食品科学 ›› 2018, Vol. 39 ›› Issue (3): 97-103.doi: 10.7506/spkx1002-6630-201803015

• 基础研究 • 上一篇    下一篇

赖氨酸诱导低离子强度下罗非鱼肌球蛋白增溶及机制

朱潘红,周春霞*,付苇娅,齐慧红,李 婷,洪鹏志   

  1. 广东海洋大学食品科技学院,广东省水产品加工与安全重点实验室,水产品深加工广东普通高等学校重点实验室,广东 湛江 524088
  • 出版日期:2018-02-15 发布日期:2018-01-30
  • 基金资助:
    广东省高等学校学科与建设专项科技创新项目(2013KJCX0098); 广东省高等学校优秀青年教师培养计划资助项目(Yq2013090)

L-Lysine-Induced Solubilization and Mechanism of Tilapia Myosin under Low Ionic Strength Conditions

ZHU Panhong, ZHOU Chunxia*, FU Weiya, QI Huihong, LI Ting, HONG Pengzhi   

  1. Key Laboratory of Advanced Processing of Aquatic Products of Guangdong Higher Education Institution, Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China
  • Online:2018-02-15 Published:2018-01-30

摘要: 以罗非鱼肉为原料提取肌球蛋白,研究5 mmol/L赖氨酸对低离子强度(1~150 mmol/L KCl)条件下肌球 蛋白(蛋白质量浓度为2.0 mg/mL)体系浊度、溶解度及分子结构和形态的影响,分析赖氨酸诱导肌球蛋白增溶 机理。结果表明,在低离子强度下,肌球蛋白分子聚集成纤丝,溶解度低,赖氨酸的添加能显著降低肌球蛋白体 系的浊度(P<0.05),抑制蛋白分子间的聚集,增溶效果明显,增溶后分子的表面疏水性增大,α-螺旋含量减小 (P<0.05),且与酸碱处理组比较,在1~40 mmol/L KCl范围内,赖氨酸增溶效果更好。增溶后的肌球蛋白Zeta- 电位的绝对值增大,丝状体解离。

关键词: 肌球蛋白, 赖氨酸, 低离子强度, 溶解性, 增溶机理

Abstract: Myosin was extracted from tilapia muscle, and the effect of 5 mmol/L L-lysine on the turbidity, solubility, molecular structure and shape of myosin (2.0 mg/mL) was studied in low ionic strength (0–150 mmol/L KCl) solutions. The L-lysine-induced solubilization behavior and mechanism of myosin were analyzed. Results showed that myosin molecules were assembled into filaments with low solubility under low ionic strength conditions. L-Lysine could significantly decrease the turbidity of myosin dispersion (P < 0.05), and inhibit the aggregation of protein molecules, thereby having an obvious solubilizing effect on L-lysine. Surface hydrophobicity of soluble myosin was increased, and α-helix content was decreased (P < 0.05). Compared with the pH shifting group, the solubilization of myosin by L-lysine was more remarkable in 1–40 mmol/L KCl solution. The absolute zeta potential of myosin treated with L-lysine was increased, leading to the dissociation of myosin filaments.

Key words: myosin, L-lysine, low ionic strength, solubility, solubilization mechanism

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