Physicochemical characteristics and gel-forming properties of myofibrillar protein in an oxidative system affected by partial substitution of NaCl with KCl, MgCl2 or CaCl2
Physicochemical characteristics and gel-forming properties of myofibrillar protein in an oxidative system affected by partial substitution of NaCl with KCl, MgCl2 or CaCl2
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KCl、MgCl2 或 CaCl2 部分取代 NaCl 影响氧化系统中肌原纤维蛋白的理化特性和凝胶形成特性
DOI：
10.1016/j.foodchem.2019.125614
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发表时间：
2020-03-20
期刊：
影响因子：
8.8
通讯作者：
Sun, Weizheng
中科院分区：
文献类型：
--
作者：
Ge, Ge;Han, Yurui;Sun, Weizheng
研究了KCl、MgCl 2和CaCl 2部分取代NaCl对肌原纤维蛋白（MP）在羟自由基产生体系中氧化特性及其热致凝胶特性的影响。结果表明，MP的氧化与氯盐类型和取代度有关。MP在0.60 M NaCl有利于蛋白质展开和凝胶质量的氧化系统。增加二硫键的形成影响MP的构象，并导致在大的颗粒尺寸和凝胶的聚集网络在50%的KCl取代度。CaCl 2或MgCl 2替代物的存在有助于蛋白质聚合和不溶性。MP聚集抑制了加热过程中形成致密连续的凝胶网络，从而导致低等级凝胶。Ca ~（2+）对凝胶性能的影响比Mg ~（2+）严重，这取决于不同的阳离子效应。用KCl代替25%的NaCl得到了可接受的凝胶质量。
Effects of partial substitution of NaCl with KCl, MgCl2 or CaCl2 on oxidative characteristics of myofibrillar protein (MP) in a hydroxyl radical generating system and their heat-induced gel properties were investigated. Results indicated that MP oxidation is dependent upon the different chloride salt types and substitution degree. MP at 0.60 M NaCl was beneficial to protein unfolding and gel quality in the oxidative system. Increased formation of disulfide bonds affected the MP conformation and resulted in a large particle size and an aggregated network of gel at the 50% substitution degree of KCl. The presence of CaCl2 or MgCl2 substitutes contributed to protein polymerization and insolubility. MP aggregation restrained the formation of dense and continuous gel networks during heating, and thus resulted in a low-grade gel. Ca2+ had more serious impact on gel properties than Mg2+, dependent on different cation effects. Substitution of 25% NaCl by KCl gave acceptable gel quality in MP.