메뉴 건너뛰기




Volumn 31, Issue 8-9, 2010, Pages 943-956

Selection of low-temperature resistance in bacteria and potential applications

Author keywords

antifreeze proteins; freeze thaw stress; ice affinity; ice nucleation proteins; osmotic stress

Indexed keywords

BACTERIA; NUCLEATION; OSMOSIS; PROTEINS; TEMPERATURE CONTROL; THAWING;

EID: 77953716333     PISSN: 09593330     EISSN: 1479487X     Source Type: Journal    
DOI: 10.1080/09593331003782417     Document Type: Review
Times cited : (23)

References (107)
  • 1
    • 0034763035 scopus 로고    scopus 로고
    • Relationship between antifreeze protein and freezing resistance in Pseudomonas putida GR12-2
    • H. Kawahara, J. Li, M. Griffith, and B.R. Glick, Relationship between antifreeze protein and freezing resistance in Pseudomonas putida GR12-2, Curr. Microbiol. 43 (2001), pp. 365-370.
    • (2001) Curr. Microbiol. , vol.43 , pp. 365-370
    • Kawahara, H.1    Li, J.2    Griffith, M.3    Glick, B.R.4
  • 4
    • 0016516090 scopus 로고
    • Psychrophilic bacteria
    • R.Y. Morita, Psychrophilic bacteria, Bacteriol. Rev. 39 (1975), pp. 144-167.
    • (1975) Bacteriol. Rev. , vol.39 , pp. 144-167
    • Morita, R.Y.1
  • 7
    • 33846222278 scopus 로고    scopus 로고
    • Characterization of the microbial diversity in a permafrost sample from the Canadian high Arctic using culture-dependent and culture-independent methods
    • B. Steven, G. Briggs, C.P. McKay, W.H. Pollard, C.W. Greer, and L.G. Whyte, Characterization of the microbial diversity in a permafrost sample from the Canadian high Arctic using culture-dependent and culture-independent methods, FEMS Microbiol. Ecol. 59 (2007), pp. 513-523.
    • (2007) FEMS Microbiol. Ecol. , vol.59 , pp. 513-523
    • Steven, B.1    Briggs, G.2    McKay, C.P.3    Pollard, W.H.4    Greer, C.W.5    Whyte, L.G.6
  • 8
    • 0018256468 scopus 로고
    • Effect of freezing and thawing on survival of three bacterial isolates from an arctic soil
    • L.M. Nelson and D. Parkinson, Effect of freezing and thawing on survival of three bacterial isolates from an arctic soil, Can. J. Microbiol. 24 (1978), pp. 1468-1474.
    • (1978) Can. J. Microbiol. , vol.24 , pp. 1468-1474
    • Nelson, L.M.1    Parkinson, D.2
  • 9
    • 33644932401 scopus 로고    scopus 로고
    • Freeze- thaw tolerance and clues to the winter survival of a soil community
    • V.K. Walker, G.R. Palmer, and G. Voordouw, Freeze- thaw tolerance and clues to the winter survival of a soil community, Appl. Environ. Microbiol. 72 (2006), pp. 1784-1792.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 1784-1792
    • Walker, V.K.1    Palmer, G.R.2    Voordouw, G.3
  • 11
    • 0019813532 scopus 로고
    • Effect of defined lipopolysaccharide core defects on resistance of Salmonella typhimurium to freezing and thawing and other stresses
    • G.M. Bennett, A. Seaver, and P.H. Calcott, Effect of defined lipopolysaccharide core defects on resistance of Salmonella typhimurium to freezing and thawing and other stresses, Appl. Environ. Microbiol. 42 (1981), pp. 843-849.
    • (1981) Appl. Environ. Microbiol. , vol.42 , pp. 843-849
    • Bennett, G.M.1    Seaver, A.2    Calcott, P.H.3
  • 12
    • 0035039666 scopus 로고    scopus 로고
    • Maintenance of membrane fluidity in Antarctic bacteria
    • M.K. Chattopadhyay and M.V. Jagannadham, Maintenance of membrane fluidity in Antarctic bacteria, Polar Biol. 24 (2001), pp. 386-388.
    • (2001) Polar Biol. , vol.24 , pp. 386-388
    • Chattopadhyay, M.K.1    Jagannadham, M.V.2
  • 13
    • 0016424293 scopus 로고
    • Mechanism of injury of Escherichia coli by freezing and thawing
    • M.D. Alur and N. Grecz, Mechanism of injury of Escherichia coli by freezing and thawing, Biochem. Biophys. Res. Commun. 62 (1975), pp. 308-312.
    • (1975) Biochem. Biophys. Res. Commun. , vol.62 , pp. 308-312
    • Alur, M.D.1    Grecz, N.2
  • 14
    • 0016679440 scopus 로고
    • The survival of Escherichia coli from freeze-thaw damage: The relative importance of wall and membrane damage
    • P.H. Calcott and R.A. MacLeod, The survival of Escherichia coli from freeze-thaw damage: The relative importance of wall and membrane damage, Can. J. Microbiol. 21 (1975), pp. 1960-1968.
    • (1975) Can. J. Microbiol. , vol.21 , pp. 1960-1968
    • Calcott, P.H.1    MacLeod, R.A.2
  • 15
    • 0013870042 scopus 로고
    • Theoretical and experimental effects of cooling and warming velocity on the survival of frozen and thawed cells
    • P. Mazur, Theoretical and experimental effects of cooling and warming velocity on the survival of frozen and thawed cells, Cryobiology 2 (1966), pp. 181-192.
    • (1966) Cryobiology , vol.2 , pp. 181-192
    • Mazur, P.1
  • 16
    • 0033932215 scopus 로고    scopus 로고
    • Roles of Fe superoxide dismutase and catalase in resistance of Campylobacter coli to freeze-thaw stress
    • D. Stead and S.F. Park, Roles of Fe superoxide dismutase and catalase in resistance of Campylobacter coli to freeze-thaw stress, Appl. Environ. Microbiol. 66 (2000), pp. 3110-3112.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 3110-3112
    • Stead, D.1    Park, S.F.2
  • 18
    • 0345828890 scopus 로고    scopus 로고
    • Bacterial activity at -2 to -20 °c in Arctic wintertime sea ice
    • K. Junge, H. Eicken, and J.W. Deming, Bacterial activity at -2 to -20 °C in Arctic wintertime sea ice, Appl. Environ. Microbiol. 70 (2004), pp. 550-557.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 550-557
    • Junge, K.1    Eicken, H.2    Deming, J.W.3
  • 19
    • 61449147160 scopus 로고    scopus 로고
    • Macromolecular synthesis by yeasts under frozen conditions
    • P. Amato, S. Doyle, and B.C. Christner, Macromolecular synthesis by yeasts under frozen conditions, Environ. Microbiol. 11 (2009), pp. 589-596.
    • (2009) Environ. Microbiol. , vol.11 , pp. 589-596
    • Amato, P.1    Doyle, S.2    Christner, B.C.3
  • 21
    • 0034020098 scopus 로고    scopus 로고
    • Fatty acid composition and freeze-thaw resistance in lactobacilli
    • A. Gómez Zavaglia, E.A. Disalvo, and G.L. De Antoni, Fatty acid composition and freeze-thaw resistance in lactobacilli, J. Dairy Res. 67 (2000), pp. 241-247.
    • (2000) J. Dairy Res. , vol.67 , pp. 241-247
    • Gómez Zavaglia, A.1    Disalvo, E.A.2    De Antoni, G.L.3
  • 22
    • 0016222684 scopus 로고
    • Survival of Escherichia coli from freeze-thaw damage: A theoretical and practical study
    • P.H. Calcott and R.A. MacLeod, Survival of Escherichia coli from freeze-thaw damage: A theoretical and practical study, Can. J. Microbiol. 20 (1974), pp. 671-681.
    • (1974) Can. J. Microbiol. , vol.20 , pp. 671-681
    • Calcott, P.H.1    MacLeod, R.A.2
  • 23
    • 0016200433 scopus 로고
    • Survival of Escherichia coli from freeze-thaw damage: Influence of nutritional status and growth rate
    • P.H. Calcott and R.A. MacLeod, Survival of Escherichia coli from freeze-thaw damage: Influence of nutritional status and growth rate, Can. J. Microbiol. 20 (1974), pp. 683-689.
    • (1974) Can. J. Microbiol. , vol.20 , pp. 683-689
    • Calcott, P.H.1    MacLeod, R.A.2
  • 24
    • 33745192637 scopus 로고    scopus 로고
    • Natural freezing as a wastewater treatment method: E. coli inactivation capacity
    • W. Gao, D.W. Smith, and Y. Li, Natural freezing as a wastewater treatment method: E. coli inactivation capacity, Water Res. 40 (2006), pp. 2321-2326.
    • (2006) Water Res. , vol.40 , pp. 2321-2326
    • Gao, W.1    Smith, D.W.2    Li, Y.3
  • 25
    • 0000434018 scopus 로고
    • Kinetics of water loss from cells at sub-zero temperatures and the likelihood of intracellular freezing
    • P. Mazur, Kinetics of water loss from cells at sub-zero temperatures and the likelihood of intracellular freezing, J. Gen. Physiol. 47 (1963), pp. 347-369.
    • (1963) J. Gen. Physiol. , vol.47 , pp. 347-369
    • Mazur, P.1
  • 26
    • 0014842224 scopus 로고
    • Freeze-thaw behavior of a moderately halophilic bacterium as a function of salt concentration
    • P.H. Deal, Freeze-thaw behavior of a moderately halophilic bacterium as a function of salt concentration, Cryobiology 7 (1970), pp. 107-112.
    • (1970) Cryobiology , vol.7 , pp. 107-112
    • Deal, P.H.1
  • 27
    • 0023781840 scopus 로고
    • Glycine betaine reverses the effects of osmotic stress on DNA replication and cellular division in Escherichia coli
    • J. Meury, Glycine betaine reverses the effects of osmotic stress on DNA replication and cellular division in Escherichia coli, Arch. Microbiol. 149 (1988), pp. 232-239.
    • (1988) Arch. Microbiol. , vol.149 , pp. 232-239
    • Meury, J.1
  • 28
    • 0022427177 scopus 로고
    • Osmotic stress drastically inhibits active transport of carbohydrates by Escherichia coli
    • W.G. Roth, M.P. Leckie, and D.N. Dietzler, Osmotic stress drastically inhibits active transport of carbohydrates by Escherichia coli, Biochem. Biophys. Res. Commun. 126 (1985), pp. 434-441.
    • (1985) Biochem. Biophys. Res. Commun. , vol.126 , pp. 434-441
    • Roth, W.G.1    Leckie, M.P.2    Dietzler, D.N.3
  • 29
    • 0028157327 scopus 로고
    • Glycine betaine confers enhanced osmotolerance and cryotolerance on Listeria monocytogenes
    • R. Ko, L. Tombras Smith, and G.M. Smith, Glycine betaine confers enhanced osmotolerance and cryotolerance on Listeria monocytogenes, J. Bacteriol. 176 (1994), pp. 426-431.
    • (1994) J. Bacteriol. , vol.176 , pp. 426-431
    • Ko, R.1    Tombras Smith, L.2    Smith, G.M.3
  • 30
    • 0033545998 scopus 로고    scopus 로고
    • Genetic engineering of the unsaturation of fatty acids in membrane lipids alters the tolerance of Synechocystis to salt stress
    • S.I. Allakhverdiev, Y. Nishiyama, I. Suzuki, Y. Tasaka, and N. Murata, Genetic engineering of the unsaturation of fatty acids in membrane lipids alters the tolerance of Synechocystis to salt stress, Proc. Nat. Acad. Sci. USA 96 (1999), pp. 5862-5867.
    • (1999) Proc. Nat. Acad. Sci. USA , vol.96 , pp. 5862-5867
    • Allakhverdiev, S.I.1    Nishiyama, Y.2    Suzuki, I.3    Tasaka, Y.4    Murata, N.5
  • 31
    • 0036548759 scopus 로고    scopus 로고
    • Regulation of the desaturation of fatty acids and its role in tolerance to cold and salt stress
    • T. Sakamoto and N. Murata. Regulation of the desaturation of fatty acids and its role in tolerance to cold and salt stress, Curr. Opin. Microbiol. 5 (2002), pp. 206-210.
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 206-210
    • Sakamoto, T.1    Murata, N.2
  • 32
    • 33645996304 scopus 로고    scopus 로고
    • Identification of genes regulated by changing salinity in the deep-sea bacterium Shewanella sp. WP3 using RNA arbitrarily primed PCR
    • S. Li, X. Xiao, J. Li, J. Luo, and F. Wang, Identification of genes regulated by changing salinity in the deep-sea bacterium Shewanella sp. WP3 using RNA arbitrarily primed PCR, Extremophiles 10 (2006), pp. 97-104.
    • (2006) Extremophiles , vol.10 , pp. 97-104
    • Li, S.1    Xiao, X.2    Li, J.3    Luo, J.4    Wang, F.5
  • 33
    • 0036739626 scopus 로고    scopus 로고
    • Comparative analysis of naturally occurring L-amino acid osmolytes and their D-isomers on protection of Escherichia coli against environmental stresses
    • H.M. Shahjee, K. Banerjee, and F. Ahmad, Comparative analysis of naturally occurring L-amino acid osmolytes and their D-isomers on protection of Escherichia coli against environmental stresses, J. Biosci. 27 (2002), pp. 515-520.
    • (2002) J. Biosci. , vol.27 , pp. 515-520
    • Shahjee, H.M.1    Banerjee, K.2    Ahmad, F.3
  • 34
    • 0020336190 scopus 로고
    • Living with water stress: Evolution of osmolyte systems
    • P.H. Yancey, M.E. Clark, S.C. Hand, R.D. Bowlus, and G.N. Somero, Living with water stress: Evolution of osmolyte systems, Science 217 (1982), pp. 1214-1222.
    • (1982) Science , vol.217 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, S.C.3    Bowlus, R.D.4    Somero, G.N.5
  • 35
    • 0034124840 scopus 로고    scopus 로고
    • Cryoprotectants lead to phenotypic adaptation to freeze-thaw stress in Lactobacillus delbrueckii ssp. bulgaricus CIP 101027T
    • J.-M. Panoff, B. Thammavongs, and M. Guéguen, Cryoprotectants lead to phenotypic adaptation to freeze-thaw stress in Lactobacillus delbrueckii ssp. bulgaricus CIP 101027T, Cryobiology 40 (2000), pp. 264-269.
    • (2000) Cryobiology , vol.40 , pp. 264-269
    • Panoff, J.-M.1    Thammavongs, B.2    Guéguen, M.3
  • 36
    • 0023186464 scopus 로고
    • Induction of proteins in response to low temperature in Escherichia coli
    • P.G. Jones, R.A. VanBogelen, and F.C. Neidhardt, Induction of proteins in response to low temperature in Escherichia coli, J. Bacteriol. 169 (1987), pp. 2092-2095.
    • (1987) J. Bacteriol. , vol.169 , pp. 2092-2095
    • Jones, P.G.1    Vanbogelen, R.A.2    Neidhardt, F.C.3
  • 37
    • 0025790144 scopus 로고
    • Identification of a cold shock transcriptional enhancer of the Escherichia coli gene encoding nucleoid protein H-NS
    • A. La Teana, A. Brandi, M. Falconi, R. Spurio, C.L. Pon, and C.O. Gualerzi, Identification of a cold shock transcriptional enhancer of the Escherichia coli gene encoding nucleoid protein H-NS, Proc. Nat. Acad. Sci. USA 88 (1991), pp. 10907-10911.
    • (1991) Proc. Nat. Acad. Sci. USA , vol.88 , pp. 10907-10911
    • La Teana, A.1    Brandi, A.2    Falconi, M.3    Spurio, R.4    Pon, C.L.5    Gualerzi, C.O.6
  • 38
    • 0032860247 scopus 로고    scopus 로고
    • Cold shock response of Bacillus subtilis: Isoleucinedependent switch in the fatty acid branching pattern for membrane adaptation to low temperatures
    • W. Klein, M.H.W. Weber, and M.A. Marahiel, Cold shock response of Bacillus subtilis: Isoleucinedependent switch in the fatty acid branching pattern for membrane adaptation to low temperatures, J. Bacteriol. 181 (1999), pp. 5341-5349.
    • (1999) J. Bacteriol. , vol.181 , pp. 5341-5349
    • Klein, W.1    Weber, M.H.W.2    Marahiel, M.A.3
  • 39
    • 0016774489 scopus 로고
    • The survival of Escherichia coli from freeze-thaw damage: Permeability barrier damage and viability
    • P.H. Calcott and R.A. MacLeod, The survival of Escherichia coli from freeze-thaw damage: Permeability barrier damage and viability, Can. J. Microbiol. 21 (1975), pp. 1724-1732.
    • (1975) Can. J. Microbiol. , vol.21 , pp. 1724-1732
    • Calcott, P.H.1    MacLeod, R.A.2
  • 40
    • 7044282883 scopus 로고    scopus 로고
    • Intracellular glycerol influences resistance to freeze stress in Saccharomyces cerevisiae: Analysis of a quadruple mutant in glycerol dehydrogenase genes and glycerol-enriched cells
    • S. Izawa, M. Sato, K. Yokoigawa, and Y. Inoue, Intracellular glycerol influences resistance to freeze stress in Saccharomyces cerevisiae: Analysis of a quadruple mutant in glycerol dehydrogenase genes and glycerol-enriched cells, Appl. Microbiol. Biotechnol. 66 (2004), pp. 108-114.
    • (2004) Appl. Microbiol. Biotechnol. , vol.66 , pp. 108-114
    • Izawa, S.1    Sato, M.2    Yokoigawa, K.3    Inoue, Y.4
  • 41
    • 0002225921 scopus 로고
    • Physical and chemical basis of injury in single cell microorganisms subjected to freezing and thawing
    • H.T. Meryman, ed., Academic Press, London
    • P. Mazur, Physical and chemical basis of injury in single cell microorganisms subjected to freezing and thawing, in Cryobiology, H.T. Meryman, ed., Academic Press, London, 1966, pp. 213-315.
    • (1966) Cryobiology , pp. 213-315
    • Mazur, P.1
  • 42
    • 0037672413 scopus 로고    scopus 로고
    • Protectants used in the cryopreservation of microorganisms
    • Z. Hubálek, Protectants used in the cryopreservation of microorganisms, Cryobiology 46 (2003), pp. 205-229.
    • (2003) Cryobiology , vol.46 , pp. 205-229
    • Hubálek, Z.1
  • 43
    • 0025959821 scopus 로고
    • Adsorption of α-helical antifreeze peptides on specific ice crystal surface planes
    • C.A. Knight, C.C. Cheng, and A.L. DeVries, Adsorption of α-helical antifreeze peptides on specific ice crystal surface planes, Biophys. J. 59 (1991), pp. 409-418.
    • (1991) Biophys. J. , vol.59 , pp. 409-418
    • Knight, C.A.1    Cheng, C.C.2    Devries, A.L.3
  • 44
    • 0029856558 scopus 로고    scopus 로고
    • Structural basis for the binding of a globular antifreeze protein to ice
    • Z. Jia, C.I. DeLuca, H. Chao, and P.L. Davies, Structural basis for the binding of a globular antifreeze protein to ice, Nature 384 (1996), pp. 285-288.
    • (1996) Nature , vol.384 , pp. 285-288
    • Jia, Z.1    Deluca, C.I.2    Chao, H.3    Davies, P.L.4
  • 46
    • 0002391250 scopus 로고
    • The role of glycoprotein antifreezes in the survival of Antarctic fishes
    • G.A. Llano, ed., Gulf Publishing Company, Houston, TX
    • A.L. DeVries and Y. Lin, The role of glycoprotein antifreezes in the survival of Antarctic fishes, in Adaptations within Antarctic Ecosystems, G.A. Llano, ed., Gulf Publishing Company, Houston, TX, 1977, pp. 439-458.
    • (1977) Adaptations Within Antarctic Ecosystems , pp. 439-458
    • De Vries, A.L.1    Lin, Y.2
  • 47
    • 0002037107 scopus 로고
    • The role of antifreeze glycopeptides and peptides in the freezing avoidance of cold water fishes
    • G. di Prisco, ed., Springer Verlag, Berlin
    • C.C. Cheng and A.L. DeVries, The role of antifreeze glycopeptides and peptides in the freezing avoidance of cold water fishes, in Life under Extreme Conditions, G. di Prisco, ed., Springer Verlag, Berlin, 1991, pp. 1-14.
    • (1991) Life under Extreme Conditions , pp. 1-14
    • Cheng, C.C.1    Devries, A.L.2
  • 48
    • 0035252181 scopus 로고    scopus 로고
    • Thermal hysteresis proteins
    • J. Barrett, Thermal hysteresis proteins, Int. J. Biochem. Cell Biol. 33 (2001), pp. 105-117.
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , pp. 105-117
    • Barrett, J.1
  • 49
    • 0042183228 scopus 로고
    • Adsorption inhibition as a mechanism of freezing resistance in polar fishes
    • J.A. Raymond and A.L. DeVries, Adsorption inhibition as a mechanism of freezing resistance in polar fishes, Proc. Nat. Acad. Sci. USA 74 (1977), pp. 2589-2593.
    • (1977) Proc. Nat. Acad. Sci. USA , vol.74 , pp. 2589-2593
    • Raymond, J.A.1    Devries, A.L.2
  • 50
    • 1642473904 scopus 로고    scopus 로고
    • Demonstration of antifreeze protein activity in Antarctic lake bacteria
    • J.A. Gilbert, P.J. Hill, C.E.R. Dodd, and J. Laybourn- Parry, Demonstration of antifreeze protein activity in Antarctic lake bacteria, Microbiology 150 (2004), pp. 171-180.
    • (2004) Microbiology , vol.150 , pp. 171-180
    • Gilbert, J.A.1    Hill, P.J.2    Dodd, C.E.R.3    Laybourn-Parry, J.4
  • 51
    • 15744400083 scopus 로고    scopus 로고
    • A hyperactive, Ca2+-dependent antifreeze protein in an Antarctic bacterium
    • J.A. Gilbert, P.L. Davies, J. Laybourn-Parry, A hyperactive, Ca2+-dependent antifreeze protein in an Antarctic bacterium, FEMS Microbiol. Lett. 245 (2005), pp. 67-72.
    • (2005) FEMS Microbiol. Lett. , vol.245 , pp. 67-72
    • Gilbert, J.A.1    Davies, P.L.2    Laybourn-Parry, J.3
  • 52
    • 50649119478 scopus 로고    scopus 로고
    • A bacterial ice-binding protein from the Vostok ice core
    • J.A. Raymond, B.C. Christner, and S.C. Schuster, A bacterial ice-binding protein from the Vostok ice core, Extremophiles 12 (2008), pp. 713-717.
    • (2008) Extremophiles , vol.12 , pp. 713-717
    • Raymond, J.A.1    Christner, B.C.2    Schuster, S.C.3
  • 53
    • 34447503551 scopus 로고    scopus 로고
    • An icebinding protein from an Antarctic sea ice bacterium
    • J.A. Raymond, C. Fritsen, and K. Shen, An icebinding protein from an Antarctic sea ice bacterium, FEMS Microbiol. Ecol. 61 (2007), pp. 214-221.
    • (2007) FEMS Microbiol. Ecol. , vol.61 , pp. 214-221
    • Raymond, J.A.1    Fritsen, C.2    Shen, K.3
  • 55
    • 0031980952 scopus 로고    scopus 로고
    • Isolation and characterization of an antifreeze protein with ice nucleation activity from the plant growth promoting rhizobacterium Pseudomonas putida GR12-2
    • H. Xu, M. Griffith, C.L. Patten, and B.R. Glick, Isolation and characterization of an antifreeze protein with ice nucleation activity from the plant growth promoting rhizobacterium Pseudomonas putida GR12-2, Can. J. Microbiol. 44 (1998), pp. 64-73.
    • (1998) Can. J. Microbiol. , vol.44 , pp. 64-73
    • Xu, H.1    Griffith, M.2    Patten, C.L.3    Glick, B.R.4
  • 56
    • 34247108684 scopus 로고    scopus 로고
    • A novel, intracellular antifreeze protein in an antarctic bacterium, Flavobacterium xanthum
    • H. Kawahara, Y. Iwanaka, S. Higa, N. Muryoi, M. Sato, M. Honda, H. Omura, and H. Obata, A novel, intracellular antifreeze protein in an antarctic bacterium, Flavobacterium xanthum, Cryo Lett. 28 (2007), pp. 39-49.
    • (2007) Cryo Lett. , vol.28 , pp. 39-49
    • Kawahara, H.1    Iwanaka, Y.2    Higa, S.3    Muryoi, N.4    Sato, M.5    Honda, M.6    Omura, H.7    Obata, H.8
  • 57
    • 0000078585 scopus 로고
    • Thermal hysteresis protein activity in bacteria fungi, and phylogenetically diverse plants
    • J.G. Duman and T.M. Olsen, Thermal hysteresis protein activity in bacteria, fungi, and phylogenetically diverse plants, Cryobiology 30 (1993), pp. 322-328.
    • (1993) Cryobiology , vol.30 , pp. 322-328
    • Duman, J.G.1    Olsen, T.M.2
  • 58
    • 33748308729 scopus 로고    scopus 로고
    • Ice-active characteristics of soil bacteria selected by ice-affinity
    • S.L. Wilson, D.L. Kelley, and V.K. Walker, Ice-active characteristics of soil bacteria selected by ice-affinity, Environ. Microbiol. 8 (2006), pp. 1816-1824.
    • (2006) Environ. Microbiol. , vol.8 , pp. 1816-1824
    • Wilson, S.L.1    Kelley, D.L.2    Walker, V.K.3
  • 59
    • 0001376901 scopus 로고
    • The use of thermal analysis in the development of a better understanding of frozen food stability
    • H.D. Goff, The use of thermal analysis in the development of a better understanding of frozen food stability, Pure Appl. Chem. 67 (1995), pp. 1801-1808.
    • (1995) Pure Appl. Chem. , vol.67 , pp. 1801-1808
    • Goff, H.D.1
  • 60
    • 0000980394 scopus 로고
    • Atmospheric ice nuclei from decomposing vegetation
    • R.C. Schnell and G. Vali, Atmospheric ice nuclei from decomposing vegetation, Nature 236 (1972), pp. 163-165.
    • (1972) Nature , vol.236 , pp. 163-165
    • Schnell, R.C.1    Vali, G.2
  • 62
    • 0033848415 scopus 로고    scopus 로고
    • Ice crystallization by Pseudomonas syringae
    • N. Cochet and P. Widehem, Ice crystallization by Pseudomonas syringae, Appl. Microbiol. Biotechnol. 54 (2000), pp. 153-161.
    • (2000) Appl. Microbiol. Biotechnol. , vol.54 , pp. 153-161
    • Cochet, N.1    Widehem, P.2
  • 63
    • 0017159805 scopus 로고
    • Nucleating agents in the haemolymph of insects tolerant to freezing
    • K.E. Zachariassen and H.T. Hammel, Nucleating agents in the haemolymph of insects tolerant to freezing, Nature 262 (1976), pp. 285-287.
    • (1976) Nature , vol.262 , pp. 285-287
    • Zachariassen, K.E.1    Hammel, H.T.2
  • 64
    • 0037193988 scopus 로고    scopus 로고
    • Physiological and ecological significance of biological ice nucleators
    • R. Lundheim, Physiological and ecological significance of biological ice nucleators, Philos. Trans. R. Soc. Lond. B. 357 (2002), pp. 937-943.
    • (2002) Philos. Trans. R. Soc. Lond. B. , vol.357 , pp. 937-943
    • Lundheim, R.1
  • 65
    • 0023056237 scopus 로고
    • Conserved repeats in diverged ice nucleation structural genes from two species of Pseudomonas
    • G. Warren, L. Corotto, and P. Wolber, Conserved repeats in diverged ice nucleation structural genes from two species of Pseudomonas, Nucleic Acids Res. 14 (1986), pp. 8047-8060.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 8047-8060
    • Warren, G.1    Corotto, L.2    Wolber, P.3
  • 66
    • 0000687463 scopus 로고
    • Size of bacterial ice-nucleation sites measured in situ by radiation inactivation analysis
    • A.G. Govindarajan and S.E. Lindow, Size of bacterial ice-nucleation sites measured in situ by radiation inactivation analysis, Proc. Natl Acad. Sci. USA 85 (1988), pp. 1334-1338.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 1334-1338
    • Govindarajan, A.G.1    Lindow, S.E.2
  • 67
    • 0026293775 scopus 로고
    • Principles and biotechnological applications of bacterial ice nucleation
    • A. Margaritis and A.S. Bassi, Principles and biotechnological applications of bacterial ice nucleation, Crit. Rev. Biotechnol. 11 (1991), pp. 277-295.
    • (1991) Crit. Rev. Biotechnol. , vol.11 , pp. 277-295
    • Margaritis, A.1    Bassi, A.S.2
  • 69
    • 0000853923 scopus 로고
    • Relationship between ice nucleation frequency of bacteria and frost injury
    • S.E. Lindow, S.S. Hirano, W.R. Barchet, D.C. Arny, and C.D. Upper, Relationship between ice nucleation frequency of bacteria and frost injury, Plant Physiol. 70 (1982), pp. 1090-1093.
    • (1982) Plant Physiol. , vol.70 , pp. 1090-1093
    • Lindow, S.E.1    Hirano, S.S.2    Barchet, W.R.3    Arny, D.C.4    Upper, C.D.5
  • 70
    • 0021709719 scopus 로고
    • Phosphatidylinositol as a component of the ice nucleating site of Pseudomonas syringae and Erwinia herbicola
    • L.M. Kozloff, M. Lute, and D. Westaway, Phosphatidylinositol as a component of the ice nucleating site of Pseudomonas syringae and Erwinia herbicola, Science 226 (1984), pp. 845-846.
    • (1984) Science , vol.226 , pp. 845-846
    • Kozloff, L.M.1    Lute, M.2    Westaway, D.3
  • 71
    • 0024377099 scopus 로고
    • An ice nucleation active gene of Erwinia ananas Sequence similarity to those of Pseudomonas species and regions required for ice nucleation activity
    • K. Abe, S. Watabe, Y. Emori, M. Watanabe, and S. Arai, An ice nucleation active gene of Erwinia ananas Sequence similarity to those of Pseudomonas species and regions required for ice nucleation activity, FEBS Lett. 258 (1989), pp. 297-300.
    • (1989) FEBS Lett. , vol.258 , pp. 297-300
    • Abe, K.1    Watabe, S.2    Emori, Y.3    Watanabe, M.4    Arai, S.5
  • 72
    • 0001599079 scopus 로고
    • Erwinia herbicola: A bacterial ice nucleus active in increasing frost injury to corn
    • S.E. Lindow, D.C. Arny, and C.D. Upper, Erwinia herbicola: A bacterial ice nucleus active in increasing frost injury to corn, Phytopathology 68 (1978), pp. 523-527.
    • (1978) Phytopathology , vol.68 , pp. 523-527
    • Lindow, S.E.1    Arny, D.C.2    Upper, C.D.3
  • 73
    • 0032765594 scopus 로고    scopus 로고
    • Identification of a novel ice-nucleating bacterium of Antarctic origin and its ice nucleation properties
    • H. Obata, N. Muryoi, H. Kawahara, K. Yamade, and J. Nishikawa, Identification of a novel ice-nucleating bacterium of Antarctic origin and its ice nucleation properties, Cryobiology 38 (1999), pp. 131-139.
    • (1999) Cryobiology , vol.38 , pp. 131-139
    • Obata, H.1    Muryoi, N.2    Kawahara, H.3    Yamade, K.4    Nishikawa, J.5
  • 74
    • 2842589358 scopus 로고    scopus 로고
    • Properties of a novel extracellular cell-free ice nuclei from icenucleating Pseudomonas antarctica IN-74
    • N. Muryoi, H. Kawahara, and H. Obata, Properties of a novel extracellular cell-free ice nuclei from icenucleating Pseudomonas antarctica IN-74, Biosci. Biotechnol. Biochem. 67 (2003), pp. 1950-1958.
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 1950-1958
    • Muryoi, N.1    Kawahara, H.2    Obata, H.3
  • 75
    • 65649096907 scopus 로고    scopus 로고
    • Characterization and recombinant expression of a divergent ice nucleation protein from 'Pseudomonas borealis'
    • Z. Wu, L. Qin, and V.K. Walker, Characterization and recombinant expression of a divergent ice nucleation protein from 'Pseudomonas borealis', Microbiology 155 (2009), pp. 1164-1169.
    • (2009) Microbiology , vol.155 , pp. 1164-1169
    • Wu, Z.1    Qin, L.2    Walker, V.K.3
  • 76
    • 0022666697 scopus 로고
    • Ice nucleation activity of Pseudomonas fluorescens: Mutagenesis, complementation analysis and identification of a gene product
    • L.V. Corotto, P.K. Wolber, and G.J. Warren, Ice nucleation activity of Pseudomonas fluorescens: Mutagenesis, complementation analysis and identification of a gene product, EMBO J. 5 (1986), pp. 231-236.
    • (1986) EMBO J. , vol.5 , pp. 231-236
    • Corotto, L.V.1    Wolber, P.K.2    Warren, G.J.3
  • 77
    • 0022365375 scopus 로고
    • Physical and functional repetition in a bacterial ice nucleation gene
    • R.L. Green and G.J. Warren, Physical and functional repetition in a bacterial ice nucleation gene, Nature 317 (1985), pp. 645-648.
    • (1985) Nature , vol.317 , pp. 645-648
    • Green, R.L.1    Warren, G.J.2
  • 78
    • 0001094058 scopus 로고
    • Identification of an ice-nucleating bacterium and its ice nucleation properties
    • H. Obata, T. Nakai, J. Tanishita, and T. Tokuyama, Identification of an ice-nucleating bacterium and its ice nucleation properties, J. Ferment. Bioeng. 67 (1989), pp. 143-147.
    • (1989) J. Ferment. Bioeng. , vol.67 , pp. 143-147
    • Obata, H.1    Nakai, T.2    Tanishita, J.3    Tokuyama, T.4
  • 79
    • 0025096026 scopus 로고
    • Cloning of bacterial ice nucleation genes of Pseudomonas viridiflava in Escherichia coli
    • Y. Hasegawa, N. Sakai, H. Yoshitome, S. Kawate, H. Obata, and T. Tokuyama, Cloning of bacterial ice nucleation genes of Pseudomonas viridiflava in Escherichia coli, J. Ferment. Bioeng. 70 (1990), pp. 143-146.
    • (1990) J. Ferment. Bioeng. , vol.70 , pp. 143-146
    • Hasegawa, Y.1    Sakai, N.2    Yoshitome, H.3    Kawate, S.4    Obata, H.5    Tokuyama, T.6
  • 80
    • 0024995479 scopus 로고
    • Conserved repetition in the ice nucleation gene inaX from Xanthomonas camperstris pv. translucens
    • J.-L. Zhao and C.S. Orser, Conserved repetition in the ice nucleation gene inaX from Xanthomonas camperstris pv. translucens, Mol. Gen. Genet. 223 (1990), pp. 163-166.
    • (1990) Mol. Gen. Genet. , vol.223 , pp. 163-166
    • Zhao, J.-L.1    Orser, C.S.2
  • 81
    • 11144318597 scopus 로고    scopus 로고
    • Pathogenic ice-nucleation active bacteria in willows for short rotation forestry
    • P. Nejad, M. Ramstedt, and U. Granhall, Pathogenic ice-nucleation active bacteria in willows for short rotation forestry, For. Pathol. 34 (2004), pp. 369-381.
    • (2004) For. Pathol. , vol.34 , pp. 369-381
    • Nejad, P.1    Ramstedt, M.2    Granhall, U.3
  • 82
    • 33751506714 scopus 로고    scopus 로고
    • Presence of quorumsensing- mediated gene regulation in pathogenic icenucleation- active (INA) bacteria
    • P. Nejad and M. Ramstedt, Presence of quorumsensing- mediated gene regulation in pathogenic icenucleation- active (INA) bacteria, World J. Microbiol. Biotechnol. 22 (2006), pp. 1373-1375.
    • (2006) World J. Microbiol. Biotechnol. , vol.22 , pp. 1373-1375
    • Nejad, P.1    Ramstedt, M.2
  • 84
    • 0242521447 scopus 로고    scopus 로고
    • A facile method for determining ice recrystallization inhibition by antifreeze proteins
    • M.M. Tomczak, C.B. Marshall, J.A. Gilbert, and P.L. Davies, A facile method for determining ice recrystallization inhibition by antifreeze proteins, Biochem. Biophys. Res. Commun. 311 (2003), pp. 1041-1046.
    • (2003) Biochem. Biophys. Res. Commun. , vol.311 , pp. 1041-1046
    • Tomczak, M.M.1    Marshall, C.B.2    Gilbert, J.A.3    Davies, P.L.4
  • 85
    • 0026331935 scopus 로고
    • The effect of enhanced α-helicity on the activity of a winter flounder antifreeze polypeptide
    • A. Chakrabartty and C.L. Hew, The effect of enhanced α-helicity on the activity of a winter flounder antifreeze polypeptide, Eur. J. Biochem. 202 (1991), pp. 1057-1063.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1057-1063
    • Chakrabartty, A.1    Hew, C.L.2
  • 86
    • 77949370657 scopus 로고    scopus 로고
    • Towards a green hydrate inhibitor: Imaging antifreeze proteins on clathrates
    • R. Gordienko, H. Ohno, V. Singh, Z. Jia, J. Ripmeester, and V.K. Walker, Towards a green hydrate inhibitor: Imaging antifreeze proteins on clathrates, PLoS ONE 5 (2010), pp. e8953.
    • (2010) PLoS ONE , vol.5
    • Gordienko, R.1    Ohno, H.2    Singh, V.3    Jia, Z.4    Ripmeester, J.5    Walker, V.K.6
  • 87
    • 0001278148 scopus 로고
    • Quantitative evaluation of experimental results on the heterogeneous freezing nucleation of supercooled liquids
    • G. Vali, Quantitative evaluation of experimental results on the heterogeneous freezing nucleation of supercooled liquids, J. Atmos. Sci. 28 (1971), pp. 402-409.
    • (1971) J. Atmos. Sci. , vol.28 , pp. 402-409
    • Vali, G.1
  • 88
    • 33751004137 scopus 로고    scopus 로고
    • Examination of the watershed-wide distribution of Escherichia coli along southern Lake Michigan: An integrated approach
    • R.L. Whitman, M.B. Nevers, and M.N. Byappanahalli, Examination of the watershed-wide distribution of Escherichia coli along southern Lake Michigan: An integrated approach, Appl. Environ. Microbiol. 72 (2006), pp. 7301-7310.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 7301-7310
    • Whitman, R.L.1    Nevers, M.B.2    Byappanahalli, M.N.3
  • 89
    • 0026762659 scopus 로고
    • Dual staining of natural bacterioplankton with 4',6-diamidino- 2-phenylindole and fluorescent oligonucleotide probes targeting kingdom-level 16S rRNA sequences
    • R.E. Hicks, R.I. Amann, and D.A. Stahl, Dual staining of natural bacterioplankton with 4',6-diamidino- 2-phenylindole and fluorescent oligonucleotide probes targeting kingdom-level 16S rRNA sequences, Appl. Environ. Microbiol. 58 (1992), pp. 2158-2163.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2158-2163
    • Hicks, R.E.1    Amann, R.I.2    Stahl, D.A.3
  • 96
    • 0030615223 scopus 로고    scopus 로고
    • Effect of antifreeze proteins on frozen primary prostatic adenocarcinoma cells
    • H. Koushafar and B. Rubinsky, Effect of antifreeze proteins on frozen primary prostatic adenocarcinoma cells, Urology 49 (1997), pp. 421-425.
    • (1997) Urology , vol.49 , pp. 421-425
    • Koushafar, H.1    Rubinsky, B.2
  • 97
    • 0031811192 scopus 로고    scopus 로고
    • Antifreeze proteins: Current status and possible food uses
    • R.E. Feeney and Y. Yeh, Antifreeze proteins: Current status and possible food uses, Trends Food Sci. Technol. 9 (1998), pp. 102-106.
    • (1998) Trends Food Sci. Technol. , vol.9 , pp. 102-106
    • Feeney, R.E.1    Yeh, Y.2
  • 98
    • 36749097294 scopus 로고    scopus 로고
    • Improvement of texture properties and flavor of frozen dough by carrot (Daucus carota) antifreeze protein supplementation
    • C. Zhang, H. Zhang, L. Wang, H. Gao, X.N. Guo, and H.Y. Yao, Improvement of texture properties and flavor of frozen dough by carrot (Daucus carota) antifreeze protein supplementation, J. Agric. Food Chem. 55 (2007), pp. 9620-9626.
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 9620-9626
    • Zhang, C.1    Zhang, H.2    Wang, L.3    Gao, H.4    Guo, X.N.5    Yao, H.Y.6
  • 99
    • 0027435104 scopus 로고
    • Cryogenic protection of oocytes with antifreeze proteins
    • A. Arav, B. Rubinsky, G. Fletcher, and E. Seren, Cryogenic protection of oocytes with antifreeze proteins, Mol. Reprod. Dev. 36 (1993), pp. 488-493.
    • (1993) Mol. Reprod. Dev. , vol.36 , pp. 488-493
    • Arav, A.1    Rubinsky, B.2    Fletcher, G.3    Seren, E.4
  • 100
    • 40049100152 scopus 로고    scopus 로고
    • Cryogenic effect of antifreeze protein on transgenic mouse ovaries and the production of live offspring by orthotopic transplantation of cryopreserved mouse ovaries
    • H. Bagis, T. Akkoç, A. Tas , and D. Aktoprakligil, Cryogenic effect of antifreeze protein on transgenic mouse ovaries and the production of live offspring by orthotopic transplantation of cryopreserved mouse ovaries, Mol. Reprod. Dev. 75 (2008), pp. 608-613.
    • (2008) Mol. Reprod. Dev. , vol.75 , pp. 608-613
    • Bagis, H.1    Akkoç, T.2    Tas, A.3    Aktoprakligil, D.4
  • 101
    • 33644943994 scopus 로고    scopus 로고
    • Effect of antifreeze proteins on the nucleation, growth, and the memory effect during tetrahydrofuran clathrate hydrate formation
    • H. Zeng, L.D. Wilson, V.K. Walker, and J.A. Ripmeester, Effect of antifreeze proteins on the nucleation, growth, and the memory effect during tetrahydrofuran clathrate hydrate formation, J. Amer. Chem. Soc. 128 (2006), pp. 2844-2850.
    • (2006) J. Amer. Chem. Soc. , vol.128 , pp. 2844-2850
    • Zeng, H.1    Wilson, L.D.2    Walker, V.K.3    Ripmeester, J.A.4
  • 102
    • 0024926975 scopus 로고    scopus 로고
    • Concentration effects of ice nucleation active bacteria on the water nucleation temperature
    • D.Y. Goswami, ed., American Society of Mechanical Engineers, New York
    • W.E. Stewert Jr. and L.L. Bear, Concentration effects of ice nucleation active bacteria on the water nucleation temperature, in Proceedings of the 23rd Intersociety Energy Conversion Engineering Conference, Vol.2., D.Y. Goswami, ed., American Society of Mechanical Engineers, New York, 1998, pp. 147-149.
    • (1998) Proceedings of the 23rd Intersociety Energy Conversion Engineering Conference , vol.2 , pp. 147-149
    • Stewert Jr., W.E.1    Bear, L.L.2
  • 103
    • 0442329211 scopus 로고    scopus 로고
    • Effect of freeze-thaw repetitions upon the supercooling release ability of ice-nucleating bacteria
    • Y. Tsuchiya, K. Sasaki, and H. Hasegawa, Effect of freeze-thaw repetitions upon the supercooling release ability of ice-nucleating bacteria, J. Biosci. Bioeng. 97 (2004), pp. 71-74.
    • (2004) J. Biosci. Bioeng. , vol.97 , pp. 71-74
    • Tsuchiya, Y.1    Sasaki, K.2    Hasegawa, H.3
  • 105
    • 4143076043 scopus 로고    scopus 로고
    • Upregulation and protein trafficking of Aquaporin-2 attenuate cold-induced osmotic damage during cryopreservation
    • W. Wang and R.N. Ben, Upregulation and protein trafficking of Aquaporin-2 attenuate cold-induced osmotic damage during cryopreservation, In Vitro Cell. Dev. Biol. - Anim. 40 (2004), pp. 67-70.
    • (2004) Vitro Cell. Dev. Biol. - Anim. , vol.40 , pp. 67-70
    • Wang, W.1    Ben, R.N.2
  • 106
    • 6544290514 scopus 로고    scopus 로고
    • Metabolic engineering of rice leading to biosynthesis of glycinebetaine and tolerance to salt and cold
    • A. Sakamoto, A. Murata, and N. Murata, Metabolic engineering of rice leading to biosynthesis of glycinebetaine and tolerance to salt and cold, Plant Mol. Biol. 38 (1998), pp. 1011-1019.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 1011-1019
    • Sakamoto, A.1    Murata, A.2    Murata, N.3
  • 107
    • 0141815742 scopus 로고    scopus 로고
    • Osmotolerance and leavening ability in sweet and frozen sweet dough. Comparative analysis between Torulaspora delbrueckii and Saccharomyces cerevisiae baker's yeast strains
    • M.J. Hernandez-Lopez, J.A. Prieto, and F. Randez-Gil, Osmotolerance and leavening ability in sweet and frozen sweet dough. Comparative analysis between Torulaspora delbrueckii and Saccharomyces cerevisiae baker's yeast strains, Antonie van Leeuwenhoek 84 (2003), pp. 125-134.
    • (2003) Antonie Van Leeuwenhoek , vol.84 , pp. 125-134
    • Hernandez-Lopez, M.J.1    Prieto, J.A.2    Randez-Gil, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.