메뉴 건너뛰기




Volumn 46, Issue 1, 2012, Pages 425-436

Ice structuring proteins from plants: Mechanism of action and food application

Author keywords

Antifreeze activity assays; Antifreeze proteins; Cold stress; Ice crystallization recrystallization; Ice structuring proteins; Plants

Indexed keywords

ANTIFREEZE ACTIVITIES; ANTIFREEZE PROTEIN; COLD STRESS; COLD TOLERANCE; DIFFERENT MECHANISMS; DUAL ROLE; FOOD APPLICATIONS; FOOD INDUSTRIES; FOOD INGREDIENTS; FOOD SCIENCE; FROZEN FOOD; ICE CRYSTALLIZATION; ICE CRYSTALS; MECHANISM OF ACTION; NUCLEATING ACTIVITY; PATHOGENESIS-RELATED PROTEINS; PLANTS; THERMAL HYSTERESIS;

EID: 84857652009     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2011.12.018     Document Type: Review
Times cited : (91)

References (117)
  • 1
    • 0030067148 scopus 로고    scopus 로고
    • Immunolocalization of antifreeze proteins in winter rye leaves, crowns, and roots by tissue printing
    • Antikainen M., Griffith M., Zhang J., Hon W.C., Yang D.S.C., Pihakaski Maunsbach K. Immunolocalization of antifreeze proteins in winter rye leaves, crowns, and roots by tissue printing. Plant Physiology 1996, 110(3):845-857.
    • (1996) Plant Physiology , vol.110 , Issue.3 , pp. 845-857
    • Antikainen, M.1    Griffith, M.2    Zhang, J.3    Hon, W.C.4    Yang, D.S.C.5    Pihakaski Maunsbach, K.6
  • 2
    • 0344011029 scopus 로고    scopus 로고
    • Antifreeze proteins in higher plants
    • Atící Ö., Nalbantoǧlu B. Antifreeze proteins in higher plants. Phytochemistry 2003, 64:1187-1196.
    • (2003) Phytochemistry , vol.64 , pp. 1187-1196
    • Atící, Ö.1    Nalbantoǧlu, B.2
  • 5
    • 0034625046 scopus 로고    scopus 로고
    • Rapid evolution in plant chitinases: Molecular targets of selection in plant-pathogen coevolution
    • Bishop J.G., Dean A.M., Mitchell-Olds T. Rapid evolution in plant chitinases: Molecular targets of selection in plant-pathogen coevolution. National Academy of Science 2000, 97:5322-5327.
    • (2000) National Academy of Science , vol.97 , pp. 5322-5327
    • Bishop, J.G.1    Dean, A.M.2    Mitchell-Olds, T.3
  • 7
    • 0032872990 scopus 로고    scopus 로고
    • Ice-binding surface of fish type III antifreeze
    • Chen G., Jia Z. Ice-binding surface of fish type III antifreeze. Biophysical Journal 1999, 77:1602-1608.
    • (1999) Biophysical Journal , vol.77 , pp. 1602-1608
    • Chen, G.1    Jia, Z.2
  • 9
    • 0035983994 scopus 로고    scopus 로고
    • Ice structuring proteins-A new name for antifreeze proteins
    • Clarke C.J., Buckley S.L., Lindner N. Ice structuring proteins-A new name for antifreeze proteins. CryoLetters 2002, 23(2):89-92.
    • (2002) CryoLetters , vol.23 , Issue.2 , pp. 89-92
    • Clarke, C.J.1    Buckley, S.L.2    Lindner, N.3
  • 12
  • 14
    • 0001158716 scopus 로고    scopus 로고
    • Hydrogen bond analysis of Type I antifreeze protein in water and the ice/water interface
    • Dalal P., Knickelbein J., Haymet A.D.J., Sonnichsen F.D., Madura J.D. Hydrogen bond analysis of Type I antifreeze protein in water and the ice/water interface. PhysChemComm 2001, 7:1-5.
    • (2001) PhysChemComm , vol.7 , pp. 1-5
    • Dalal, P.1    Knickelbein, J.2    Haymet, A.D.J.3    Sonnichsen, F.D.4    Madura, J.D.5
  • 15
    • 38048999744 scopus 로고    scopus 로고
    • Inhibition of ice crystal growth in ice cream by gelatin hydrolysate
    • Damodaran S. Inhibition of ice crystal growth in ice cream by gelatin hydrolysate. Journal of Agricultural and Food Chemistry 2007, 55:10918-10923.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , pp. 10918-10923
    • Damodaran, S.1
  • 19
    • 0020653892 scopus 로고
    • Antifreeze peptides and glycopeptides in cold-water fishes
    • DeVries A.L. Antifreeze peptides and glycopeptides in cold-water fishes. Annual Review of Physiology 1983, 45:245-260.
    • (1983) Annual Review of Physiology , vol.45 , pp. 245-260
    • DeVries, A.L.1
  • 23
    • 0031811192 scopus 로고    scopus 로고
    • Antifreeze proteins: Current status and possible food uses
    • Feeney R.E., Yeh Y. Antifreeze proteins: Current status and possible food uses. Trends in Food Science and Technology 1998, 9:102-106.
    • (1998) Trends in Food Science and Technology , vol.9 , pp. 102-106
    • Feeney, R.E.1    Yeh, Y.2
  • 24
    • 0002333303 scopus 로고
    • Nature of the freezing process
    • Marcel Dekker Inc., New York, O.R. Fennema, W.D. Powrie, E.H. Marth (Eds.)
    • Fennema O.R. Nature of the freezing process. Low temperature preservation of foods and living matters 1973, 151-227. Marcel Dekker Inc., New York. O.R. Fennema, W.D. Powrie, E.H. Marth (Eds.).
    • (1973) Low temperature preservation of foods and living matters , pp. 151-227
    • Fennema, O.R.1
  • 26
    • 0009665409 scopus 로고    scopus 로고
    • Antifreeze polypeptide-expressing microorganisms useful in fermentation and freezing of foods
    • U. S. Patent 5676985.
    • Fletcher, G. L., Hew, C. L., Joshi, S. B., & Wu, Y. (1997). Antifreeze polypeptide-expressing microorganisms useful in fermentation and freezing of foods. U. S. Patent 5676985.
    • (1997)
    • Fletcher, G.L.1    Hew, C.L.2    Joshi, S.B.3    Wu, Y.4
  • 28
    • 84857647875 scopus 로고    scopus 로고
    • Ice-binding proteins adsorb to their ligand via anchored clathrate waters. Ph.D dissertation. Queen's University. accessed on 11/07/2011.
    • Garnham, C. P. (2011). Ice-binding proteins adsorb to their ligand via anchored clathrate waters. Ph.D dissertation. Queen's University. accessed on 11/07/2011. https://qspace.library.queensu.ca/handle/1974/6619.
    • (2011)
    • Garnham, C.P.1
  • 30
    • 55649109611 scopus 로고    scopus 로고
    • Food at subzero temperatures
    • Marcel Dekker Inc., New York, J.R. Dutcher, A.G. Marangoni (Eds.)
    • Goff H.D. Food at subzero temperatures. Soft materials structure and dynamics 2005, 229-320. Marcel Dekker Inc., New York. J.R. Dutcher, A.G. Marangoni (Eds.).
    • (2005) Soft materials structure and dynamics , pp. 229-320
    • Goff, H.D.1
  • 31
    • 0012892286 scopus 로고    scopus 로고
    • The potential for natural ice-structuring proteins in ice cream
    • Goff H.D., Regand A., Tharp B.W. The potential for natural ice-structuring proteins in ice cream. Dairy Industries International 2002, 67(10):30-32.
    • (2002) Dairy Industries International , vol.67 , Issue.10 , pp. 30-32
    • Goff, H.D.1    Regand, A.2    Tharp, B.W.3
  • 33
    • 0034691594 scopus 로고    scopus 로고
    • β-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect
    • Graether S.P., Kuiper M.J., Gagné S.M., Walker V.K., Jia Z., Sykes B.D., Davies P.L. β-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect. Nature 2001, 406:325-328.
    • (2001) Nature , vol.406 , pp. 325-328
    • Graether, S.P.1    Kuiper, M.J.2    Gagné, S.M.3    Walker, V.K.4    Jia, Z.5    Sykes, B.D.6    Davies, P.L.7
  • 34
    • 4344642832 scopus 로고    scopus 로고
    • Cold survival in freeze-intolerant insects. The structure and function of h-helical antifreeze proteins
    • Graether S.P., Sykes B.D. Cold survival in freeze-intolerant insects. The structure and function of h-helical antifreeze proteins. European Journal of Biochemistry 2004, 271:3285-3296.
    • (2004) European Journal of Biochemistry , vol.271 , pp. 3285-3296
    • Graether, S.P.1    Sykes, B.D.2
  • 35
    • 0033150319 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of spruce budworm antifreeze protein
    • Graether S.P., Ye Q.L., Davies P.L., Jia Z.C. Crystallization and preliminary X-ray crystallographic analysis of spruce budworm antifreeze protein. Journal of Structural Biology 1999, 126(1):72-75.
    • (1999) Journal of Structural Biology , vol.126 , Issue.1 , pp. 72-75
    • Graether, S.P.1    Ye, Q.L.2    Davies, P.L.3    Jia, Z.C.4
  • 40
    • 0028835687 scopus 로고
    • Antifreeze proteins and their potential uses in frozen foods
    • Griffith M., Ewart K.V. Antifreeze proteins and their potential uses in frozen foods. Biotechnology Advances 1995, 13:375-402.
    • (1995) Biotechnology Advances , vol.13 , pp. 375-402
    • Griffith, M.1    Ewart, K.V.2
  • 42
    • 4344568284 scopus 로고    scopus 로고
    • Antifreeze proteins in overwintering plants: A tale of two activities
    • Griffith M., Yaish M.W.F. Antifreeze proteins in overwintering plants: A tale of two activities. Trends in Plant Science 2004, 9(8):399-405.
    • (2004) Trends in Plant Science , vol.9 , Issue.8 , pp. 399-405
    • Griffith, M.1    Yaish, M.W.F.2
  • 43
    • 52949083132 scopus 로고    scopus 로고
    • Metabolic activity of cytochrome P450 isoforms in hepatocytes cryopreserved with wheat protein extract
    • Grondin M., Hamel F., Sarhan F., Averill-Bates D.A. Metabolic activity of cytochrome P450 isoforms in hepatocytes cryopreserved with wheat protein extract. Drug Metabolism and Disposition 2008, 36:2121-2129.
    • (2008) Drug Metabolism and Disposition , vol.36 , pp. 2121-2129
    • Grondin, M.1    Hamel, F.2    Sarhan, F.3    Averill-Bates, D.A.4
  • 44
    • 3542995705 scopus 로고    scopus 로고
    • The effect of water, sugars, and proteins on the pattern of ice nucleation and propagation in acclimated and nonacclimated canola leaves
    • Gusta L.V., Wisniewski M., Nesbitt N.T., Gusta M.L. The effect of water, sugars, and proteins on the pattern of ice nucleation and propagation in acclimated and nonacclimated canola leaves. Plant Physiology 2004, 135:1642-1653.
    • (2004) Plant Physiology , vol.135 , pp. 1642-1653
    • Gusta, L.V.1    Wisniewski, M.2    Nesbitt, N.T.3    Gusta, M.L.4
  • 45
    • 0022081053 scopus 로고
    • Altered gene expression during cold acclimation of spinach
    • Guy C.L., Niemi K.J., Brambl R. Altered gene expression during cold acclimation of spinach. National Academy of Science 1985, 82:3673-3677.
    • (1985) National Academy of Science , vol.82 , pp. 3673-3677
    • Guy, C.L.1    Niemi, K.J.2    Brambl, R.3
  • 47
    • 0024295490 scopus 로고
    • Differential scanning calorimetric analysis of antifreeze protein activity in the common mealworm, Tenebrio molitor
    • Hansen T.N., Baust J.G. Differential scanning calorimetric analysis of antifreeze protein activity in the common mealworm, Tenebrio molitor. Biochimica and Biophysica Acta 1988, 957:217-221.
    • (1988) Biochimica and Biophysica Acta , vol.957 , pp. 217-221
    • Hansen, T.N.1    Baust, J.G.2
  • 49
    • 0033568338 scopus 로고    scopus 로고
    • Type I antifreeze proteins. Structure activity studies and mechanisms of ice growth inhibition
    • Harding M.M., Ward L.G., Haymet A.D. Type I antifreeze proteins. Structure activity studies and mechanisms of ice growth inhibition. European Journal of Biochemistry 1999, 264:653-665.
    • (1999) European Journal of Biochemistry , vol.264 , pp. 653-665
    • Harding, M.M.1    Ward, L.G.2    Haymet, A.D.3
  • 50
    • 84857647872 scopus 로고    scopus 로고
    • Extraction, purification and study of the mechanism of action of apoplastic ice structuring proteins from cold acclimated winter wheat leaves
    • Ph.D. dissertation. University of Guelph. accessed on 10/15/2011.
    • Hassas-Roudsari, M. (2011). Extraction, purification and study of the mechanism of action of apoplastic ice structuring proteins from cold acclimated winter wheat leaves. Ph.D. dissertation. University of Guelph. accessed on 10/15/2011. https://dspace.lib.uoguelph.ca/xmlui/bitstream/handle/10214/2987/Final%20Thesis.pdf?sequence=1.
    • (2011)
    • Hassas-Roudsari, M.1
  • 51
    • 84857640834 scopus 로고    scopus 로고
    • A new quantitative method to measure activity of ice structuring proteins using differential scanning calorimetry
    • (in press)
    • Hassas-Roudsari, M., Goff, H. D. (in press) A new quantitative method to measure activity of ice structuring proteins using differential scanning calorimetry. Cryoletters.
    • Cryoletters.
    • Hassas-Roudsari, M.1    Goff, H.D.2
  • 52
    • 0032479347 scopus 로고    scopus 로고
    • Valine substituted winter flounder antifreeze: Preservation of ice growth hysteresis
    • Haymet A.D.J., Ward L.G., Harding M.M., Knight C.A. Valine substituted winter flounder antifreeze: Preservation of ice growth hysteresis. FEBS Letters 1998, 430:301-306.
    • (1998) FEBS Letters , vol.430 , pp. 301-306
    • Haymet, A.D.J.1    Ward, L.G.2    Harding, M.M.3    Knight, C.A.4
  • 54
    • 0028086816 scopus 로고
    • Extraction and isolation of antifreeze proteins from winter rye (Secale cereale L.) leaves
    • Hon W.-C., Griffith M., Chong P., Yang D.S.C. Extraction and isolation of antifreeze proteins from winter rye (Secale cereale L.) leaves. Plant Physiology 1994, 104:971-980.
    • (1994) Plant Physiology , vol.104 , pp. 971-980
    • Hon, W.-C.1    Griffith, M.2    Chong, P.3    Yang, D.S.C.4
  • 55
    • 0029411516 scopus 로고
    • Antifreeze proteins in winter rye are similar to pathogenesis-related proteins
    • Hon W.-C., Griffith M., Mlynarz A., Kwok Y.C., Yang D.S.C. Antifreeze proteins in winter rye are similar to pathogenesis-related proteins. Plant Physiology 1995, 109:879-889.
    • (1995) Plant Physiology , vol.109 , pp. 879-889
    • Hon, W.-C.1    Griffith, M.2    Mlynarz, A.3    Kwok, Y.C.4    Yang, D.S.C.5
  • 56
    • 64949105216 scopus 로고    scopus 로고
    • Cold adaptation in the phytopathogenic fungi causing snow molds
    • Hoshino T., Xiao N., Tkachenko O.B. Cold adaptation in the phytopathogenic fungi causing snow molds. Mycoscience 2009, 50(1):26-38.
    • (2009) Mycoscience , vol.50 , Issue.1 , pp. 26-38
    • Hoshino, T.1    Xiao, N.2    Tkachenko, O.B.3
  • 58
    • 0036009053 scopus 로고    scopus 로고
    • Cloning and characterization of a thermal hysteresis (antifreeze) protein with DNA-binding activity from winter bittersweet nightshade, Solanum dulcamara
    • Huang T., Duman J.G. Cloning and characterization of a thermal hysteresis (antifreeze) protein with DNA-binding activity from winter bittersweet nightshade, Solanum dulcamara. Plant Molecular Biology 2001, 48:339-350.
    • (2001) Plant Molecular Biology , vol.48 , pp. 339-350
    • Huang, T.1    Duman, J.G.2
  • 59
    • 0036470053 scopus 로고    scopus 로고
    • Antifreeze proteins: An unusual receptor-ligand interaction
    • Jia Z.C., Davies P.L. Antifreeze proteins: An unusual receptor-ligand interaction. Trends in Biochemical Sciences 2002, 27:101-106.
    • (2002) Trends in Biochemical Sciences , vol.27 , pp. 101-106
    • Jia, Z.C.1    Davies, P.L.2
  • 60
    • 2442665207 scopus 로고    scopus 로고
    • Theoretical study of interaction of winter flounder antifreeze protein with ice
    • Jorov A., Zhorov B.S., Yang D.S. Theoretical study of interaction of winter flounder antifreeze protein with ice. Protein Science 2004, 13:1524-1537.
    • (2004) Protein Science , vol.13 , pp. 1524-1537
    • Jorov, A.1    Zhorov, B.S.2    Yang, D.S.3
  • 61
    • 0034691564 scopus 로고    scopus 로고
    • Structural biology. Adding to the antifreeze agenda
    • Knight C.A. Structural biology. Adding to the antifreeze agenda. Nature 2000, 406:249-251.
    • (2000) Nature , vol.406 , pp. 249-251
    • Knight, C.A.1
  • 62
    • 0025959821 scopus 로고
    • Adsorption of alpha-helical antifreeze peptides on specific ice crystal-surface planes
    • Knight C.A., Cheng C.C., DeVries A.L. Adsorption of alpha-helical antifreeze peptides on specific ice crystal-surface planes. Biophysical Journal 1991, 59:409-418.
    • (1991) Biophysical Journal , vol.59 , pp. 409-418
    • Knight, C.A.1    Cheng, C.C.2    DeVries, A.L.3
  • 63
    • 0027396926 scopus 로고
    • Adsorption to ice of fish antifreeze glycopeptides-7 and glycopeptides-8
    • Knight C.A., Driggers E., DeVries A.L. Adsorption to ice of fish antifreeze glycopeptides-7 and glycopeptides-8. Biophysical Journal 1993, 64:252-259.
    • (1993) Biophysical Journal , vol.64 , pp. 252-259
    • Knight, C.A.1    Driggers, E.2    DeVries, A.L.3
  • 64
    • 0023840588 scopus 로고
    • Solute effects on ice recrystallization: An assessment technique
    • Knight C.A., Hallett J., DeVries A.L. Solute effects on ice recrystallization: An assessment technique. Cryobiology 1988, 25:55-60.
    • (1988) Cryobiology , vol.25 , pp. 55-60
    • Knight, C.A.1    Hallett, J.2    DeVries, A.L.3
  • 65
    • 40849135901 scopus 로고    scopus 로고
    • Effect of aging and ice-structuring proteins on physical properties of frozen flour-water mixtures
    • Kontogiorgos V., Goff H.D., Kasapis S. Effect of aging and ice-structuring proteins on physical properties of frozen flour-water mixtures. Food Hydrocolloids 2008, 22(6):1135-1147.
    • (2008) Food Hydrocolloids , vol.22 , Issue.6 , pp. 1135-1147
    • Kontogiorgos, V.1    Goff, H.D.2    Kasapis, S.3
  • 66
    • 28744456989 scopus 로고    scopus 로고
    • The mechanism by which fish antifreeze proteins cause thermal hysteresis
    • Kristiansen E., Zachariassen K.E. The mechanism by which fish antifreeze proteins cause thermal hysteresis. Cryobiology 2005, 51:262-280.
    • (2005) Cryobiology , vol.51 , pp. 262-280
    • Kristiansen, E.1    Zachariassen, K.E.2
  • 67
    • 0035193216 scopus 로고    scopus 로고
    • A theoretical model of a plant antifreeze protein from Lolium perenne
    • Kuiper M.J., Davies P.L., Walker V.K. A theoretical model of a plant antifreeze protein from Lolium perenne. Biophysical Journal 2001, 81(6):3560-3565.
    • (2001) Biophysical Journal , vol.81 , Issue.6 , pp. 3560-3565
    • Kuiper, M.J.1    Davies, P.L.2    Walker, V.K.3
  • 68
    • 0036258690 scopus 로고    scopus 로고
    • Abscisic acid- and cold-induced thaumatin-like protein in winter wheat has an antifungal activity against snow mould, Microdochium nivale
    • Kuwabara C., Takezawa D., Shimada T., Hamada T., Fujikawa S., Arakawa K. Abscisic acid- and cold-induced thaumatin-like protein in winter wheat has an antifungal activity against snow mould, Microdochium nivale. Physiologia Plantarum 2002, 115:101-110.
    • (2002) Physiologia Plantarum , vol.115 , pp. 101-110
    • Kuwabara, C.1    Takezawa, D.2    Shimada, T.3    Hamada, T.4    Fujikawa, S.5    Arakawa, K.6
  • 70
    • 77957551202 scopus 로고    scopus 로고
    • Effects of ice structuring proteins on freeze-thaw stability of corn and wheat starch gels
    • Li L., Kim Y., Huang W., Jia C., Xu B. Effects of ice structuring proteins on freeze-thaw stability of corn and wheat starch gels. Cereal Chemistry 2010, 87:497-503.
    • (2010) Cereal Chemistry , vol.87 , pp. 497-503
    • Li, L.1    Kim, Y.2    Huang, W.3    Jia, C.4    Xu, B.5
  • 71
    • 33745386446 scopus 로고    scopus 로고
    • Low-temperature tolerance and genetic potential in wheat (Triticum aestivum L.): Response to photoperiod, vernalization and plant development
    • Limin A.E., Fowler D.B. Low-temperature tolerance and genetic potential in wheat (Triticum aestivum L.): Response to photoperiod, vernalization and plant development. Planta 2006, 224:360-366.
    • (2006) Planta , vol.224 , pp. 360-366
    • Limin, A.E.1    Fowler, D.B.2
  • 72
    • 33646049352 scopus 로고    scopus 로고
    • Theoretical model of antifreeze protein-ice adsorption: Binding of large ligands to a two-dimensional homogenous lattice
    • Liu J., Li Q. Theoretical model of antifreeze protein-ice adsorption: Binding of large ligands to a two-dimensional homogenous lattice. Chemical Physics Letters 2006, 422:67-71.
    • (2006) Chemical Physics Letters , vol.422 , pp. 67-71
    • Liu, J.1    Li, Q.2
  • 74
    • 0036209679 scopus 로고    scopus 로고
    • Differential scanning calorimetric and circular dichroistic studies on plant antifreeze proteins
    • Lu M., Wang B., Li Zh., Fei Y., Wie L., Gao Sh. Differential scanning calorimetric and circular dichroistic studies on plant antifreeze proteins. Journal of Thermal Analysis and Calorimetry 2002, 67:689-698.
    • (2002) Journal of Thermal Analysis and Calorimetry , vol.67 , pp. 689-698
    • Lu, M.1    Wang, B.2    Li, Z.3    Fei, Y.4    Wie, L.5    Gao, S.6
  • 75
    • 0034113381 scopus 로고    scopus 로고
    • Molecular recognition and binding of thermal hysteresis proteins to ice
    • Madura J.D., Baran K., Wiezbicki A. Molecular recognition and binding of thermal hysteresis proteins to ice. Journal of Molecular Recognition 2000, 13:101-113.
    • (2000) Journal of Molecular Recognition , vol.13 , pp. 101-113
    • Madura, J.D.1    Baran, K.2    Wiezbicki, A.3
  • 76
    • 84989665769 scopus 로고
    • Proteins accumulate in the apoplast of winter rye leaves during cold acclimation
    • Marentes E., Griffith M., Mlynarz A., Brush R.A. Proteins accumulate in the apoplast of winter rye leaves during cold acclimation. Plant Physiology 1993, 87:499-507.
    • (1993) Plant Physiology , vol.87 , pp. 499-507
    • Marentes, E.1    Griffith, M.2    Mlynarz, A.3    Brush, R.A.4
  • 77
    • 0032973262 scopus 로고    scopus 로고
    • A leucine-rich repeat protein of carrot that exhibits antifreeze activity
    • Meyer K., Keil M., Naldrett M.J. A leucine-rich repeat protein of carrot that exhibits antifreeze activity. FEBS Letters 1999, 447:171-178.
    • (1999) FEBS Letters , vol.447 , pp. 171-178
    • Meyer, K.1    Keil, M.2    Naldrett, M.J.3
  • 79
    • 30544451084 scopus 로고    scopus 로고
    • Heterologous expression of type I antifreeze peptide GS-5 in baker's yeast increases freeze tolerance and provides enhanced gas production in frozen dough
    • Panadero J., Randez-Gil F., Prieto J.A. Heterologous expression of type I antifreeze peptide GS-5 in baker's yeast increases freeze tolerance and provides enhanced gas production in frozen dough. Journal of Agricultural and Food Chemistry 2005, 53(26):9966-9970.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.26 , pp. 9966-9970
    • Panadero, J.1    Randez-Gil, F.2    Prieto, J.A.3
  • 80
    • 21344488051 scopus 로고
    • The effects of antifreeze proteins on chilled and frozen meats
    • Payne S.R., Sandford D., Harris A., Young O.A. The effects of antifreeze proteins on chilled and frozen meats. Meat Science 1994, 37:429-438.
    • (1994) Meat Science , vol.37 , pp. 429-438
    • Payne, S.R.1    Sandford, D.2    Harris, A.3    Young, O.A.4
  • 81
    • 21844481638 scopus 로고
    • Effects of pre-slaughter administration of antifreeze proteins on frozen meat quality
    • Payne S.R., Young O.A. Effects of pre-slaughter administration of antifreeze proteins on frozen meat quality. Meat Science 1995, 41:147-155.
    • (1995) Meat Science , vol.41 , pp. 147-155
    • Payne, S.R.1    Young, O.A.2
  • 82
    • 0001607990 scopus 로고
    • Cell-shape and localization of ice in leaves of overwintering wheat during frost stress in the field
    • Pearce R.S., Ashworth E.N. Cell-shape and localization of ice in leaves of overwintering wheat during frost stress in the field. Planta 1992, 188:324-331.
    • (1992) Planta , vol.188 , pp. 324-331
    • Pearce, R.S.1    Ashworth, E.N.2
  • 84
    • 0037240232 scopus 로고    scopus 로고
    • Structure and ice recrystallization in frozen stabilized ice cream model systems
    • Regand A., Goff H.D. Structure and ice recrystallization in frozen stabilized ice cream model systems. Food Hydrocolloids 2003, 17:95-102.
    • (2003) Food Hydrocolloids , vol.17 , pp. 95-102
    • Regand, A.1    Goff, H.D.2
  • 85
    • 29544432160 scopus 로고    scopus 로고
    • Freezing and ice recrystallization properties of sucrose solutions containing ice structuring proteins from cold acclimated winter wheat grass extract
    • Regand A., Goff H.D. Freezing and ice recrystallization properties of sucrose solutions containing ice structuring proteins from cold acclimated winter wheat grass extract. Journal of Food Science 2005, 70:E552-E556.
    • (2005) Journal of Food Science , vol.70
    • Regand, A.1    Goff, H.D.2
  • 86
    • 30844452668 scopus 로고    scopus 로고
    • Ice recrystaization inhibition in ice cream as affected by ice structuring proteins from winter wheat grass
    • Regand A., Goff H.D. Ice recrystaization inhibition in ice cream as affected by ice structuring proteins from winter wheat grass. Journal of Dairy Science 2006, 89:49-57.
    • (2006) Journal of Dairy Science , vol.89 , pp. 49-57
    • Regand, A.1    Goff, H.D.2
  • 88
    • 0001817934 scopus 로고    scopus 로고
    • Fundamental aspects of the freezing process
    • Marcel Dekker Inc., New York, L.E. Jeremiah (Ed.)
    • Sahagian M.E., Goff H.D. Fundamental aspects of the freezing process. Freezing effects on food quality 1996, 1-50. Marcel Dekker Inc., New York. L.E. Jeremiah (Ed.).
    • (1996) Freezing effects on food quality , pp. 1-50
    • Sahagian, M.E.1    Goff, H.D.2
  • 92
    • 0033917639 scopus 로고    scopus 로고
    • Plant-pathogen arms races at the molecular level
    • Stahl E.A., Bishop J.G. Plant-pathogen arms races at the molecular level. Current Opinion in Plant Biology 2000, 3(4):299-304.
    • (2000) Current Opinion in Plant Biology , vol.3 , Issue.4 , pp. 299-304
    • Stahl, E.A.1    Bishop, J.G.2
  • 93
    • 20444363811 scopus 로고    scopus 로고
    • Remembering winter: Toward a molecular understanding of vernalization
    • Sung S., Amasino R.M. Remembering winter: Toward a molecular understanding of vernalization. Annual Review of Plant Biology 2005, 56:491-508.
    • (2005) Annual Review of Plant Biology , vol.56 , pp. 491-508
    • Sung, S.1    Amasino, R.M.2
  • 94
    • 34447322409 scopus 로고    scopus 로고
    • Molecular genetic studies of the memory of winter
    • Sung S., Amasino R.M. Molecular genetic studies of the memory of winter. Journal of Experimental Botany 2006, 57:3369-3377.
    • (2006) Journal of Experimental Botany , vol.57 , pp. 3369-3377
    • Sung, S.1    Amasino, R.M.2
  • 95
    • 0002132589 scopus 로고    scopus 로고
    • Recrystallization in model ice cream solutions as affected by stabilizer concentration
    • Sutton R.L., Wilcox J. Recrystallization in model ice cream solutions as affected by stabilizer concentration. Journal of Food Science 1998, 63:9-11.
    • (1998) Journal of Food Science , vol.63 , pp. 9-11
    • Sutton, R.L.1    Wilcox, J.2
  • 97
    • 0035144222 scopus 로고    scopus 로고
    • So what's new in the field of plant cold acclimation? Lots!
    • Thomashow M.F. So what's new in the field of plant cold acclimation? Lots!. Plant Physiology 2001, 125:89-93.
    • (2001) Plant Physiology , vol.125 , pp. 89-93
    • Thomashow, M.F.1
  • 100
    • 40349103663 scopus 로고    scopus 로고
    • Properties, potentials, and prospects of antifreeze proteins
    • Venketesh S., Dayananda C. Properties, potentials, and prospects of antifreeze proteins. Critical Reviews in Biotechnology 2008, 28(1):57-82.
    • (2008) Critical Reviews in Biotechnology , vol.28 , Issue.1 , pp. 57-82
    • Venketesh, S.1    Dayananda, C.2
  • 101
    • 31544483880 scopus 로고    scopus 로고
    • A thaumatin-like protein from larvae of the beetle Dendroides canadensis enhances the activity of antifreeze proteins
    • Wang L., Duman J.G. A thaumatin-like protein from larvae of the beetle Dendroides canadensis enhances the activity of antifreeze proteins. Biochemistry 2006, 45:1278-1284.
    • (2006) Biochemistry , vol.45 , pp. 1278-1284
    • Wang, L.1    Duman, J.G.2
  • 102
    • 55649091387 scopus 로고    scopus 로고
    • Controlling the freezing process with antifreeze proteins
    • Elsevier, London, D. Sun (Ed.)
    • Wathen B., Jia Z. Controlling the freezing process with antifreeze proteins. Emerging technologies for food processing 2005, 653-674. Elsevier, London. D. Sun (Ed.).
    • (2005) Emerging technologies for food processing , pp. 653-674
    • Wathen, B.1    Jia, Z.2
  • 103
    • 0037460192 scopus 로고    scopus 로고
    • A new model for simulating 3-D crystal growth and its application to the study of antifreeze proteins
    • Wathen B., Kuiper M., Walker V., Jia Z. A new model for simulating 3-D crystal growth and its application to the study of antifreeze proteins. Journal of the American Chemical Society 2003, 125(3):729-737.
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.3 , pp. 729-737
    • Wathen, B.1    Kuiper, M.2    Walker, V.3    Jia, Z.4
  • 104
    • 0027459477 scopus 로고
    • A D-antifreeze polypeptide displays the same activity as its natural L-enantiomer
    • Wen D., Laursen R.A. A D-antifreeze polypeptide displays the same activity as its natural L-enantiomer. FEBS Letters 1993, 317:31-34.
    • (1993) FEBS Letters , vol.317 , pp. 31-34
    • Wen, D.1    Laursen, R.A.2
  • 105
    • 34548647991 scopus 로고    scopus 로고
    • Antifreeze proteins at the ice/water interface: Three calculated discriminating properties for orientation of type I proteins
    • Wierzbicki A., Dalal P., Cheatham T.E., Knickelbein J.E., Haymet A.D.J., Madura J.D. Antifreeze proteins at the ice/water interface: Three calculated discriminating properties for orientation of type I proteins. Biophysical Journal 2007, 93(5):1442-1451.
    • (2007) Biophysical Journal , vol.93 , Issue.5 , pp. 1442-1451
    • Wierzbicki, A.1    Dalal, P.2    Cheatham, T.E.3    Knickelbein, J.E.4    Haymet, A.D.J.5    Madura, J.D.6
  • 107
    • 0033047676 scopus 로고    scopus 로고
    • Purification, immunolocalization, cryoprotective, and antifreeze activity of PCA60: A dehydrin from peach (Prunus persica)
    • Wisniewski M., Webb R., Balsamo R., Close T.J., Yu X.-M., Griffith M. Purification, immunolocalization, cryoprotective, and antifreeze activity of PCA60: A dehydrin from peach (Prunus persica). Physiologia Plantarum 1999, 105:600-608.
    • (1999) Physiologia Plantarum , vol.105 , pp. 600-608
    • Wisniewski, M.1    Webb, R.2    Balsamo, R.3    Close, T.J.4    Yu, X.-M.5    Griffith, M.6
  • 108
    • 61749101133 scopus 로고    scopus 로고
    • Evaluation of water holding capacity and breadmaking properties for frozen dough containing ice structuring proteins from winter wheat
    • Xu H.N., Huang W.N., Jia C.L., Kim Y.S., Liu H.P. Evaluation of water holding capacity and breadmaking properties for frozen dough containing ice structuring proteins from winter wheat. Journal of Cereal Science 2009, 49:250-253.
    • (2009) Journal of Cereal Science , vol.49 , pp. 250-253
    • Xu, H.N.1    Huang, W.N.2    Jia, C.L.3    Kim, Y.S.4    Liu, H.P.5
  • 110
    • 0031968333 scopus 로고    scopus 로고
    • Identification of the ice-binding surface on type III antifreeze protein with a 'flatness function' algorithm
    • Yang D.S., Hon W.C., Bubanko S., Xue Y., Seetharaman J., Hew C.L., Sicheri F. Identification of the ice-binding surface on type III antifreeze protein with a 'flatness function' algorithm. Biophysical Journal 1998, 74(5):2142-2151.
    • (1998) Biophysical Journal , vol.74 , Issue.5 , pp. 2142-2151
    • Yang, D.S.1    Hon, W.C.2    Bubanko, S.3    Xue, Y.4    Seetharaman, J.5    Hew, C.L.6    Sicheri, F.7
  • 111
    • 9144257407 scopus 로고    scopus 로고
    • Antifreeze proteins: Structures and mechanisms of function
    • Yeh Y., Feeney R.E. Antifreeze proteins: Structures and mechanisms of function. Chemical Reviews 1996, 96:601-617.
    • (1996) Chemical Reviews , vol.96 , pp. 601-617
    • Yeh, Y.1    Feeney, R.E.2
  • 112
    • 67650879321 scopus 로고    scopus 로고
    • Production of a recombinant type 1 antifreeze protein analogue by Lactococcus lactis and its application on frozen meat and frozen dough
    • Yeh C.M., Kao B.Y., Peng H.J. Production of a recombinant type 1 antifreeze protein analogue by Lactococcus lactis and its application on frozen meat and frozen dough. Journal of Agricultural and Food Chemistry 2009, 57(14):6216-6223.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , Issue.14 , pp. 6216-6223
    • Yeh, C.M.1    Kao, B.Y.2    Peng, H.J.3
  • 114
    • 0032770110 scopus 로고    scopus 로고
    • Antifreeze proteins in winter rye leaves form oligomeric complexes
    • Yu X.M., Griffith M. Antifreeze proteins in winter rye leaves form oligomeric complexes. Plant Physiology 1999, 119(4):1361-1370.
    • (1999) Plant Physiology , vol.119 , Issue.4 , pp. 1361-1370
    • Yu, X.M.1    Griffith, M.2
  • 115
    • 0034480912 scopus 로고    scopus 로고
    • Ice nucleation and antinucleation in nature
    • Zachariassen K.E., Kristiansen E. Ice nucleation and antinucleation in nature. Cryobiology 2000, 41(4):257-279.
    • (2000) Cryobiology , vol.41 , Issue.4 , pp. 257-279
    • Zachariassen, K.E.1    Kristiansen, E.2
  • 116
    • 70349819779 scopus 로고    scopus 로고
    • Physical-chemical principles in freezing
    • Taylor and Francis Group, Florida, D. Sun (Ed.)
    • Zaritzky N. Physical-chemical principles in freezing. Handbook of frozen food packaging and processing 2006, 23-25. Taylor and Francis Group, Florida. D. Sun (Ed.).
    • (2006) Handbook of frozen food packaging and processing , pp. 23-25
    • Zaritzky, N.1
  • 117
    • 34247590409 scopus 로고    scopus 로고
    • Effect of carrot (Daucus carota) antifreeze proteins on the fermentation capacity of frozen dough
    • Zhang C., Zhang H., Wang L. Effect of carrot (Daucus carota) antifreeze proteins on the fermentation capacity of frozen dough. Food Research International 2007, 40(6):763-769.
    • (2007) Food Research International , vol.40 , Issue.6 , pp. 763-769
    • Zhang, C.1    Zhang, H.2    Wang, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.