Antifreeze glycoproteins: Influence of polymer length and ice crystal habit on activity

Authors


  • Portions of this work have been published in a preliminary letter (Ref. 1) and have been presented at the American Chemical Society National Meeting, 1982, St. Louis, Mo. Parts of this material were taken from the theses of M.J.K. and T.S.B. submitted to the Graduate Division, University of California, Davis in partial fulfillment of the requirements for an M.S. degree.

Abstract

The effect of the ice crystalline habit and the length of the polymer on the ability of the antifreeze glycoproteins (AFGP) from polar fish to depress the freezing temperature of water was investigated. The low-molecular-weight components of the glycoproteins, AFGP- 6–8, are inactive when a solution of such a sample is nucleated at −6°C. A solution of large AFGP (1–4) is fully functional under the same conditions. The low-molecular-weight components differ from the height-molecular-weight components in that they contain some proline replacing the alanine in the Ala-Ala-Thr · disaccharide polymer unit. In the present experiments, antifreeze activity was examined in the presence of two different forms of ice crystal growth habits, and homodimders of AFGP 6 and 8 were prepared to investigate the function of polymer length and the on antifreeze activity at different degrees of supercooling. The results indicate that the ice crystal growth habit and the introduction of proline into the polymer unit may be responsible for the loss of activity at deep supercooling (−6°C) of AFGP 6–8. The loss in the ability of AFGP to depress the freezing temperature of water at deep supercooling is not solely due to polymer length, as carbodiimide-linked dimers of AFGP 6 do not function under these freezing conditions. A Model of antifreezing action based on Langmuirian adsorption of AFGP on the ice surface and direct competition between water and AFGP molecules for the incorporation sites in the ice crystal lattice is presented.

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