메뉴 건너뛰기




Volumn 23, Issue 5, 2014, Pages 1507-1513

Heterologous expression and purification of Zea mays transglutaminase in Pichia pastoris

Author keywords

Pichia pastoris GS115; polymerization effect; protein expression; purification; Zea mays transglutaminase

Indexed keywords

BAKERIES; ION EXCHANGE RESINS; POLYMERIZATION; PROTEINS; PURIFICATION; TEXTURES;

EID: 84918516204     PISSN: 12267708     EISSN: 20926456     Source Type: Journal    
DOI: 10.1007/s10068-014-0206-1     Document Type: Article
Times cited : (8)

References (29)
  • 1
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature’s biological glues
    • COI: 1:CAS:528:DC%2BD38XovF2jt78%3D
    • Griffin M, Casadio R, Bergamini CM. Transglutaminases: Nature’s biological glues. Biochem. J. 368: 377–396 (2002)
    • (2002) Biochem. J. , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 2
    • 2442610049 scopus 로고    scopus 로고
    • Properties and applications of microbial transglutaminase
    • COI: 1:CAS:528:DC%2BD2cXjtFyis7w%3D
    • Yokoyama K, Nio N, Kikuchi Y. Properties and applications of microbial transglutaminase. Appl. Microbiol. Biotechnol. 64: 447–454 (2004)
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 447-454
    • Yokoyama, K.1    Nio, N.2    Kikuchi, Y.3
  • 3
    • 0036813333 scopus 로고    scopus 로고
    • Transglutaminase catalyzed reactions: Impact on food applications
    • COI: 1:CAS:528:DC%2BD38XptVensbk%3D
    • DeJong G, Koppelman S. Transglutaminase catalyzed reactions: Impact on food applications. J. Food Sci. 67: 2798–2806 (2002)
    • (2002) J. Food Sci. , vol.67 , pp. 2798-2806
    • DeJong, G.1    Koppelman, S.2
  • 4
    • 42749091455 scopus 로고    scopus 로고
    • Purification and activation of a recombinant histidine-tagged pro-transglutaminase after soluble expression in Escherichia coli and partial characterization of the active enzyme
    • COI: 1:CAS:528:DC%2BD1cXlvVSgsb4%3D
    • Marx CK, Hertel TC, Pietzsch M. Purification and activation of a recombinant histidine-tagged pro-transglutaminase after soluble expression in Escherichia coli and partial characterization of the active enzyme. Enzyme Microb. Technol. 42: 568–575 (2008)
    • (2008) Enzyme Microb. Technol. , vol.42 , pp. 568-575
    • Marx, C.K.1    Hertel, T.C.2    Pietzsch, M.3
  • 5
    • 70449107878 scopus 로고    scopus 로고
    • Recent patents on transglutaminase production and applications: A brief review
    • COI: 1:CAS:528:DC%2BD1MXhsFWhtLbL
    • Santos M, Torne J. Recent patents on transglutaminase production and applications: A brief review. Recent Patents Biotechnol. 3: 166–174 (2009)
    • (2009) Recent Patents Biotechnol. , vol.3 , pp. 166-174
    • Santos, M.1    Torne, J.2
  • 6
    • 0000182588 scopus 로고
    • Evidence for transglutaminase activity in plant tissue
    • COI: 1:CAS:528:DyaL2sXlt12lu7k%3D
    • Icekson I, Apelbaum A. Evidence for transglutaminase activity in plant tissue. Plant Physiol. 84: 972–974 (1987)
    • (1987) Plant Physiol. , vol.84 , pp. 972-974
    • Icekson, I.1    Apelbaum, A.2
  • 7
    • 0002152563 scopus 로고
    • Identification of the large subunit of ribulose 1, 5-bisphosphate carboxylase/oxygenase as a substrate for transglutaminase in Medicago sativa L. (Alfalfa)
    • COI: 1:CAS:528:DyaK3cXhtFCksrk%3D
    • Margosiak SA, Dharma A, Bruce-Carver MR, Gonzales AP, Louie D, Kuehn GD. Identification of the large subunit of ribulose 1, 5-bisphosphate carboxylase/oxygenase as a substrate for transglutaminase in Medicago sativa L. (Alfalfa). Plant Physiol. 92: 88–96 (1990)
    • (1990) Plant Physiol. , vol.92 , pp. 88-96
    • Margosiak, S.A.1    Dharma, A.2    Bruce-Carver, M.R.3    Gonzales, A.P.4    Louie, D.5    Kuehn, G.D.6
  • 8
    • 0028042505 scopus 로고
    • Identification of chlorophyll-a/b proteins as substrates of transglutaminase activity in isolated chloroplasts of Helianthus tuberosus L
    • Duca S, Tidu V, Bassi R, Esposito C, Serafmi-Fracassini D. Identification of chlorophyll-a/b proteins as substrates of transglutaminase activity in isolated chloroplasts of Helianthus tuberosus L. Planta 193: 283–289 (1994)
    • (1994) Planta , vol.193 , pp. 283-289
    • Duca, S.1    Tidu, V.2    Bassi, R.3    Esposito, C.4    Serafmi-Fracassini, D.5
  • 9
    • 0030583141 scopus 로고    scopus 로고
    • Purification and properties of transglutaminase from soybean (Glycine max) leaves
    • COI: 1:CAS:528:DyaK28Xjs1yhtL8%3D
    • Kang H, Cho YD. Purification and properties of transglutaminase from soybean (Glycine max) leaves. Biochem. Bioph. Res. Co. 223: 288–292 (1996)
    • (1996) Biochem. Bioph. Res. Co. , vol.223 , pp. 288-292
    • Kang, H.1    Cho, Y.D.2
  • 10
    • 0033403636 scopus 로고    scopus 로고
    • Changes in polyamine content, arginine and ornithine decarboxylases and transglutaminase activities during light/dark phases (of initial differentiation) in maize calluses and their chloroplasts
    • COI: 1:CAS:528:DC%2BD3cXhtValuro%3D
    • Bernet E, Claparols I, Dondini L, Asunción Santos M, Serafini-Fracassini D, Torné JM. Changes in polyamine content, arginine and ornithine decarboxylases and transglutaminase activities during light/dark phases (of initial differentiation) in maize calluses and their chloroplasts. Plant Physiol. Bioch. 37: 899–909 (1999)
    • (1999) Plant Physiol. Bioch. , vol.37 , pp. 899-909
    • Bernet, E.1    Claparols, I.2    Dondini, L.3    Asunción Santos, M.4    Serafini-Fracassini, D.5    Torné, J.M.6
  • 11
    • 0034987989 scopus 로고    scopus 로고
    • Immunogold localization of a transglutaminase related to grana development in different maize cell types
    • COI: 1:CAS:528:DC%2BD3MXnvVamt7c%3D
    • Villalobos E, Torné J, Rigau J, Ollés I, Claparols I, Santos M. Immunogold localization of a transglutaminase related to grana development in different maize cell types. Protoplasma. 216: 155–163 (2001)
    • (2001) Protoplasma. , vol.216 , pp. 155-163
    • Villalobos, E.1    Torné, J.2    Rigau, J.3    Ollés, I.4    Claparols, I.5    Santos, M.6
  • 12
    • 3242794297 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a maize transglutaminase complementary DNA
    • COI: 1:CAS:528:DC%2BD2cXltFOqtrc%3D
    • Villalobos E, Santos M, Talavera D, Rodrlguez-Falcón M, Torné J. Molecular cloning and characterization of a maize transglutaminase complementary DNA. Gene 336: 93–104 (2004)
    • (2004) Gene , vol.336 , pp. 93-104
    • Villalobos, E.1    Santos, M.2    Talavera, D.3    Rodrlguez-Falcón, M.4    Torné, J.5
  • 14
    • 79851472440 scopus 로고    scopus 로고
    • Activity of maize transglutaminase overexpressed in Escherichia coli inclusion bodies: An alternative to protein refolding
    • COI: 1:CAS:528:DC%2BC3MXivF2ls70%3D
    • Carvajal P, Gibert J, Campos N, Lopera O, Barberà E, Torné JM, Santos M. Activity of maize transglutaminase overexpressed in Escherichia coli inclusion bodies: An alternative to protein refolding. Biotechnol. Prog. 27: 232–240 (2011)
    • (2011) Biotechnol. Prog. , vol.27 , pp. 232-240
    • Carvajal, P.1    Gibert, J.2    Campos, N.3    Lopera, O.4    Barberà, E.5    Torné, J.M.6    Santos, M.7
  • 15
    • 14744285206 scopus 로고    scopus 로고
    • Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production
    • COI: 1:CAS:528:DC%2BD2MXitFOns7Y%3D
    • Daly R, Hearn MTW. Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production. J. Mol. Recognit. 18: 119–138 (2005)
    • (2005) J. Mol. Recognit. , vol.18 , pp. 119-138
    • Daly, R.1    Hearn, M.T.W.2
  • 16
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • COI: 1:CAS:528:DC%2BD3cXltVClug%3D%3D
    • Cereghino JL, Cregg JM. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 24: 45–66 (2000)
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 17
    • 45449105347 scopus 로고    scopus 로고
    • A new fermentation strategy for S-adenosylmethionine production in recombinant Pichia pastoris
    • Zhang J, Wang X, Su E, Fang G, Ren Y, Wei D. A new fermentation strategy for S-adenosylmethionine production in recombinant Pichia pastoris. Biochem. Eng. J. 41: 74–78 (2008)
    • (2008) Biochem. Eng. J. , vol.41 , pp. 74-78
    • Zhang, J.1    Wang, X.2    Su, E.3    Fang, G.4    Ren, Y.5    Wei, D.6
  • 18
    • 79959753179 scopus 로고    scopus 로고
    • Cloning of levansucrase from Leuconostoc mesenteroides and its expression in Pichia pastoris
    • COI: 1:CAS:528:DC%2BC3MXisVKks7Y%3D
    • Kang HK, Yun SI, Lim TY, Xia YM, Kim D. Cloning of levansucrase from Leuconostoc mesenteroides and its expression in Pichia pastoris. Food Sci. Biotechnol. 20: 277–281 (2011)
    • (2011) Food Sci. Biotechnol. , vol.20 , pp. 277-281
    • Kang, H.K.1    Yun, S.I.2    Lim, T.Y.3    Xia, Y.M.4    Kim, D.5
  • 19
    • 79959697903 scopus 로고    scopus 로고
    • Expression, purification, and characterization of human intestinal maltase secreted from Pichia pastoris
    • COI: 1:CAS:528:DC%2BC3MXlsFSiu7w%3D
    • Ryu HJ, Seo ES, Kang HK, Kim YM, Kim D. Expression, purification, and characterization of human intestinal maltase secreted from Pichia pastoris. Food Sci. Biotechnol. 20: 561–565 (2011)
    • (2011) Food Sci. Biotechnol. , vol.20 , pp. 561-565
    • Ryu, H.J.1    Seo, E.S.2    Kang, H.K.3    Kim, Y.M.4    Kim, D.5
  • 20
    • 84862525931 scopus 로고    scopus 로고
    • Enzymatic characterization of transglutaminase from Streptomyces mobaraensis DSM 40587 in high salt and effect of enzymatic cross-linking of yak milk proteins on functional properties of stirred yogurt
    • COI: 1:CAS:528:DC%2BC38XoslGmsLw%3D
    • Zhang L, Zhang L, Yi H, Du M, Ma C, Han X, Feng Z, Jiao Y, Zhang Y. Enzymatic characterization of transglutaminase from Streptomyces mobaraensis DSM 40587 in high salt and effect of enzymatic cross-linking of yak milk proteins on functional properties of stirred yogurt. J. Dairy Sci. 95: 3559–3568 (2012)
    • (2012) J. Dairy Sci. , vol.95 , pp. 3559-3568
    • Zhang, L.1    Zhang, L.2    Yi, H.3    Du, M.4    Ma, C.5    Han, X.6    Feng, Z.7    Jiao, Y.8    Zhang, Y.9
  • 21
    • 84918511278 scopus 로고    scopus 로고
    • Cloning and expression of maize transglutaminase in Escherichia coli
    • COI: 1:CAS:528:DC%2BC3cXot12ks7g%3D
    • Qin LX, Wang L, Zhang LW. Cloning and expression of maize transglutaminase in Escherichia coli. Food Sci. 31: 177–181 (2010)
    • (2010) Food Sci. , vol.31 , pp. 177-181
    • Qin, L.X.1    Wang, L.2    Zhang, L.W.3
  • 22
    • 3242882045 scopus 로고    scopus 로고
    • A Pichia pastoris fermentation strategy for enhancing the heterologous expression of an Escherichia coli phytase
    • Chen CC, Wu PH, Huang CT, Cheng KJ. A Pichia pastoris fermentation strategy for enhancing the heterologous expression of an Escherichia coli phytase. Enzyme Microb. Technol. 35: 315–320 (2004)
    • (2004) Enzyme Microb. Technol. , vol.35 , pp. 315-320
    • Chen, C.C.1    Wu, P.H.2    Huang, C.T.3    Cheng, K.J.4
  • 23
    • 76549212824 scopus 로고
    • The enzymatic formation of hydroxamic acids from glutamine and asparagine
    • COI: 1:CAS:528:DyaG3MXitF2isg%3D%3D
    • Grossowicz N, Wainfan E, Borek E, Waelsch H. The enzymatic formation of hydroxamic acids from glutamine and asparagine. J. Biol. Chem. 187: 111–125 (1950)
    • (1950) J. Biol. Chem. , vol.187 , pp. 111-125
    • Grossowicz, N.1    Wainfan, E.2    Borek, E.3    Waelsch, H.4
  • 24
    • 45449089087 scopus 로고    scopus 로고
    • Protein expression and purification of human Zbtb7A in Pichia pastoris via gene codon optimization and synthesis
    • COI: 1:CAS:528:DC%2BD1cXns1ahtr4%3D
    • Wang H, Wang Q, Zhang F, Huang Y, Ji Y, Hou Y. Protein expression and purification of human Zbtb7A in Pichia pastoris via gene codon optimization and synthesis. Protein Expr. Purif. 60: 97–102 (2008)
    • (2008) Protein Expr. Purif. , vol.60 , pp. 97-102
    • Wang, H.1    Wang, Q.2    Zhang, F.3    Huang, Y.4    Ji, Y.5    Hou, Y.6
  • 25
    • 78650175370 scopus 로고    scopus 로고
    • Expression and purification of soluble murine CD40L monomers and polymers in yeast Pichia pastoris
    • COI: 1:CAS:528:DC%2BC3cXhsFGgsb%2FI
    • Hermanrud CE, Lucas CL, Sykes M, Huang CA, Wang Z. Expression and purification of soluble murine CD40L monomers and polymers in yeast Pichia pastoris. Protein Expr. Purif. 76: 115–120 (2011)
    • (2011) Protein Expr. Purif. , vol.76 , pp. 115-120
    • Hermanrud, C.E.1    Lucas, C.L.2    Sykes, M.3    Huang, C.A.4    Wang, Z.5
  • 26
    • 22744459759 scopus 로고    scopus 로고
    • Effect of methanol concentration on the recombinant Pichia pastoris Muts fermentation
    • COI: 1:CAS:528:DC%2BD2MXovV2nur4%3D
    • Kupcsulik B, Sevella B. Effect of methanol concentration on the recombinant Pichia pastoris Muts fermentation. Chem. Eng. 48: 73–87 (2004)
    • (2004) Chem. Eng. , vol.48 , pp. 73-87
    • Kupcsulik, B.1    Sevella, B.2
  • 27
    • 33847294641 scopus 로고    scopus 로고
    • A novel feeding strategy during the production phase for enhancing the enzymatic synthesis of S-adenosyl-l-methionine by methylotrophic Pichia pastoris
    • COI: 1:CAS:528:DC%2BD2sXit1Gks7g%3D
    • Hu XQ, Chu J, Zhang SL, Zhuang YP, Wang YH, Zhu S, Zhu ZG, Yuan ZY. A novel feeding strategy during the production phase for enhancing the enzymatic synthesis of S-adenosyl-l-methionine by methylotrophic Pichia pastoris. Enzyme Microb. Technol. 40: 669–674 (2007)
    • (2007) Enzyme Microb. Technol. , vol.40 , pp. 669-674
    • Hu, X.Q.1    Chu, J.2    Zhang, S.L.3    Zhuang, Y.P.4    Wang, Y.H.5    Zhu, S.6    Zhu, Z.G.7    Yuan, Z.Y.8
  • 28
    • 33747594745 scopus 로고    scopus 로고
    • Stability of casein micelles cross-linked by transglutaminase
    • COI: 1:CAS:528:DC%2BD28Xlt1eru78%3D
    • Smiddy M, Martin JEGH, Kelly A, De Kruif C, Huppertz T. Stability of casein micelles cross-linked by transglutaminase. J. Dairy Sci. 89: 1906–1914 (2006)
    • (2006) J. Dairy Sci. , vol.89 , pp. 1906-1914
    • Smiddy, M.1    Martin, J.E.G.H.2    Kelly, A.3    De Kruif, C.4    Huppertz, T.5
  • 29
    • 58249100043 scopus 로고    scopus 로고
    • Properties of casein micelles cross-linked by transglutaminase
    • COI: 1:CAS:528:DC%2BD1MXislOgsLs%3D
    • Moon JH, Hong YH, Huppertz T, Fox PF, Kelly AL. Properties of casein micelles cross-linked by transglutaminase. Int. J. Dairy Technol. 62: 27–32 (2009)
    • (2009) Int. J. Dairy Technol. , vol.62 , pp. 27-32
    • Moon, J.H.1    Hong, Y.H.2    Huppertz, T.3    Fox, P.F.4    Kelly, A.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.