메뉴 건너뛰기




Volumn 69, Issue 1, 2010, Pages 112-119

Secretory expression of functional barley limit dextrinase by Pichia pastoris using high cell-density fermentation

Author keywords

Barley limit dextrinase; Cyclodextrin affinity; High cell density fermentation; Pichia pastoris; Pullulan hydrolysis

Indexed keywords

CYCLODEXTRIN; GLUCAN; GLYCOSIDASE; PULLULAN; PULLULANASE; RECOMBINANT PROTEIN;

EID: 70350776503     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2009.08.016     Document Type: Article
Times cited : (26)

References (52)
  • 2
    • 84983947206 scopus 로고
    • Studies on carbohydrate metabolising enzymes. Part XXVI. Limit dextrinase from germinated barley
    • Manners D.J., and Yellowlees D. Studies on carbohydrate metabolising enzymes. Part XXVI. Limit dextrinase from germinated barley. Starch/Stärke 23 (1971) 228-234
    • (1971) Starch/Stärke , vol.23 , pp. 228-234
    • Manners, D.J.1    Yellowlees, D.2
  • 3
    • 0040020893 scopus 로고
    • α-amylase limit dextrinase, and α-glucosidase enzymes in barley and malt
    • MacGregor A.W. α-amylase limit dextrinase, and α-glucosidase enzymes in barley and malt. Crit. Rev. Biotechnol. 5 (1987) 117-128
    • (1987) Crit. Rev. Biotechnol. , vol.5 , pp. 117-128
    • MacGregor, A.W.1
  • 4
    • 0032920149 scopus 로고    scopus 로고
    • Isolation and characterization of the gene encoding the starch debranching enzyme limit dextrinase from germinating barley
    • Kristensen M., Lok F., Planchot V., Svendsen I., Leah R., and Svensson B. Isolation and characterization of the gene encoding the starch debranching enzyme limit dextrinase from germinating barley. Biochim. Biophys. Acta 1431 (1999) 538-546
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 538-546
    • Kristensen, M.1    Lok, F.2    Planchot, V.3    Svendsen, I.4    Leah, R.5    Svensson, B.6
  • 6
    • 33845665889 scopus 로고    scopus 로고
    • Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of alpha-amylase-related proteins
    • Stam M.R., Danchin E.G.J., Rancurel C., Coutinho P.M., and Henrissat B. Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of alpha-amylase-related proteins. Protein Eng. Des. Sel. 19 (2006) 555-562
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 555-562
    • Stam, M.R.1    Danchin, E.G.J.2    Rancurel, C.3    Coutinho, P.M.4    Henrissat, B.5
  • 7
    • 0033102225 scopus 로고    scopus 로고
    • A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley
    • Burton R.A., Zhang X.Q., Hrmova M., and Fincher G.B. A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley. Plant Physiol. 119 (1999) 859-871
    • (1999) Plant Physiol. , vol.119 , pp. 859-871
    • Burton, R.A.1    Zhang, X.Q.2    Hrmova, M.3    Fincher, G.B.4
  • 8
    • 0002440434 scopus 로고    scopus 로고
    • Synthesis of limit dextrinase in germinated barley kernels and aleurone tissues
    • Schroeder S.W., and MacGregor A.W. Synthesis of limit dextrinase in germinated barley kernels and aleurone tissues. J. Am. Soc. Brew. Chem. 56 (1998) 32-37
    • (1998) J. Am. Soc. Brew. Chem. , vol.56 , pp. 32-37
    • Schroeder, S.W.1    MacGregor, A.W.2
  • 9
    • 0037341209 scopus 로고    scopus 로고
    • Mutational analysis of the pullulanase-type debranching enzyme of maize indicates multiple functions in starch metabolism
    • Dinges J.R., Colleoni C., James M.G., and Myers A.M. Mutational analysis of the pullulanase-type debranching enzyme of maize indicates multiple functions in starch metabolism. Plant Cell 15 (2003) 666-680
    • (2003) Plant Cell , vol.15 , pp. 666-680
    • Dinges, J.R.1    Colleoni, C.2    James, M.G.3    Myers, A.M.4
  • 11
    • 0010980673 scopus 로고
    • Studies on limit dextrinase in barley. 3. Limit dextrinase in developing kernels
    • Sissons M.J., Lance R.C.M., and Sparrow D.H.B. Studies on limit dextrinase in barley. 3. Limit dextrinase in developing kernels. J. Cereal Sci. 17 (1993) 19-24
    • (1993) J. Cereal Sci. , vol.17 , pp. 19-24
    • Sissons, M.J.1    Lance, R.C.M.2    Sparrow, D.H.B.3
  • 12
    • 0029328417 scopus 로고
    • Starch synthesis
    • Martin C., and Smith A.M. Starch synthesis. Plant Cell 7 (1995) 971-985
    • (1995) Plant Cell , vol.7 , pp. 971-985
    • Martin, C.1    Smith, A.M.2
  • 13
    • 0034890627 scopus 로고    scopus 로고
    • The biosynthesis of starch granules
    • Smith A.M. The biosynthesis of starch granules. Biomacromolecules 2 (2001) 335-341
    • (2001) Biomacromolecules , vol.2 , pp. 335-341
    • Smith, A.M.1
  • 14
    • 62549154915 scopus 로고    scopus 로고
    • Starch granule biosynthesis in Arabidopsis is abolished by removal of all debranching enzymes but restored by the subsequent removal of an endoamylase
    • Streb S., Delatte T., Umhang M., Eicke S., Schorderet M., Reinhardt D., and Zeeman S.C. Starch granule biosynthesis in Arabidopsis is abolished by removal of all debranching enzymes but restored by the subsequent removal of an endoamylase. Plant Cell 20 (2008) 3448-3466
    • (2008) Plant Cell , vol.20 , pp. 3448-3466
    • Streb, S.1    Delatte, T.2    Umhang, M.3    Eicke, S.4    Schorderet, M.5    Reinhardt, D.6    Zeeman, S.C.7
  • 15
    • 0000687121 scopus 로고
    • Development of limit dextrinase in germinated barley (Hordeum vulgare L.) (evidence of proteolytic activation)
    • Longstaff M.A., and Bryce J.H. Development of limit dextrinase in germinated barley (Hordeum vulgare L.) (evidence of proteolytic activation). Plant Physiol. 101 (1993) 881-889
    • (1993) Plant Physiol. , vol.101 , pp. 881-889
    • Longstaff, M.A.1    Bryce, J.H.2
  • 17
    • 0028095685 scopus 로고
    • Purification and characterization of limit dextrinase inhibitors from barley
    • MacGregor A.W., Macri L.J., Schroeder S.W., and Bazin S.L. Purification and characterization of limit dextrinase inhibitors from barley. J. Cereal Sci. 20 (1994) 33-41
    • (1994) J. Cereal Sci. , vol.20 , pp. 33-41
    • MacGregor, A.W.1    Macri, L.J.2    Schroeder, S.W.3    Bazin, S.L.4
  • 18
    • 0008581550 scopus 로고
    • Thioredoxin-dependent deinhibition of pullulanase of barley malt by inactivation of a specific inhibitor protein
    • Wong J.H., Iiao I.A., Kobrehel K., and Buchanan B.B. Thioredoxin-dependent deinhibition of pullulanase of barley malt by inactivation of a specific inhibitor protein. Plant Physiol. 108 (1995) 67
    • (1995) Plant Physiol. , vol.108 , pp. 67
    • Wong, J.H.1    Iiao, I.A.2    Kobrehel, K.3    Buchanan, B.B.4
  • 19
    • 14944341315 scopus 로고    scopus 로고
    • Limit dextrinase-does its malt activity relate to its activity during brewing
    • McCafferty C.A., Jenkinson H.R., Brosnan J.M., and Bryce J.H. Limit dextrinase-does its malt activity relate to its activity during brewing. J. Inst. Brew. 110 (2004) 284-296
    • (2004) J. Inst. Brew. , vol.110 , pp. 284-296
    • McCafferty, C.A.1    Jenkinson, H.R.2    Brosnan, J.M.3    Bryce, J.H.4
  • 20
    • 7444266924 scopus 로고
    • The separation of limit dextrinase from R-enzyme and aspects of the activity of the separated enzymes
    • MacWilliam I.C., and Harris G. The separation of limit dextrinase from R-enzyme and aspects of the activity of the separated enzymes. Arch. Biochem. Biophys. 84 (1959) 442-454
    • (1959) Arch. Biochem. Biophys. , vol.84 , pp. 442-454
    • MacWilliam, I.C.1    Harris, G.2
  • 21
    • 0036399743 scopus 로고    scopus 로고
    • Enzymatic properties and regulation of ZPU1, the maize pullulanase-type starch debranching enzyme
    • Wu C.Y., Colleoni C., Myers A.M., and James M.G. Enzymatic properties and regulation of ZPU1, the maize pullulanase-type starch debranching enzyme. Arch. Biochem. Biophys. 406 (2002) 21-32
    • (2002) Arch. Biochem. Biophys. , vol.406 , pp. 21-32
    • Wu, C.Y.1    Colleoni, C.2    Myers, A.M.3    James, M.G.4
  • 22
    • 0032080115 scopus 로고    scopus 로고
    • CDNA sequence and heterologous expression of monomeric spinach pullulanase: multiple isomeric forms arise from the same polypeptide
    • Renz A., Schikora S., Schmid R., Kossmann J., and Beck E. CDNA sequence and heterologous expression of monomeric spinach pullulanase: multiple isomeric forms arise from the same polypeptide. Biochem. J. 331 (1998) 937-945
    • (1998) Biochem. J. , vol.331 , pp. 937-945
    • Renz, A.1    Schikora, S.2    Schmid, R.3    Kossmann, J.4    Beck, E.5
  • 23
    • 39649119081 scopus 로고    scopus 로고
    • In vitro pullulanase activity of wheat (Triticum aestivum L.) limit-dextrinase type starch debranching enzyme is modulated by redox conditions
    • Repellin A., Baga M., and Chibbar R.N. In vitro pullulanase activity of wheat (Triticum aestivum L.) limit-dextrinase type starch debranching enzyme is modulated by redox conditions. J. Cereal Sci. 47 (2008) 302-309
    • (2008) J. Cereal Sci. , vol.47 , pp. 302-309
    • Repellin, A.1    Baga, M.2    Chibbar, R.N.3
  • 24
    • 0032190488 scopus 로고    scopus 로고
    • Expression of enzymatically active, recombinant barley alpha-glucosidase in yeast and immunological detection of alpha-glucosidase from seed tissue
    • Tibbot B.K., Henson C.A., and Skadsen R.W. Expression of enzymatically active, recombinant barley alpha-glucosidase in yeast and immunological detection of alpha-glucosidase from seed tissue. Plant Mol. Biol. 38 (1998) 379-391
    • (1998) Plant Mol. Biol. , vol.38 , pp. 379-391
    • Tibbot, B.K.1    Henson, C.A.2    Skadsen, R.W.3
  • 25
    • 32644463519 scopus 로고    scopus 로고
    • Production of enzymatically active recombinant full-length barley high pI alpha-glucosidase of glycoside family 31 by high cell-density fermentation of Pichia pastoris and affinity purification
    • Naested H., Kramhoft B., Lok F., Bojsen K., Yu S.K., and Svensson B. Production of enzymatically active recombinant full-length barley high pI alpha-glucosidase of glycoside family 31 by high cell-density fermentation of Pichia pastoris and affinity purification. Protein Expr. Purif. 46 (2006) 56-63
    • (2006) Protein Expr. Purif. , vol.46 , pp. 56-63
    • Naested, H.1    Kramhoft, B.2    Lok, F.3    Bojsen, K.4    Yu, S.K.5    Svensson, B.6
  • 26
    • 0346787608 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of branched oligo- and polysaccharides as potential substrates for starch active enzymes
    • Greffe L., Jensen M.T., Bosso C., Svensson B., and Driguez H. Chemoenzymatic synthesis of branched oligo- and polysaccharides as potential substrates for starch active enzymes. Chembiochem 4 (2003) 1307-1311
    • (2003) Chembiochem , vol.4 , pp. 1307-1311
    • Greffe, L.1    Jensen, M.T.2    Bosso, C.3    Svensson, B.4    Driguez, H.5
  • 27
    • 2242454125 scopus 로고    scopus 로고
    • Chemoenzymatic syntheses of linear and branched hemithiomaltodextrins as potential inhibitors for starch-debranching enzymes
    • Greffe L., Jensen M.T., Chang-Pi-Hin F., Fruchard S., O'Donohue M.J., Svensson B., and Driguez H. Chemoenzymatic syntheses of linear and branched hemithiomaltodextrins as potential inhibitors for starch-debranching enzymes. Chem. Eur. J. 8 (2002) 5447-5455
    • (2002) Chem. Eur. J. , vol.8 , pp. 5447-5455
    • Greffe, L.1    Jensen, M.T.2    Chang-Pi-Hin, F.3    Fruchard, S.4    O'Donohue, M.J.5    Svensson, B.6    Driguez, H.7
  • 30
    • 0031873219 scopus 로고    scopus 로고
    • Large-scale purification and characterization of barley limit dextrinase, a member of the α-amylase structural family
    • Kristensen M., Planchot V., Abe J.I., and Svensson B. Large-scale purification and characterization of barley limit dextrinase, a member of the α-amylase structural family. Cereal Chem. 75 (1998) 473-479
    • (1998) Cereal Chem. , vol.75 , pp. 473-479
    • Kristensen, M.1    Planchot, V.2    Abe, J.I.3    Svensson, B.4
  • 31
    • 0031608474 scopus 로고    scopus 로고
    • High cell-density fermentation
    • Higgings D.R., and Cregg J.M. (Eds), Humana Press, Inc., Totowa, NJ
    • Stratton J., Chiruvolu V., and Meager M. High cell-density fermentation. In: Higgings D.R., and Cregg J.M. (Eds). Pichia Protocols. Methods in Molecular Biology (1998), Humana Press, Inc., Totowa, NJ 107-120
    • (1998) Pichia Protocols. Methods in Molecular Biology , pp. 107-120
    • Stratton, J.1    Chiruvolu, V.2    Meager, M.3
  • 33
    • 0027113459 scopus 로고
    • Measurement of the content of limit dextrinase in cereal flours
    • McCleary B.V. Measurement of the content of limit dextrinase in cereal flours. Carbohydr. Res. 227 (1992) 257-268
    • (1992) Carbohydr. Res. , vol.227 , pp. 257-268
    • McCleary, B.V.1
  • 34
    • 0025766291 scopus 로고
    • Miniaturizing of 3 carbohydrate analyses a microsample plate reader
    • Fox J.D., and Robyt J.F. Miniaturizing of 3 carbohydrate analyses a microsample plate reader. Anal. Biochem. 195 (1991) 93-96
    • (1991) Anal. Biochem. , vol.195 , pp. 93-96
    • Fox, J.D.1    Robyt, J.F.2
  • 36
    • 0033057707 scopus 로고    scopus 로고
    • Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry
    • Gobom J., Nordhoff E., Mirgorodskaya E., Ekman R., and Roepstorff P. Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry. J. Mass Spectrom. 34 (1999) 105-116
    • (1999) J. Mass Spectrom. , vol.34 , pp. 105-116
    • Gobom, J.1    Nordhoff, E.2    Mirgorodskaya, E.3    Ekman, R.4    Roepstorff, P.5
  • 37
    • 0024509811 scopus 로고
    • Amino-acid analysis-determination of cysteine plus half-cystine in proteins after hydrochloric-acid hydrolysis with a disulfide compound as additive
    • Barkholt V., and Jensen A.L. Amino-acid analysis-determination of cysteine plus half-cystine in proteins after hydrochloric-acid hydrolysis with a disulfide compound as additive. Anal. Biochem. 177 (1989) 318-322
    • (1989) Anal. Biochem. , vol.177 , pp. 318-322
    • Barkholt, V.1    Jensen, A.L.2
  • 39
    • 34547657101 scopus 로고    scopus 로고
    • Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: biological implications for cell wall metabolism
    • Baumann M.J., Eklof J.M., Michel G., Kallas A.M., Teeri T.T., Czjzek M., and Brumer H. Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: biological implications for cell wall metabolism. Plant Cell 19 (2007) 1947-1963
    • (2007) Plant Cell , vol.19 , pp. 1947-1963
    • Baumann, M.J.1    Eklof, J.M.2    Michel, G.3    Kallas, A.M.4    Teeri, T.T.5    Czjzek, M.6    Brumer, H.7
  • 40
    • 0033118394 scopus 로고    scopus 로고
    • Lignocellulose degradation by Phanerochaete chrysosporium: purification and characterization of the main α-galactosidase
    • Brumer H., Sims P.F.G., and Sinnott M.L. Lignocellulose degradation by Phanerochaete chrysosporium: purification and characterization of the main α-galactosidase. Biochem. J. 339 (1999) 43-53
    • (1999) Biochem. J. , vol.339 , pp. 43-53
    • Brumer, H.1    Sims, P.F.G.2    Sinnott, M.L.3
  • 41
    • 0028670148 scopus 로고
    • Comparison of the binding of β-cyclodextrin and α-cyclodextrin and γ-cyclodextrin with pullulanase from Klebsiella pneumoniae as studied by equilibrium and kinetic fluorometry
    • Iwamoto H., Ohno M., Ohmori M., Hirose J., Tanaka A., Sakai S., and Hiromi K. Comparison of the binding of β-cyclodextrin and α-cyclodextrin and γ-cyclodextrin with pullulanase from Klebsiella pneumoniae as studied by equilibrium and kinetic fluorometry. J. Biochem. 116 (1994) 1264-1268
    • (1994) J. Biochem. , vol.116 , pp. 1264-1268
    • Iwamoto, H.1    Ohno, M.2    Ohmori, M.3    Hirose, J.4    Tanaka, A.5    Sakai, S.6    Hiromi, K.7
  • 42
    • 0000573870 scopus 로고    scopus 로고
    • Modelling the contribution of alpha-amylase, beta-amylase and limit dextrinase to starch degradation during mashing
    • MacGregor A.W., Bazin S.L., Macri L.J., and Babb J.V. Modelling the contribution of alpha-amylase, beta-amylase and limit dextrinase to starch degradation during mashing. J. Cereal Sci. 29 (1999) 161-169
    • (1999) J. Cereal Sci. , vol.29 , pp. 161-169
    • MacGregor, A.W.1    Bazin, S.L.2    Macri, L.J.3    Babb, J.V.4
  • 43
    • 0344154423 scopus 로고    scopus 로고
    • Limit dextrinase in barley cultivars of differing malting quality: activity, inhibitors and limit dextrin profiles
    • Ross H.A., Sungurtas J., Ducreux L., Swanston J.S., Davies H.V., and McDougall G.J. Limit dextrinase in barley cultivars of differing malting quality: activity, inhibitors and limit dextrin profiles. J. Cereal Sci. 38 (2003) 325-334
    • (2003) J. Cereal Sci. , vol.38 , pp. 325-334
    • Ross, H.A.1    Sungurtas, J.2    Ducreux, L.3    Swanston, J.S.4    Davies, H.V.5    McDougall, G.J.6
  • 45
    • 2942627936 scopus 로고    scopus 로고
    • Temperature limited fed-batch technique for control of proteolysis in Pichia pastoris bioreactor cultures
    • Jahic M., Wallberg F., Bollok M., Garcia P., and Enfors S. Temperature limited fed-batch technique for control of proteolysis in Pichia pastoris bioreactor cultures. Microb. Cell Fact. 2 (2003) 1-11
    • (2003) Microb. Cell Fact. , vol.2 , pp. 1-11
    • Jahic, M.1    Wallberg, F.2    Bollok, M.3    Garcia, P.4    Enfors, S.5
  • 46
    • 0033809942 scopus 로고    scopus 로고
    • Expression of recombinant galactose oxidase by Pichia pastoris
    • Whittaker M.M., and Whittaker J.W. Expression of recombinant galactose oxidase by Pichia pastoris. Protein Expr. Purif. 20 (2000) 105-111
    • (2000) Protein Expr. Purif. , vol.20 , pp. 105-111
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 47
    • 2942584928 scopus 로고    scopus 로고
    • Increasing secretion of a bivalent anti-T-cell immunotoxin by Pichia pastoris
    • Woo J.H., Liu Y.Y., Stavrou S., and Neville D.M. Increasing secretion of a bivalent anti-T-cell immunotoxin by Pichia pastoris. Appl. Environ. Microbiol. 70 (2004) 3370-3376
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3370-3376
    • Woo, J.H.1    Liu, Y.Y.2    Stavrou, S.3    Neville, D.M.4
  • 49
    • 0003149025 scopus 로고
    • Barley malt limit dextrinase-its extraction, heat-stability, and activity during malting and mashing
    • Sissons M., Taylor M., and Proudlove M. Barley malt limit dextrinase-its extraction, heat-stability, and activity during malting and mashing. J. Am. Soc. Brew. Chem. 53 (1995) 104-110
    • (1995) J. Am. Soc. Brew. Chem. , vol.53 , pp. 104-110
    • Sissons, M.1    Taylor, M.2    Proudlove, M.3
  • 50
    • 0000955950 scopus 로고
    • Limit dextrinase from malted barley: extraction, purification and characterization
    • MacGregor A.W., Macri L.J., Schroeder S.W., and Bazin S.L. Limit dextrinase from malted barley: extraction, purification and characterization. Cereal Chem. 71 (1994) 610-617
    • (1994) Cereal Chem. , vol.71 , pp. 610-617
    • MacGregor, A.W.1    Macri, L.J.2    Schroeder, S.W.3    Bazin, S.L.4
  • 51
    • 1442291031 scopus 로고    scopus 로고
    • Limit dextrinase from germinating barley has endotransglycosylase activity, which explains its activation by maltodextrins
    • McDougall G.J., Ross H.A., Swanston J.S., and Davies H.V. Limit dextrinase from germinating barley has endotransglycosylase activity, which explains its activation by maltodextrins. Planta 218 (2004) 542-551
    • (2004) Planta , vol.218 , pp. 542-551
    • McDougall, G.J.1    Ross, H.A.2    Swanston, J.S.3    Davies, H.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.