难溶性钙表面与蛋白胶体的相互作用
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- 英文论文题名：Interaction between insoluble calcium particle surface and protein hydrocolloid
- 论文作者：胡锦华 ; 文丽杰 ; 陆计萍 ; 周鹏
- 英文论文作者：Jinhua Hu ; Lijie Wen ; Jiping Lu ; Peng Zhou ; State Key Laboratory of Food Science and Technology ; School of Food Science and Technology ; Jiangnan University
- 年：2016
- 作者机构：江南大学食品学院食品科学与技术国家重点实验室;
- 论文关键词：碳酸钙 ; 羟基磷灰石 ; 磷酸钙 ; α-酪蛋白 ; β-酪蛋白
- 会议召开时间：2016-07-01
- 会议录名称：中国化学会第30届学术年会摘要集-第三十一分会：胶体与界面化学
- 语种：中文
- 分类号：TS201.2
- 学会代码：ZGHY
- 会议名称：中国化学会第30届学术年会-第三十一分会 ; 胶体与界面化学
- 会议地点：中国辽宁大连
- 主办单位：中国化学会
- 学会名称：中国化学会
- 页数：2
- 文件大小：246k
- 原文格式：D
- 会议级别：全国
摘要
本研究对三种难溶性钙(碳酸钙、羟基磷灰石和磷酸三钙)和浓缩乳蛋白(MPC)之间的相互作用进行了探索。首先通过ζ-电位和激光共聚焦显微镜的表征证实了难溶性钙与MPC之间存在相互作用,钙颗粒表面吸附后MPC之后,颗粒表面的ζ-电位绝对值明显增大。对吸附机理的深入探讨表明,难溶性钙与MPC之间通过反离子对发生相互作用,钙颗粒表面的Ca~(2+)位点与蛋白质的羧基和磷酸化丝氨酸基团发生相互作用,钙颗粒表面的负电荷位点(碳酸根或磷酸根位点)与蛋白质的氨基间发生相互作用,且前者更为强烈。吸附等温线的分析进一步揭示了难溶性钙与MPC之间的相互作用受到到蛋白组分、钙盐种类以及反应条件的影响。聚丙烯酰胺凝胶电泳的结果揭示了β-酪蛋白与钙颗粒表面的相互作用始终强于α-酪蛋白,但不受难溶性钙种类的影响。本研究结果有助于深入理解蛋白胶体与钙颗粒表面的相互作用。
This project studied the interaction between the particle surface of insoluble calcium salts(i.e.,calcium carbonate,hydroxyapatite and tricalcium phosphate) and protein hydrocolloid(milk protein concentration,MPC).The interaction between protein and calcium particle surface was first confirmed by ζ-potential characterization and laser scanning confocal microscope images.It found that MPC could interact with the surface of various calcium particles and led to an increase in surface charge of calcium particles.The mechanism discussion revealed that the interaction between MPC and calcium particle surface was driven by the electrostatic interactions between counter-ions,including Ca2+ sites on the calcium particle surface and the phosphorylated Ser and carboxyl groups of MPC,as well as the negatively charged sites on the calcium particle surface and the amino groups of MPC,and the former one was more strong.In addition,the interaction varing among MPC protein components,calcium salt types and preparing conditions was described using different types of adsorption isotherm.Moreover,the interaction of individual protein components with calcium particle surface was investigated by the polyacrylamide gel electrophoresis.The interaction preference order for MPC was β-casein > α-casein,and independent from the calcium types.These experimental facts may provide a better understanding of interaction between protein hydrocolloids and insoluble calcium particle surface.
This project studied the interaction between the particle surface of insoluble calcium salts(i.e.,calcium carbonate,hydroxyapatite and tricalcium phosphate) and protein hydrocolloid(milk protein concentration,MPC).The interaction between protein and calcium particle surface was first confirmed by ζ-potential characterization and laser scanning confocal microscope images.It found that MPC could interact with the surface of various calcium particles and led to an increase in surface charge of calcium particles.The mechanism discussion revealed that the interaction between MPC and calcium particle surface was driven by the electrostatic interactions between counter-ions,including Ca2+ sites on the calcium particle surface and the phosphorylated Ser and carboxyl groups of MPC,as well as the negatively charged sites on the calcium particle surface and the amino groups of MPC,and the former one was more strong.In addition,the interaction varing among MPC protein components,calcium salt types and preparing conditions was described using different types of adsorption isotherm.Moreover,the interaction of individual protein components with calcium particle surface was investigated by the polyacrylamide gel electrophoresis.The interaction preference order for MPC was β-casein > α-casein,and independent from the calcium types.These experimental facts may provide a better understanding of interaction between protein hydrocolloids and insoluble calcium particle surface.
引文
[1]Tercinier,L.;Ye,A.;Anema,S.;Singh,A.;Singh,H.J.Colloid Interface Sci.,2011,394:458.
[2]郭灵虹.体内及体外磷酸钙与蛋白质生物材料相互作用[D].四川大学,2001.
[2]郭灵虹.体内及体外磷酸钙与蛋白质生物材料相互作用[D].四川大学,2001.