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当前位置: 首页 > 文章 > 超声波对鸡肉肌浆蛋白理化性质和结构的影响 食品科学 2013,34 (19) 32-36
Position: Home > Articles > Effects of Ultrasonic Treatment on the Physico-chemical Properties and Structure of Chicken Sarcoplasmic Proteins FOOD SCIENCE 2013,34 (19) 32-36

超声波对鸡肉肌浆蛋白理化性质和结构的影响

作  者：
涂宗财;马达;王辉;张露;沙小梅;常海霞;梁百惠;周华璐
单  位：
南昌大学
关键词：
超声波;肌浆蛋白;紫外;荧光;乳化性;起泡性
摘  要：
以鸡肉肌浆蛋白为原料,采用超声波对其进行处理,利用紫外、荧光谱仪、SDS-PAGE等分析肌浆蛋白理化性质和结构的变化。结果表明:超声功率和超声时间对肌浆蛋白的乳化性、起泡性、表面疏水性、内源荧光等均有较大的影响。随超声功率和超声时间的增加,肌浆蛋白的乳化性降低,乳化稳定性和起泡稳定性均呈先上升后下降,起泡性随超声功率的增加先下降后上升,而超声时间对其影响相反。超声波处理可使肌浆蛋白的表面疏水性和内源荧光强度增加,但其紫外光谱和分子质量无明显影响,说明超声波处理不会导致其肽键断裂。
译  名：
Effects of Ultrasonic Treatment on the Physico-chemical Properties and Structure of Chicken Sarcoplasmic Proteins
作  者：
TU Zong-cai;MA Da;WANG Hui;ZHANG Lu;SHA Xiao-mei;CHANG Hai-xia;LIANG Bai-hui;ZHOU Hua-lu;State Key Laboratory of Food Science and Technology,Engineering Research Center for Biomass Conversion,Ministry of Education,Nanchang University;College of Life Science,Jiangxi Normal University;
关键词：
ultrasonic;;sarcoplasmic proteins;;ultraviolet;;fluorescence;;emulsifying properties;;forming properties
摘  要：
Ultraviolet(UV) spectroscopy, fluorescence spectroscopy and SDS-PAGE were used to measure changes in the physio-chemical properties and structure of chicken sarcoplasmic proteins after ultrasonic treatment. Results indicated that ultrasonic power and treatment time exhibited great effects on the emulsifying properties, forming properties, surface hydrophobicity and intrinsic fluorescence properties of chicken sarcoplasmic proteins. As ultrasonic power and treatment time increased, the emulsifying capacity of chicken sarcoplasmic proteins decreased, and emulsion stability and foam stability increased initially and then decreased. However, an opposite effect of ultrasonic treatment time was observed the emulsifying properties and forming properties of chicken sarcoplasmic proteins. Moreover, the surface hydrophobicity and intrinsic fluorescence intensity became enhanced after ultrasonic treatment, but the UV spectra and molecular weight presented no obvious changes. These observations illustrate that ultrasonic exposure can not lead to fragmentation of peptide bonds in chicken sarcoplasmic proteins.

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