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钙离子对酪蛋白胶束结构影响的光谱学研究
引用本文:王鹏杰,吴建平,张昊,郭慧媛,刘洪娜,任发政.钙离子对酪蛋白胶束结构影响的光谱学研究[J].光谱学与光谱分析,2014,34(1):92-97.
作者姓名:王鹏杰  吴建平  张昊  郭慧媛  刘洪娜  任发政
作者单位:1. 中国农业大学食品科学与营养工程学院,食品质量与安全北京实验室,北京 100083
2. 阿尔伯塔大学,加拿大埃德蒙顿市
3. 甘肃农业大学食品科学与工程学院,甘肃 兰州 630070
基金项目:International Science & Technology Cooperation Program of China(2011DFA32550), Ministry of Science and Technology of China (2012BAD12B08)
摘    要:综合运用动态光散射光谱、荧光光谱和高效液相-紫外光谱法检测钙离子对酪蛋白胶束结构的影响。外源添加的钙离子的浓度从0增加至12 mmol·L-1的过程中,酪蛋白胶束的外源ANS荧光强度和浊度一直增大,但是其体积平均直径和胶束的多分散指数是一直下降。同时,当外源添加的钙螯合剂(柠檬酸根)离子的浓度从0 增加至12 mmol·L-1的过程中,酪蛋白胶束的外源ANS荧光强度和浊度一直减小,但是酪蛋白胶束的体积平均直径、胶束的多分散指数和胶束的稳定性是增大的。因此,在对酪蛋白胶束的结构影响方面,钙离子和柠檬酸根离起到了相反的作用。研究证实,外源钙离子可以有效地调节酪蛋白胶束的结构,进而改善其功能特性。

关 键 词:光谱  钙离子  酪蛋白胶束  结构    
收稿时间:2013/4/10

Spectroscopic Investigation of the Influence of Calcium Ion on the Structures of Casein Micelles
WANG Peng-jie;WU Jian-ping;ZHANG Hao;GUO Hui-yuan;LIU Hong-na;REN Fa-zheng.Spectroscopic Investigation of the Influence of Calcium Ion on the Structures of Casein Micelles[J].Spectroscopy and Spectral Analysis,2014,34(1):92-97.
Authors:WANG Peng-jie;WU Jian-ping;ZHANG Hao;GUO Hui-yuan;LIU Hong-na;REN Fa-zheng
Institution:1. Beijing Laboratory for Food Quality and Safety, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China2. University of Alberta, Edmonton, Canada3. College of Food Science and Technology, Gansu Agricultural University, Lanzhou 630070, China
Abstract:The effects of calcium ion on the structural properties of casein micelles in the course of heat treatment were synthetically examined by non-structure-invasive spectrometry. The hydrophobicity, reflected by extrinsic fluorescence (ANS fluorescence), was positively correlated with the concentration of the calcium ion, within the range of 0 to 12 mmol·L-1. Meanwhile, the turbidity and stability of casein micelles also increased with the growth of calcium concentrations. However, opposite results were observed for hydrodynamic diameter and polydispersity index. Compared with the calcium ion, the calcium-chelator (citrate) has an opposite effect on the structural characteristics of casein micelles. Within the calcium concentrations range of 0 to 12 mmol·L-1, the hydrophobicity, stability and turbidity were negatively correlated with the concentration of the calcium ion, nevertheless, opposite results were observed for hydrodynamic diameter and polydispersity index. All the results indicate that the calcium ion could be used to modify the structures of casein micelles during heat heatment.
Keywords:Casein micelles  Calcium ions  Structures  Spectroscopy
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