超声波处理对酪蛋白结构特性的影响  

Effect of ultrasonic on the structural properties of casein

作　　者：冯景丽[1] 贾峰[1] 王金水[1] 高芸芳[1] 周晓配 李小伟[2] 

机构地区：[1]河南工业大学生物工程学院,郑州450001 [2]河南工业大学粮油食品学院,郑州450001

出　　处：《中国乳品工业》2015年第6期20-23,共4页China Dairy Industry

基　　金：河南工业大学博士基金项目(No.2012BS013);河南省教育厅科学技术研究重点项目(No.13A550166);郑州市普通科技攻关计划项目(N2013G0077);河南工业大学校基础研究重点培育基金(2013JCYJ05)

摘　　要：利用不同功率超声波处理酪蛋白之后,采用电子扫描电镜检测酪蛋白的表面特征,激光粒度分布仪检测酪蛋白的粒度分布,傅里叶红外光谱检测酪蛋白的二级结构变化。结果表明:超声波处理能够使酪蛋白的表面致密的结构发生层片化和孔洞化变化,较大的酪蛋白颗粒的粒度变小,与分子量分布的检测结果相一致,酪蛋白的二级结构α-螺旋、β-折叠和无规则卷曲减少,即减少分子中的弹性结构,而β-转角的含量增加,使得酪蛋白原先致密的结构变得相对松散,增加了比表面积。研究结果为利用酪蛋白制备生物活性肽,呈味肽等新产品提供理论基础,拓宽其在食品和非食品领域的应用。In this study, the casein was treated by ultrasonic wave and the surface characteristics was tested by scanning electron microsco- py（SEM）, the particle size distribution was tested by laser particle size analyzer, the secondary structure changes was tested by Fourier infrared spectrometer. The results showed that ultrasonic treatment on casein can make it＇ s density structure become lamellar and voided, the larger casein particles become smaller, which was consistent with the results of molecular weight distribution. The α-helix, β-sheet and coil of the secondary structure of casein were decreased, which means reduction of the elastic structure in the molecule. While the increasing of the con- tent of β-turn made the casein compact structure originally becomes relatively loose, it increased the specific surface area. The results provide theoretical basis for the use of casein to produce bioactive peptides, peptides and other new products, and broaden its application in food and non-food fields.

关 键 词：酪蛋白 超声波 粒度分布 二级结构 傅里叶红外光谱(FTIR) 

分 类 号：Q93-33[生物学—微生物学]