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Chemical Research in Chinese Universities ›› 2012, Vol. 28 ›› Issue (6): 1070-1073.

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Thermodynamic Properties of Linear Protein Solutions: an Application to Type I Antifreeze Protein Solutions

LI Li-fen1,2, LIANG Xi-xia1, LI Qian-zhong1   

  1. 1. Department of Physics, Inner Mongolia University, Hohhot 010021, P. R. China;
    2. Department of Basic Curriculum, North China Institute of Science and Technology, Beijing 101601, P. R. China
  • Received:2012-01-10 Revised:2012-02-16 Online:2012-11-25 Published:2012-11-09
  • Contact: LIANG Xi-xia E-mail:xxliang@imu.edu.cn
  • Supported by:

    Supported by the National Natural Science Foundation of China(Nos.10764003, 30560039) and the Special Fund for Basic Scientific Research of Central Colleges, North China Institute of Science and Technology for Nationalities(No.JCB1201A).

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Abstract:

A statistical thermodynamic theory of linear protein solutions was proposed with the aid of a lattice model and applied to type I antifreeze protein(AFPI) solutions. The numerical results for several AFPI solutions show that the Gibbs function of the solution has a minimum at a certain protein concentration, but the protein chemical potential increases with increasing the concentration. The influences of temperature and protein chain length on the AFPI chemical potential were also discussed. The evaluation for the colligative depression of the freezing point confirms that the antifreeze action should be recognized as non-colligative. The theoretical deduction for the concentration dependence of the thermal hysteresis activity coincides qualitatively with the previous experimental and theoretical results.

Key words: Antifreeze protein solution, Gibbs function, Chemical potential, Thermal hysteresis