0.01 g/g pro)对肌原纤维蛋白结构和凝胶特性的影响。结果表 明:NaCl浓度低于0.45 mol/L时,肌原纤维蛋白中添加迷迭香提取物不利于形成良好的凝胶结构,肌原纤维蛋白的 保水性较差;然而,NaCl浓度在0.45 mol/L时,迷迭香提取物协同NaCl可以显著提高肌原纤维蛋白的储能模量、凝 胶强度和保水性。在此NaCl浓度下,迷迭香提取物与NaCl协同作用,使肌原纤维蛋白内源荧光强度明显下降,波 长红移2 nm,肌原纤维蛋白三级结构的有利改变是造成减盐条件下,肌原纤维蛋白保水性没有显著下降的重要原 因。上述结果可为NaCl替代物的开发提供新的参考思路。

关键词: NaCl, 迷迭香提取物, 肌原纤维蛋白, 蛋白结构, 凝胶特性

Abstract: The synergistic effect of combinations of rosemary extract (0.01 g/g pro) and NaCl at different concentrations on the structure and gel properties of myofibrillar proteins from pork Longissimus dorsi muscle was investigated by determining intrinsic fluorescence intensity, sulfhydryl group content, gel strength, water-holding capacity and rheological properties. The results indicated that addition of rosemary extract did not benefit the formation of stable gel network structure and decreased the water-holding capacity of myofibrillar proteins at NaCl concentration below 0.45 mol/L. However, the combination of rosemary extract and NaCl at 0.45 mol/L could significantly improve the gel strength, storage modulus and water-holding capacity and result in a remarkable decrease in the intrinsic fluorescence intensity of myofibrillar proteins as manifested by a 2 nm red shift. The tertiary structure of myofibrillar proteins changed favorably at lower NaCl concentrations so that the water-holding capacity did not decrease markedly. These results may be expected to provide new insights for the development of salt substitutes.

Key words: NaCl, rosemary extract, myofibrillar protein, protein structure, gel properties

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