메뉴 건너뛰기




Volumn 37, Issue 10, 2014, Pages 1495-1505

Molecular cloning, expression and characterisation of Afp4, an antifreeze protein from Glaciozyma antarctica

Author keywords

Heterologous protein expression; Homology modelling; Inhibition of recrystallisation; Thermal hysteresis

Indexed keywords

CLONE; DNA; FILTRATION; GENE EXPRESSION; GROWTH RATE; HOMOLOGY; HYDROPHOBICITY; PROTEIN; RECRYSTALLIZATION; SURVIVORSHIP; YEAST;

EID: 84907883232     PISSN: 07224060     EISSN: 14322056     Source Type: Journal    
DOI: 10.1007/s00300-014-1539-1     Document Type: Article
Times cited : (25)

References (52)
  • 1
    • 17844392864 scopus 로고    scopus 로고
    • Combining prediction of secondary structure and solvent accessibility in proteins
    • Adamczak R, Porollo A, Meller J (2005) Combining prediction of secondary structure and solvent accessibility in proteins. Proteins Struct Funct Bioinform 59:467–475
    • (2005) Proteins Struct Funct Bioinform , vol.59 , pp. 467-475
    • Adamczak, R.1    Porollo, A.2    Meller, J.3
  • 3
    • 0041621597 scopus 로고    scopus 로고
    • Preservation of myocyte structure and mitochondrial integrity in subzero cryopreservation of mammalian hearts for transplantation using antifreeze proteins: an electron microscopy study
    • PID: 12895622
    • Amir G, Rubinsky B, Kassif Y, Horowitz L, Smolinsky AK, Lavee J (2003) Preservation of myocyte structure and mitochondrial integrity in subzero cryopreservation of mammalian hearts for transplantation using antifreeze proteins: an electron microscopy study. Eur J Cardiothorac Surg 24:292–297
    • (2003) Eur J Cardiothorac Surg , vol.24 , pp. 292-297
    • Amir, G.1    Rubinsky, B.2    Kassif, Y.3    Horowitz, L.4    Smolinsky, A.K.5    Lavee, J.6
  • 4
    • 0035252181 scopus 로고    scopus 로고
    • Thermal hysteresis proteins
    • PID: 11240367, COI: 1:CAS:528:DC%2BD3MXhs1emt7c%3D
    • Barrett J (2001) Thermal hysteresis proteins. Int J Biochem Cell Biol 33:105–117
    • (2001) Int J Biochem Cell Biol , vol.33 , pp. 105-117
    • Barrett, J.1
  • 5
    • 77954634710 scopus 로고    scopus 로고
    • Antifreeze proteins in polar sea ice diatoms: diversity and gene expression in the genus Fragilariopsis
    • PID: 20105220, COI: 1:CAS:528:DC%2BC3cXmtFCrs7c%3D
    • Bayer-Giraldi M, Uhlig C, John U, Mock T, Valentin K (2010) Antifreeze proteins in polar sea ice diatoms: diversity and gene expression in the genus Fragilariopsis. Environ Microbiol 12:1041–1052
    • (2010) Environ Microbiol , vol.12 , pp. 1041-1052
    • Bayer-Giraldi, M.1    Uhlig, C.2    John, U.3    Mock, T.4    Valentin, K.5
  • 6
    • 33747856166 scopus 로고    scopus 로고
    • The MPI bioinformatics toolkit for protein sequence analysis
    • PID: 16845021, COI: 1:CAS:528:DC%2BD28Xps1yhsrY%3D
    • Biegert A, Mayer C, Remmert M, Söding J, Lupas AN (2006) The MPI bioinformatics toolkit for protein sequence analysis. Nucleic Acids Res 34:W335–W339
    • (2006) Nucleic Acids Res , vol.34 , pp. W335-W339
    • Biegert, A.1    Mayer, C.2    Remmert, M.3    Söding, J.4    Lupas, A.N.5
  • 7
    • 84873994571 scopus 로고    scopus 로고
    • Thermal stress responses in Antarctic yeast, Glaciozyma antarctica PI12, characterized by real-time quantitative PCR
    • Boo S, Wong C, Rodrigues K, Najimudin N, Murad A, Mahadi N (2013) Thermal stress responses in Antarctic yeast, Glaciozyma antarctica PI12, characterized by real-time quantitative PCR. Polar Biol 36:381–389
    • (2013) Polar Biol , vol.36 , pp. 381-389
    • Boo, S.1    Wong, C.2    Rodrigues, K.3    Najimudin, N.4    Murad, A.5    Mahadi, N.6
  • 8
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • PID: 1853201, COI: 1:CAS:528:DyaK3MXltV2qsbk%3D
    • Bowie J, Luthy R, Eisenberg D (1991) A method to identify protein sequences that fold into a known three-dimensional structure. Science 253:164–170
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.1    Luthy, R.2    Eisenberg, D.3
  • 9
    • 17144365873 scopus 로고    scopus 로고
    • Characterization of antifreeze activity in Antarctic plants
    • PID: 15723822, COI: 1:CAS:528:DC%2BD2MXisVGqs7k%3D
    • Bravo LA, Griffith M (2005) Characterization of antifreeze activity in Antarctic plants. J Exp Bot 56:1189–1196
    • (2005) J Exp Bot , vol.56 , pp. 1189-1196
    • Bravo, L.A.1    Griffith, M.2
  • 10
    • 74149089142 scopus 로고    scopus 로고
    • Bioprospecting for microbial products that affect ice crystal formation and growth
    • PID: 19841917, COI: 1:CAS:528:DC%2BC3cXit1yhsw%3D%3D
    • Christner B (2010) Bioprospecting for microbial products that affect ice crystal formation and growth. Appl Microbiol Biotechnol 85:481–489
    • (2010) Appl Microbiol Biotechnol , vol.85 , pp. 481-489
    • Christner, B.1
  • 11
    • 0027180507 scopus 로고
    • Verification of protein structures: patterns of nonbonded atomic interactions
    • PID: 8401235, COI: 1:CAS:528:DyaK2cXhvVKltbk%3D
    • Colovos C, Yeates TO (1993) Verification of protein structures: patterns of nonbonded atomic interactions. Protein Sci 2:1511–1519
    • (1993) Protein Sci , vol.2 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 13
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • PID: 15034147, COI: 1:CAS:528:DC%2BD2cXisF2ks7w%3D
    • Edgar RC (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32:1792–1797
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 15
    • 0029901637 scopus 로고    scopus 로고
    • Inferring phylogenies from protein sequences by parsimony, distance, and likelihood methods
    • Felsenstein J (1996) Inferring phylogenies from protein sequences by parsimony, distance, and likelihood methods. In: Russell FD (ed) Methods in enzymology. Academic Press, pp 418–27
    • (1996) Methods in enzymology. Academic Press , pp. 418-427
    • Felsenstein, J.1    Russell, F.D.2
  • 16
    • 0035050777 scopus 로고    scopus 로고
    • Antifreeze proteins of teleost fishes
    • PID: 11181960, COI: 1:CAS:528:DC%2BD3MXjtFKmtLY%3D
    • Fletcher GL, Hew CL, Davies PL (2001) Antifreeze proteins of teleost fishes. Annu Rev Physiol 63:359–390
    • (2001) Annu Rev Physiol , vol.63 , pp. 359-390
    • Fletcher, G.L.1    Hew, C.L.2    Davies, P.L.3
  • 18
    • 79956332670 scopus 로고    scopus 로고
    • Anchored clathrate waters bind antifreeze proteins to ice
    • PID: 21482800, COI: 1:CAS:528:DC%2BC3MXmtFSrsrY%3D
    • Garnham CP, Campbell RL, Davies PL (2011) Anchored clathrate waters bind antifreeze proteins to ice. Proc Natl Acad Sci USA 108:7363–7367
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 7363-7367
    • Garnham, C.P.1    Campbell, R.L.2    Davies, P.L.3
  • 20
    • 0034691594 scopus 로고    scopus 로고
    • Beta-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect
    • PID: 10917537, COI: 1:STN:280:DC%2BD3czovVOisg%3D%3D
    • Graether SP, Kuiper MJ, Gagné SM, Walker VK, Jia Z, Sykes BD, Davies PL (2000) Beta-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect. Nature 406:325–328
    • (2000) 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
  • 21
    • 0028835687 scopus 로고
    • Antifreeze proteins and their potential use in frozen foods
    • PID: 14536093, COI: 1:CAS:528:DyaK2MXpslSlsb4%3D
    • Griffith M, Ewart KV (1995) Antifreeze proteins and their potential use in frozen foods. Biotechnol Adv 13:375–402
    • (1995) Biotechnol Adv , vol.13 , pp. 375-402
    • Griffith, M.1    Ewart, K.V.2
  • 22
    • 4344568284 scopus 로고    scopus 로고
    • Antifreeze proteins in overwintering plants: a tale of two activities
    • PID: 15358271, COI: 1:CAS:528:DC%2BD2cXmsVCqtbs%3D
    • Griffith M, Yaish MWF (2004) Antifreeze proteins in overwintering plants: a tale of two activities. Trends Plant Sci 9:399–405
    • (2004) Trends Plant Sci , vol.9 , pp. 399-405
    • Griffith, M.1    Yaish, M.W.F.2
  • 25
    • 0036470053 scopus 로고    scopus 로고
    • Antifreeze proteins: an unusual receptor–ligand interaction
    • PID: 11852248, COI: 1:CAS:528:DC%2BD38XhtlGjur4%3D
    • Jia Z, Davies PL (2002) Antifreeze proteins: an unusual receptor–ligand interaction. Trends Biochem Sci 27:101–106
    • (2002) Trends Biochem Sci , vol.27 , pp. 101-106
    • Jia, Z.1    Davies, P.L.2
  • 26
    • 34247108684 scopus 로고    scopus 로고
    • A novel, intracellular antifreeze protein in an antarctic bacterium, Flavobacterium xanthum
    • PID: 17369961, COI: 1:CAS:528:DC%2BD2sXkvVOnu70%3D
    • Kawahara H, Iwanaka Y, Higa S, Muryoi N, Sato M, Honda M, Omura H, Obata H (2007) A novel, intracellular antifreeze protein in an antarctic bacterium, Flavobacterium xanthum. Cryoletters 28:39–49
    • (2007) Cryoletters , 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
  • 27
    • 84930337649 scopus 로고    scopus 로고
    • Production of antifreeze proteins by cold-adapted yeasts
    • Buzzini P, Margesin R, (eds), Springer, Heidelberg:
    • Kim H, Lee J, Do H, Jung W (2014) Production of antifreeze proteins by cold-adapted yeasts. In: Buzzini P, Margesin R (eds) Cold-adapted yeasts. Springer, Heidelberg, pp 259–280
    • (2014) Cold-adapted yeasts , pp. 259-280
    • Kim, H.1    Lee, J.2    Do, H.3    Jung, W.4
  • 28
    • 0027396926 scopus 로고
    • Adsorption to ice of fish antifreeze glycopeptides 7 and 8
    • PID: 8431545, COI: 1:CAS:528:DyaK3sXhs1emtrc%3D
    • Knight CA, Driggers E, DeVries AL (1993) Adsorption to ice of fish antifreeze glycopeptides 7 and 8. Biophys J 64:252–259
    • (1993) Biophys J , vol.64 , pp. 252-259
    • Knight, C.A.1    Driggers, E.2    DeVries, A.L.3
  • 29
    • 84862182041 scopus 로고    scopus 로고
    • Ice-binding site of snow mold fungus antifreeze protein deviates from structural regularity and high conservation
    • PID: 22645341, COI: 1:CAS:528:DC%2BC38Xptlaiurg%3D
    • Kondo H, Hanada Y, Sugimoto H, Hoshino T, Garnham CP, Davies PL, Tsuda S (2012) Ice-binding site of snow mold fungus antifreeze protein deviates from structural regularity and high conservation. Proc Natl Acad Sci USA 109:9360–9365
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 9360-9365
    • Kondo, H.1    Hanada, Y.2    Sugimoto, H.3    Hoshino, T.4    Garnham, C.P.5    Davies, P.L.6    Tsuda, S.7
  • 30
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • COI: 1:CAS:528:DyaK3sXit12lurY%3D
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26:283–291
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 31
    • 77349110662 scopus 로고    scopus 로고
    • An extracellular ice-binding glycoprotein from an Arctic psychrophilic yeast
    • PID: 20067781, COI: 1:CAS:528:DC%2BC3cXivFemtL0%3D
    • Lee JK, Park KS, Park S, Park H, Song YH, Kang S-H, Kim HJ (2010) An extracellular ice-binding glycoprotein from an Arctic psychrophilic yeast. Cryobiology 60:222–228
    • (2010) Cryobiology , vol.60 , pp. 222-228
    • Lee, J.K.1    Park, K.S.2    Park, S.3    Park, H.4    Song, Y.H.5    Kang, S.-H.6    Kim, H.J.7
  • 32
    • 84859508078 scopus 로고    scopus 로고
    • Structural basis for antifreeze activity of ice-binding protein from Arctic yeast
    • PID: 22303017, COI: 1:CAS:528:DC%2BC38XkvVWltL0%3D
    • Lee JH, Park AK, Do H, Park KS, Moh SH, Chi YM, Kim HJ (2012) Structural basis for antifreeze activity of ice-binding protein from Arctic yeast. J Biol Chem 287:11460–11468
    • (2012) J Biol Chem , vol.287 , pp. 11460-11468
    • Lee, J.H.1    Park, A.K.2    Do, H.3    Park, K.S.4    Moh, S.H.5    Chi, Y.M.6    Kim, H.J.7
  • 33
    • 35648999092 scopus 로고    scopus 로고
    • Fold assessment for comparative protein structure modeling
    • PID: 17905832, COI: 1:CAS:528:DC%2BD2sXht1ygu7jJ
    • Melo F, Sali A (2007) Fold assessment for comparative protein structure modeling. Protein Sci 16:2412–2426
    • (2007) Protein Sci , vol.16 , pp. 2412-2426
    • Melo, F.1    Sali, A.2
  • 34
    • 4344665035 scopus 로고    scopus 로고
    • Cloning and expression of afpA, a gene encoding an antifreeze protein from the arctic plant growth-promoting rhizobacterium Pseudomonas putida GR12-2
    • PID: 15317770, COI: 1:CAS:528:DC%2BD2cXntlCmt70%3D
    • Muryoi N, Sato M, Kaneko S, Kawahara H, Obata H, Yaish MWF, Griffith M, Glick BR (2004) Cloning and expression of afpA, a gene encoding an antifreeze protein from the arctic plant growth-promoting rhizobacterium Pseudomonas putida GR12-2. J Bacteriol 186:5661–5671
    • (2004) J Bacteriol , vol.186 , pp. 5661-5671
    • Muryoi, N.1    Sato, M.2    Kaneko, S.3    Kawahara, H.4    Obata, H.5    Yaish, M.W.F.6    Griffith, M.7    Glick, B.R.8
  • 35
    • 84862807174 scopus 로고    scopus 로고
    • Characterization of the ice-binding protein from Arctic yeast Leucosporidium sp. AY30
    • PID: 22426061, COI: 1:CAS:528:DC%2BC38Xks12jur8%3D
    • Park KS, Do H, Lee JH, Park SI, Kim EJ, Kim S-J, Kang S-H, Kim HJ (2012) Characterization of the ice-binding protein from Arctic yeast Leucosporidium sp. AY30. Cryobiology 64:286–296
    • (2012) Cryobiology , vol.64 , pp. 286-296
    • Park, K.S.1    Do, H.2    Lee, J.H.3    Park, S.I.4    Kim, E.J.5    Kim, S.-J.6    Kang, S.-H.7    Kim, H.J.8
  • 36
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • PID: 21959131, COI: 1:CAS:528:DC%2BC3MXht1CrtrbL
    • Petersen TN, Brunak S, von Heijne G, Nielsen H (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8:785–786
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 37
    • 84867333492 scopus 로고    scopus 로고
    • Structural prediction of a novel chitinase from the psychrophilic Glaciozyma antarctica PI12 and an analysis of its structural properties and function
    • PID: 22710891, COI: 1:CAS:528:DC%2BC38Xht1ens7bI
    • Ramli A, Mahadi N, Shamsir M, Rabu A, Joyce-Tan K, Murad A, Illias R (2012) Structural prediction of a novel chitinase from the psychrophilic Glaciozyma antarctica PI12 and an analysis of its structural properties and function. J Comput Aided Mol Des 26:947–961
    • (2012) J Comput Aided Mol Des , vol.26 , pp. 947-961
    • Ramli, A.1    Mahadi, N.2    Shamsir, M.3    Rabu, A.4    Joyce-Tan, K.5    Murad, A.6    Illias, R.7
  • 38
    • 0042183228 scopus 로고
    • Adsorption inhibition as a mechanism of freezing resistance in polar fishes
    • PID: 267952, COI: 1:CAS:528:DyaE2sXks1Cgsbg%3D
    • Raymond JA, DeVries AL (1977) Adsorption inhibition as a mechanism of freezing resistance in polar fishes. Proc Natl Acad Sci USA 74:2589–2593
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 2589-2593
    • Raymond, J.A.1    DeVries, A.L.2
  • 39
    • 84860436217 scopus 로고    scopus 로고
    • Possible role of horizontal gene transfer in the colonization of sea ice by algae
    • PID: 22567121, COI: 1:CAS:528:DC%2BC38Xntlegu78%3D
    • Raymond JA, Kim HJ (2012) Possible role of horizontal gene transfer in the colonization of sea ice by algae. PLoS One 7:e35968
    • (2012) PLoS One , vol.7 , pp. e35968
    • Raymond, J.A.1    Kim, H.J.2
  • 40
    • 30844452668 scopus 로고    scopus 로고
    • Ice recrystallization inhibition in ice cream as affected by ice structuring proteins from winter wheat grass
    • PID: 16357267, COI: 1:CAS:528:DC%2BD28XisVSlsg%3D%3D
    • Regand A, Goff HD (2006) Ice recrystallization inhibition in ice cream as affected by ice structuring proteins from winter wheat grass. J Dairy Sci 89:49–57
    • (2006) J Dairy Sci , vol.89 , pp. 49-57
    • Regand, A.1    Goff, H.D.2
  • 41
    • 0034904149 scopus 로고    scopus 로고
    • Cold adaptation in Arctic and Antarctic fungi
    • COI: 1:CAS:528:DC%2BD3MXmsF2hsLc%3D
    • Robinson CH (2001) Cold adaptation in Arctic and Antarctic fungi. New Phytol 151:341–353
    • (2001) New Phytol , vol.151 , pp. 341-353
    • Robinson, C.H.1
  • 42
    • 79956333156 scopus 로고    scopus 로고
    • A peek at ice binding by antifreeze proteins
    • PID: 21518869, COI: 1:CAS:528:DC%2BC3MXmtFSku78%3D
    • Sharp KA (2011) A peek at ice binding by antifreeze proteins. Proc Natl Acad Sci USA 108:7281–7282
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 7281-7282
    • Sharp, K.A.1
  • 43
    • 0029013417 scopus 로고
    • Ice-binding structure and mechanism of an antifreeze protein from winter flounder
    • PID: 7760940, COI: 1:CAS:528:DyaK2MXmtVehtro%3D
    • Sicheri F, Yang DSC (1995) Ice-binding structure and mechanism of an antifreeze protein from winter flounder. Nature 375:427–431
    • (1995) Nature , vol.375 , pp. 427-431
    • Sicheri, F.1    Yang, D.S.C.2
  • 44
    • 0030589054 scopus 로고    scopus 로고
    • Refined solution structure of type III antifreeze protein: hydrophobic groups may be involved in the energetics of the protein ice interaction
    • PID: 8939756
    • Sönnichsen FD, DeLuca CI, Davies PL, Sykes BD (1996) Refined solution structure of type III antifreeze protein: hydrophobic groups may be involved in the energetics of the protein ice interaction. Structure 4:1325–1337
    • (1996) Structure , vol.4 , pp. 1325-1337
    • Sönnichsen, F.D.1    DeLuca, C.I.2    Davies, P.L.3    Sykes, B.D.4
  • 45
    • 0028807747 scopus 로고
    • Low temperature growth, freezing survival, and production of antifreeze protein by the plant growth promoting rhizobacterium Pseudomonas putida GR12-2
    • PID: 7585354, COI: 1:CAS:528:DyaK2MXotlKksro%3D
    • Sun X, Griffith M, Pasternak JJ, Glick BR (1995) Low temperature growth, freezing survival, and production of antifreeze protein by the plant growth promoting rhizobacterium Pseudomonas putida GR12-2. Can J Microbiol 41:776–784
    • (1995) Can J Microbiol , vol.41 , pp. 776-784
    • Sun, X.1    Griffith, M.2    Pasternak, J.J.3    Glick, B.R.4
  • 46
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: molecular evolutionary genetics analysis (MEGA) Software Version 4.0
    • PID: 17488738, COI: 1:CAS:528:DC%2BD2sXpsVGrsL8%3D
    • Tamura K, Dudley J, Nei M, Kumar S (2007) MEGA4: molecular evolutionary genetics analysis (MEGA) Software Version 4.0. Mol Biol Evol 24:1596–1599
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 48
    • 82155196420 scopus 로고    scopus 로고
    • Heterologous expression, refolding and functional characterization of two antifreeze proteins from Fragilariopsis cylindrus (Bacillariophyceae)
    • PID: 21884691, COI: 1:CAS:528:DC%2BC3MXhsFCqsLbF
    • Uhlig C, Kabisch J, Palm GJ, Valentin K, Schweder T, Krell A (2011) Heterologous expression, refolding and functional characterization of two antifreeze proteins from Fragilariopsis cylindrus (Bacillariophyceae). Cryobiology 63:220–228
    • (2011) Cryobiology , vol.63 , pp. 220-228
    • Uhlig, C.1    Kabisch, J.2    Palm, G.J.3    Valentin, K.4    Schweder, T.5    Krell, A.6
  • 49
    • 40349103663 scopus 로고    scopus 로고
    • Properties, potentials, and prospects of antifreeze proteins
    • PID: 18322856, COI: 1:CAS:528:DC%2BD1cXislGks7k%3D
    • Venketesh S, Dayananda C (2008) Properties, potentials, and prospects of antifreeze proteins. Crit Rev Biotechnol 28:57–82
    • (2008) Crit Rev Biotechnol , vol.28 , pp. 57-82
    • Venketesh, S.1    Dayananda, C.2
  • 50
    • 34249928081 scopus 로고
    • Purification and characterization of antifreeze proteins from larvae of the beetle Dendroides canadensis
    • COI: 1:CAS:528:DyaK3MXmtVWmsro%3D
    • Wu DW, Duman JG, Cheng C-HC, Castellino FJ (1991) Purification and characterization of antifreeze proteins from larvae of the beetle Dendroides canadensis. J Comp Phys B 161:271–278
    • (1991) J Comp Phys B , vol.161 , pp. 271-278
    • Wu, D.W.1    Duman, J.G.2    Cheng, C.-H.C.3    Castellino, F.J.4
  • 51
    • 74549175232 scopus 로고    scopus 로고
    • Comparison of functional properties of two fungal antifreeze proteins from Antarctomyces psychrotrophicus and Typhula ishikariensis
    • PID: 20030710, COI: 1:CAS:528:DC%2BC3cXptVWiug%3D%3D
    • Xiao N, Suzuki K, Nishimiya Y, Kondo H, Miura A, Tsuda S, Hoshino T (2010) Comparison of functional properties of two fungal antifreeze proteins from Antarctomyces psychrotrophicus and Typhula ishikariensis. FEBS J 277:394–403
    • (2010) FEBS J , vol.277 , pp. 394-403
    • Xiao, N.1    Suzuki, K.2    Nishimiya, Y.3    Kondo, H.4    Miura, A.5    Tsuda, S.6    Hoshino, T.7
  • 52
    • 34247590409 scopus 로고    scopus 로고
    • Effect of carrot (Daucus carota) antifreeze proteins on the fermentation capacity of frozen dough
    • COI: 1:CAS:528:DC%2BD2sXkvFOiu74%3D
    • Zhang C, Zhang H, Wang L (2007) Effect of carrot (Daucus carota) antifreeze proteins on the fermentation capacity of frozen dough. Food Res Int 40:763–769
    • (2007) Food Res Int , vol.40 , pp. 763-769
    • Zhang, C.1    Zhang, H.2    Wang, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.