超声波对酪蛋白结构与功能性质的影响  

Effects of ultrasound treatment on structure and functional properties of casein

作　　者：石燕[1] 葛辉[1] 涂宗财[1,2] 王辉[1] 

机构地区：[1]南昌大学食品科学与技术国家重点实验室,南昌大学食品科学与工程系,江西南昌330047 [2]江西师范大学功能有机小分子教育部重点实验室,江西南昌330022

出　　处：《食品与发酵工业》2014年第2期16-21,共6页Food and Fermentation Industries

基　　金：国家重点基础研究发展规划项目计划(973计划)(2012CB126314);江西省重大创新基础研究项目(20124ACB00600)

摘　　要：为了探讨超声波对酪蛋白结构与功能性质的影响,研究了酪蛋白溶液经过超声波处理后溶解度、起泡性、乳化性、粒度、二级结构、分子柔顺性和分子质量的变化规律。结果表明:随着超声波功率的增大及处理时间的延长,酪蛋白的溶解度逐渐增大。480 W下起泡性、960 W下乳化性最高,分别比未处理的提高了17.03%和31.78%;固定功率240 W,处理时间为25 min的起泡性、15 min的乳化性最高,分别比未处理的提高了22.65%和18.88%。适当条件的超声波处理能使酪蛋白溶液粒度减小且分散均匀,同时还能显著提高酪蛋白分子柔顺性、降低酪蛋白的α-螺旋含量,240 W超声处理15 min后,α-螺旋含量降低了4.80%。但超声波处理不会使酪蛋白分子质量发生明显变化,不会导致其肽键断裂。To study the effect of ultrasound treatment on structure and functional properties of casein, this article studied the changes of particle size, solubility, foaming capacity, emulsifying activity, secondary structures, flexibil- ity and molecular weight of casein after ultrasound treatment. The results indicated that the solubility of casein was gradually increased with the increase of ultrasonic power and time. When ultrasonic power was 480W, the foaming ca- pacity of casein solution was the highest 17.03% higher than that of untreated; and emulsifying activity at 960W was 31.78% higher than that of untreated. Setting the ultrasonic power up to 240W, the highest foaming capacity was ob- tained at 25 min, and highest emulsifying activity was obtained at 15 min, both increased by 22.65% and 18.88% than untreated ones. The particle size of casein decreased and the particle distributed more homogeneous after an ap- propriate ultrasound treatment. At the same time, the treatment of ultrasound may also increase the flexibility of case- in. The content of a-helix was decreased significantly after ultrasound treatment, when the casein solution was at ul- trasound 240W for 15 min, the content of a-helix decreased by 4. 80%. However, ultrasound treatment had no effect on the molecular weight of casein, which indicated that ultrasound did not break the peptide bonds.

关 键 词：超声波处理 酪蛋白 功能性质 二级结构 分子柔顺性 

分 类 号：TS201.21[轻工技术与工程—食品科学]