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  • 1 Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, Urumqi 830046, China, lzy1168@gmail.com, lilyxjmm@163.com
  • | 2 School of Medicine, Tsinghua University, Hai'dian District, Beijing 100084, China, lihongleihn@163.com
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Abstract

Many ectotherms organisms produce antifreeze proteins (AFPs), also known as thermal hysteresis proteins (THPs), which can lower the freezing temperature of body liquids without significantly affecting the melting point. In this article, thermal hysteresis activity (THA) of ApAFP752 from the desert beetle Anatolica polita was measured with differential scanning calorimetry (DSC). When the ice fraction was less than 25.3%, a delay in the onset temperature of refreezing was observed, indicating that the ApAFP752 solution has thermal hysteresis effect. When the amount of ice in the solution was less than 5.1%, THA of the ApAFP752 reached as high as 0.76 °C. THA of ApAFP752 was concentration-dependent. Hydrophilic ability of ApAFP752 was evaluated by thermal gravimetry (TG). The results of TG showed that ApAFP752 has strong hydrophilicity. The secondary structure of ApAFP752 was studied with circular dichroism (CD). The CD spectrum from 190 to 240 nm indicated a well-defined secondary structure consisting of 11.1% α-helix, 53.6% β-sheet, 8.3% turn, and 27.0% random coil.

  • 1. Knight, CA, Cheng, CC De Vries, AL Adsorption of α-helical antifreeze peptides on specific ice crystal surface planes. Biophys J 1991 59:409418 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 2. Sidebottom, C, Buckley, S, Pudney, P, Twigg, S, Jarman, C, Holt, C, Telford, J, McArthu, A, Worrall, D, Hubbard, R, Lillford, P. Heat-stable antifreeze protein from grass. Nature 2000 406:256 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 3. Graham, LA, Davies, PL. Glycine-rich antifreeze proteins from snow fleas. Science 2005 310:461 .

  • 4. Wierzbicki, A, Dalal, P, Cheatham, TE, Knickelbein, JE, Haymet, ADJ, Madura, JD. Antifreeze proteins at the ice/water interface: three calculated discriminating properties for orientation of type I proteins. Biophys J 2007 93:14421451 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 5. Li, N, Chibber, BAK, Castellino, FJ, Duman, JG. Mapping of disulfide bridges in antifreeze proteins from overwintering larvae of the beetle Dendroidesc anadensis. Biochemistry 1998 37:63436350 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 6. Feeney, RE, Hofmann, R. Depression of freezing point by glycoproteins from an Antarctic fish. Nature 1973 243:357359 .

  • 7. Wang, S, Amornwittawat, N, Juwita, V, Kao, Y, Duman, JG, Pascal, TA, Goddard, WA, Wen, X. Arginine, a key residue for the enhancing ability of an antifreeze protein of the Beetle Dendroides canadensis. Biochemistry 2009 48:96969703 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 8. Fletcher, GL, Goddard, SV, Wu, Y. Antifreeze proteins and their genes: from basic research to business opportunity. Chemtech 1999 30:1728.

    • Search Google Scholar
    • Export Citation
  • 9. Venketesh, S, Dayananda, C. Properties, potentials, and prospects of antifreeze proteins. Crit Rev Biotechnol 2008 28:5782 .

  • 10. Yeh, CM, Kao, BY, Peng, HJ. Production of a recombinant type 1 antifreeze protein analogue by L. lactis and its applications on frozen meat and frozen dough. J Agric Food Chem 2009 57:62166223 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 11. Zhang, C, Zhang, H, Wang, L. Effect of carrot (Daucus carota) antifreeze proteins on the fermentation capacity of frozen dough. Food Res Int 2007 40:763769 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 12. Liou, YC, Tocilj, A, Davies, P, Jia, ZC. Mimicry of ice structure by surface hydroxyls and water of a β-helix antifreeze protein. Nature 2000 406:322324 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 13. Marshall, CB, Daley, ME, Sykes, BD, Davies, PL. Enhancing the activity of a β-helical antifreeze protein by the engineered addition of coils. Biochemistry 2004 43:1163711646 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 14. Graether, SP, Kuiper, MJ, Gagne, SM, Walker, VK, Jia, ZC, Sykes, BD. Davies PL. β-Helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect. Nature 2000 406:325328 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 15. Jia, ZC, Davies, PL. Antifreeze proteins: an unusual receptor–ligand interaction. Trends Biochem Sci 2002 27:101106 .

  • 16. Nicodemus, J, O'tousa, JE, Duman, JG. Expression of a beetle, Dendroides canadensis, antifreeze protein in Drosophila melanogaster. J Insect Physiol 2006 52:888896 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 17. Lin, X, O'tousa, JE, Duman, JG. Expression of two self-enhancing antifreeze proteins from the beetle Dendroides canadensis in Drosophila melanogaster. J Insect Physiol 2010 56:341349 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 18. Qiu, LM, Ma, J, Wang, J, Zhang, FC, Wang, Y. Thermal stability properties of an antifreeze protein from the desert beetle Microdera punctipennis. Cryobiology 2010 60:192197 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 19. Hansen, TN, Baust, JG. Differential scanning calorimetric analysis of antifreeze protein activity in the common mealworm, Tenebrio molitor. Biochim Biophys Acta 1988 957:217221 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 20. Lu, M, Wang, B, Li, Z, Fei, Y, Wei, L, Gao, Sh. Differential scanning calorimetric and circular dichroistic studies on plant antifreeze proteins. J Therm Anal Calorim 2002 67:689698 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 21. Ramlov, H De Vries, AL Wilson, PW. Antifreeze glycoproteins from the Antarctic fish Dissostichus mawsoni studied by differential scanning calorimetry (DSC) in combination with nanolitre osmometry. Cryo Lett. 2005;26:7384.

    • Search Google Scholar
    • Export Citation
  • 22. Hansen, TN De Vries, AL Baust, JG. Calorimetric analysis of antifreeze glycoproteins of the polar fish, Dissostichus mawsoni 1991. Biochim Biophys Acta 1079:169173 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 23. Amornwittawat, N, Wang, S, Duman, JG, Wen, X. Polycarboxylates enhance beetle antifreeze protein activity. Biochim Biophy Acta 2008 1784:19421948.

    • Search Google Scholar
    • Export Citation
  • 24. Thelma, M, Virginia, CA, Ana, M. Thermal behavior of in vitro mineralized anionic collagen matrices. J Therm Anal Calorim 2009 95:945949 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 25. Vijayasundaram, V, Ramasamy, V, Palaniappan, PLRM. The study of the changes in the thermal properties of Labeo rohita bones due to arsenic exposure. J Therm Anal Calorim 2009 98:183188 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 26. Sohar, G, Pallagi, E, Szabo-Revesz, P, Toth, K. New thermogravimetric protocol for the investigation of normal and damaged human hyaline cartilage. J Therm Anal Calorim 2007 89:853856 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 27. Öz, S, Kurtaran, R, Arıcı, C, Ergun, Ü, Dinçer Kaya, FN, Emregül, KC, Atakol, O, Ülkü, D. Two non-linear azide containing heteronuclear complexes: crystal structure and thermal decomposition. J Therm Anal Calorim 2010 99:363368 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 28. Verdu, JR, Casas, JL, Lobo, JM, Numa, C. Dung beetles eat acorns to increase their ovarian development and thermal tolerance. PLoS ONE 2010 5:18 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 29. Zhang, C, Zhang, H, Wang, L, Yao, HY. Validation of antifreeze properties of glutathione based on its thermodynamic characteristics and protection of baker's yeast during cryopreservation. J Agric Food Chem 2007 55:46984703 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 30. Zhang, C, Zhang, H, Wang, L, Zhang, JH, Yao, HY. Purification of antifreeze protein from wheat bran (Triticum aestivun L.) based on its hydrophilicity and ice-binding capacity. J Agric Food Chem 2007 55:76547658 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 31. Li, N, Kendric, BS, Manning, MC, Carpenter, JF, Duman, JG. Secondary structure of antifreeze proteins from overwintering larvae of the beetle Dendroides canadensis. Arch Biochem Biophys 1998 360:2532 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 32. Sieber, V, Jurnak, F, Moe, GR. Circular dichroism of the parallel beta helical proteins pectate lyase C and E. Proteins 1995 23:3237 .

  • 33. Nishimiya, Y, Kondo, H, Takamichi, M, Sugimoto, H, Suzuki, M, Miura, A, Tsuda, S. Crystal structure and mutational analysis of Ca2+-independent type II antifreeze protein from Longsnout Poacher, Brachyopsis rostratus. J Mol Biol 2008 382:734746 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 34. Graham, LA, Liou, YC, Walker, VK, Davies, PL. Hyperactive antifreeze protein from beetles. Nature 1997 388:727728 .

  • 35. Deng, G, Andrews, DW, Laursen, RA. Amino acid sequence of a new type of antifreeze protein from the longhorn sculpin Myoxocephalus octodecinspittosis. FEBS Lett 1997 402:1720 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 36. Dijk, LV, Bobbert, PA, Spano, FC. Extreme sensitivity of circular dichroism to long-range excitonic couplings in helical supramolecular assemblies. J Phys Chem B 2010 114:817825 .

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 37. Fiche, JB, Laredo, T, Tanchak, O, Lipkowski, J, Dutcher, JR, Yada, RY. Influence of an electric field on oriented films of DMPC/gramicidin bilayers: a circular dichroism study. Langmuir 2010 26:10571066 .

    • Crossref
    • Search Google Scholar
    • Export Citation