Manipulating interfacial behavior and emulsifying properties of myosin through alkali-heat treatment
Manipulating interfacial behavior and emulsifying properties of myosin through alkali-heat treatment
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通过碱热处理控制肌球蛋白的界面行为和乳化特性
DOI：
10.1016/j.foodhyd.2018.06.044
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发表时间：
2018-12-01
影响因子：
10.7
通讯作者：
Sun, Jian
中科院分区：
文献类型：
--
作者：
Li, Lingyun;Cai, Ruying;Sun, Jian
本研究调查了 pH（7.0、8.0 和 9.0）加热处理（75℃，30 分钟）对肌球蛋白（从鸡胸肉中提取）重新调整至 7.0 后的界面和乳化特性的影响。应用浊度和粒度分布来表征肌球蛋白的聚集；结果表明，碱热处理有效降低了热诱导的肌球蛋白聚集程度。聚集程度取决于加热过程中的pH值，顺序为S1>S2>S3。与单独热处理相比，碱热诱导的聚集体扩散到大豆油-水界面附近的速度更快，并且表现出更高的界面压力和更高的界面蛋白浓度。热诱导的肌球蛋白聚集体的聚集程度影响乳液稳定性。与S1和S2（高度聚集）相比，S3（低度聚集）稳定的乳液表现出更小的液滴尺寸和更好的储存稳定性。共焦激光扫描显微镜分析表明，桥联絮凝是聚集体S1和S2乳液乳化性能差的主要原因，而S3优异的乳液稳定性甚至可以与天然肌球蛋白相媲美。根据以上结果，S3可能通过空间排斥以微凝胶状形式稳定乳液。这些结果表明，碱热处理对于使用肉蛋白作为乳化剂的基于蛋白质聚集体的乳液的配制具有重要意义。
This study investigated the influence of pH (7.0, 8.0 and 9.0) plus thermal treatment (75 degrees C, 30 min) on the interfacial and emulsifying properties of myosin (extracted from chicken breast) after re-adjusted to pH 7.0. Turbidity and particle size distribution was applied to characterize the aggregation of myosin; results revealed that the alkali-heat treatment effectively decreased the extent of heat-induced aggregation of myosin. The degree of aggregation depends on the pH during heating, with the order being S1 > S2 > S3. Compared with heat treatment alone, alkali-heat induced aggregates diffused to the vicinity of the soy oil-water interface more rapidly and exhibited the higher interfacial pressure with the higher interfacial protein concentration. The degree of heat-induced aggregation of myosin aggregates influenced the emulsion stability. The emulsions stabilized by S3 (low degree aggregation) presented the smaller droplet size and better storage stability than S1 and S2 (high degree aggregation). Confocal laser scanning microscopy analysis demonstrated that bridging flocculation was the main reason for poor emulsifying properties in aggregates S1 and S2 emulsions, whereas the excellent emulsion stability of S3 can even match that of native myosin. According to the above results, S3 possibly stabilized the emulsion with steric repulsion in a microgel-like form. These results indicate that alkali-heat treatment have important implications for the formulation of protein aggregates based emulsions, using meat proteins as emulsifier.