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阳离子和pH值对肌原纤维蛋白冷冻稳定性的影响

苟浩 徐万军 张钰 胡逸凡 包玉龙

肉类研究2026,Vol.40Issue(9):27-35,9.
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肉类研究2026,Vol.40Issue(9):27-35,9.DOI:10.7506/rlyj1001-8123-20250814-265

阳离子和pH值对肌原纤维蛋白冷冻稳定性的影响

Effects of Cations and pH on the Frozen Storage Stability of Myofibrillar Proteins

苟浩 1徐万军 1张钰 1胡逸凡 1包玉龙1

作者信息

  • 1. 江苏大学食品与生物工程学院,江苏 镇江 212013
  • 折叠

摘要

Abstract

This study aimed to investigate the effects of different cations(Na+,K+and Li+)at a concentration of 0.6 mol/L and pH levels(7.0,6.0 and 5.0)on the frozen storage stability of myofibrillar protein(MP)solution.The results demonstrated that both cation species and pH significantly influenced the degree of MP denaturation during freezing.At the same pH level,K+addition resulted in the most pronounced aggregation of MP after freezing,while Na+and Li+had similar effects on MP aggregation.At pH 7.0 in the presence of K+,the solubility of MP was the lowest after freezing,with a marked decrease from 83.08%to 43.38%.Concurrently,the presence of K+resulted in significantly higher surface hydrophobicity and larger particle size in MP compared to the other cations(P<0.05).Among the three ions,K+had the most substantial impact on MP structure after freezing,manifested by a conformational shift from α-helix to β-turn and random coil,along with reduced maximum fluorescence intensity of intrinsic fluorescence spectroscopy.Furthermore,K+treatment led to the highest degree of MP oxidation after freezing.Decreasing pH enhanced the detrimental effects of freezing on MP,with the effect being particularly pronounced in the presence of K+.In conclusion,different cations and pH levels significantly affected the physicochemical properties of MP following freezing;notably,K+promoted MP denaturation and oxidation.

关键词

肌原纤维蛋白/阳离子/冷冻稳定性/pH值

Key words

myofibrillar protein/cations/frozen storage stability/pH

分类

轻工纺织

引用本文复制引用

苟浩,徐万军,张钰,胡逸凡,包玉龙..阳离子和pH值对肌原纤维蛋白冷冻稳定性的影响[J].肉类研究,2026,40(9):27-35,9.

基金项目

江苏省研究生科研与实践创新计划项目(KYCX254279) (KYCX254279)

肉类研究

1001-8123

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