Study on Surface Properties and Mechanism of Milk Protein Coated Nanotricalcium Phosphate Hydrate
CSTR:
Author:
Affiliation:

Clc Number:

Fund Project:

  • Article
  • |
  • Figures
  • |
  • Metrics
  • |
  • Reference
  • |
  • Related
  • |
  • Cited by
  • |
  • Materials
  • |
  • Comments
    Abstract:

    The adsorption of caseins from sodium caseinate(SC) and whey proteins from whey protein isolate(WPI) onto particles of nanotricalcium phosphate hydrate(TCP) was studied. Zeta-potential measurements involved that both SC and WPI bound to TCP,resulting in an increase in the absolute value of the zeta-potential of the particles. This adsorption improved the suspension stability of the TCP particles in water. WPI has stronger ability of improvement in suspension,and SC is easier that absorbed on TCP particles. For WPI,there was a preference in the protein adsorption:β-lactoglobulin>α-lactalbumin. Possible mechanisms showed the interaction between milk proteins and TCP are discussed. It is related to the structure and the surface properties of SC,WPI and TCP particles.

    Reference
    Related
    Cited by
Get Citation

LI Yanbo, CHEN Chen, LIU Xiaoming, HU Jinhua, ZHOU Peng. Study on Surface Properties and Mechanism of Milk Protein Coated Nanotricalcium Phosphate Hydrate[J]. Journal of Food Science and Biotechnology,2016,35(7):714-720.

Copy
Share
Article Metrics
  • Abstract:
  • PDF:
  • HTML:
  • Cited by:
History
  • Received:
  • Revised:
  • Adopted:
  • Online: November 01,2016
  • Published:
Article QR Code

Copy Right:Editorial Board of Journal of Food Science and Biotechnology

Address:No. 1800, Lihu Avenue, Wuxi 214122, Jiangsu Province,China  PostCode:214122

Phone:0510-85913526  E-mail:xbbjb@jiangnan.edu.cn

Supported by:Beijing E-Tiller Technology Development Co., Ltd.

WeChat

Mobile website