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Volumn 233, Issue 1, 2004, Pages 53-64

Cloning and expression of Lipomyces starkeyi α-amylase in Escherichia coli and determination of some of its properties

Author keywords

amylase; Cloning; Expression; Lipomyces starkeyi

Indexed keywords

ACARBOSE; AMINO ACID; AMYLASE; CALCIUM ION; COMPLEMENTARY DNA; COPPER ION; DEXTRANASE; DNA FRAGMENT; EDETIC ACID; EGTAZIC ACID; ENZYME ANTIBODY; FUNGAL ENZYME; MAGNESIUM ION; MALTODEXTRIN; MUTANT PROTEIN; NUCLEOTIDE; POLYACRYLAMIDE GEL; STARCH;

EID: 1642384434     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsle.2004.01.036     Document Type: Article
Times cited : (29)

References (45)
  • 1
    • 0029361087 scopus 로고
    • Enzyme and microbial systems involved in starch processing
    • Nigam P., Singh P. Enzyme and microbial systems involved in starch processing. Enzyme Microbial. Technol. 17:1995;770-778.
    • (1995) Enzyme Microbial. Technol. , vol.17 , pp. 770-778
    • Nigam, P.1    Singh, P.2
  • 2
    • 0002622145 scopus 로고
    • Conversion of starch by yeasts
    • H. Verachtert, & R. De Mot. New York: Marcel Dekker
    • De Mot R. Conversion of starch by yeasts. Verachtert H., De Mot R. Yeast: biotechnology and biocatalysis. 1990;163-221 Marcel Dekker, New York.
    • (1990) Yeast: Biotechnology and Biocatalysis , pp. 163-221
    • De Mot, R.1
  • 4
    • 0024971034 scopus 로고
    • The purification and characterization of a dextranase from Lipomyces starkeyi
    • Koenig D.W., Day D.F. The purification and characterization of a dextranase from Lipomyces starkeyi. Eur. J. Biochem. 183:1989;161-167.
    • (1989) Eur. J. Biochem. , vol.183 , pp. 161-167
    • Koenig, D.W.1    Day, D.F.2
  • 5
    • 0042647722 scopus 로고    scopus 로고
    • Lipomyces Loder et Kreger-van Rij
    • N.J.W. Kreger-van Rij. Amsterdam: Elsevier Science Publishers
    • Phaff H.J., Kurtzman C.P. Lipomyces Loder et Kreger-van Rij. Kreger-van Rij N.J.W. The yeasts, a taxonomic study. 1996;252-260 Elsevier Science Publishers, Amsterdam.
    • (1996) The Yeasts, a Taxonomic Study , pp. 252-260
    • Phaff, H.J.1    Kurtzman, C.P.2
  • 6
    • 0033694563 scopus 로고    scopus 로고
    • Amylolytic enzymes of Lipomyces starkeyi: Purification and size-determination
    • Bignell G.R., Bruce I.J., Evans I.H. Amylolytic enzymes of Lipomyces starkeyi: purification and size-determination. Biotechol. Lett. 22:2000;1713-1718.
    • (2000) Biotechol. Lett. , vol.22 , pp. 1713-1718
    • Bignell, G.R.1    Bruce, I.J.2    Evans, I.H.3
  • 7
    • 0020501528 scopus 로고
    • Selection of yeast for single cell protein production on media based on Jerusalem artichoke extracts
    • Apaire V., Guiraud J.P., Galzy P. Selection of yeast for single cell protein production on media based on Jerusalem artichoke extracts. Z. Allg. Mikribiol. 23:1983;211-218.
    • (1983) Z. Allg. Mikribiol. , vol.23 , pp. 211-218
    • Apaire, V.1    Guiraud, J.P.2    Galzy, P.3
  • 8
    • 0032767795 scopus 로고    scopus 로고
    • Characterization of a novel carbohydrase from Lipomyces starkeyi KSM 22 for dental application
    • Kim D., Ryu S.J., Heo S.J., Kim D.W., Kim H.S. Characterization of a novel carbohydrase from Lipomyces starkeyi KSM 22 for dental application. J. Microbiol. Biotechnol. 9:1999;260-264.
    • (1999) J. Microbiol. Biotechnol. , vol.9 , pp. 260-264
    • Kim, D.1    Ryu, S.J.2    Heo, S.J.3    Kim, D.W.4    Kim, H.S.5
  • 9
    • 0028518896 scopus 로고
    • A new process for the production of clinical dextran by mixed-culture fermentation of Lipomyces starkeyi and Leuconostoc mesenteroides
    • Kim D., Day D.F. A new process for the production of clinical dextran by mixed-culture fermentation of Lipomyces starkeyi and Leuconostoc mesenteroides. Enzyme Microbial. Technol. 16:1994;844-848.
    • (1994) Enzyme Microbial. Technol. , vol.16 , pp. 844-848
    • Kim, D.1    Day, D.F.2
  • 11
    • 0027450658 scopus 로고
    • A new way of producing isomalto-oligosaccharide syrup by using the transglycosylation reaction of neopullulanase
    • Kuriki T., Yanase M., Takata H., Takesada Y., Imanaka T., Okada S. A new way of producing isomalto-oligosaccharide syrup by using the transglycosylation reaction of neopullulanase. Appl. Environ. Microbiol. 59:1993;953-959.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 953-959
    • Kuriki, T.1    Yanase, M.2    Takata, H.3    Takesada, Y.4    Imanaka, T.5    Okada, S.6
  • 12
    • 0029885397 scopus 로고    scopus 로고
    • Molecular cloning and determination of the Nucleotide Sequence of a gene encoding an acid-stable α-amylase from Aspergillus kawachii
    • Kaneko A., Sudo S., Takayasu-Sakamoto Y., Tamura G., Ishikawa T., Oba T. Molecular cloning and determination of the Nucleotide Sequence of a gene encoding an acid-stable α-amylase from Aspergillus kawachii. J. Ferment. Bioengineer. 81:1996;292-298.
    • (1996) J. Ferment. Bioengineer. , vol.81 , pp. 292-298
    • Kaneko, A.1    Sudo, S.2    Takayasu-Sakamoto, Y.3    Tamura, G.4    Ishikawa, T.5    Oba, T.6
  • 13
    • 0027220264 scopus 로고
    • Expression of Aspergillus oryzae α-amylase gene in Saccharomyces cerevisiae
    • Randez-Gil F., Sanz P. Expression of Aspergillus oryzae α-amylase gene in Saccharomyces cerevisiae. FEMS Microbiol. Lett. 112:1993;119-124.
    • (1993) FEMS Microbiol. Lett. , vol.112 , pp. 119-124
    • Randez-Gil, F.1    Sanz, P.2
  • 14
    • 0026548763 scopus 로고
    • Nucleotide sequence of the extracellular α-amylase gene in the yeast Schwanniomyces occidentailis ATCC 26077
    • Park J.C., Bai S., Tai C.Y., Chun S.B. Nucleotide sequence of the extracellular α-amylase gene in the yeast Schwanniomyces occidentailis ATCC 26077. FEMS Microbiol. Lett. 93:1992;17-24.
    • (1992) FEMS Microbiol. Lett. , vol.93 , pp. 17-24
    • Park, J.C.1    Bai, S.2    Tai, C.Y.3    Chun, S.B.4
  • 15
    • 0028884418 scopus 로고
    • Cloning, sequence analysis and expression in yeasts of a cDNA containing a Lipomyces kononenkoae α-amylase-encoding gene
    • Steyn A.J.C., Marmur J., Pretorius I.S. Cloning, sequence analysis and expression in yeasts of a cDNA containing a Lipomyces kononenkoae α-amylase-encoding gene. Gene. 166:1995;65-71.
    • (1995) Gene , vol.166 , pp. 65-71
    • Steyn, A.J.C.1    Marmur, J.2    Pretorius, I.S.3
  • 16
    • 0346908614 scopus 로고    scopus 로고
    • Molecular cloning: A laboratory manual
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • Sambrook J., Russell D.W. Molecular cloning: a laboratory manual. 3rd ed. 2001;Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
    • (2001) 3rd Ed.
    • Sambrook, J.1    Russell, D.W.2
  • 17
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for the determination of reducing sugars
    • Miller C.L. Use of dinitrosalicylic acid reagent for the determination of reducing sugars. Anal. Chem. 31:1959;426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, C.L.1
  • 18
    • 0029794038 scopus 로고    scopus 로고
    • Simplified an improved methylation analysis of saccharides, using a modified procedure and thin-layer chromatography
    • Mukerjea R., Kim D., Robyt J.F. Simplified an improved methylation analysis of saccharides, using a modified procedure and thin-layer chromatography. Carbohydr. Res. 292:1996;11-20.
    • (1996) Carbohydr. Res. , vol.292 , pp. 11-20
    • Mukerjea, R.1    Kim, D.2    Robyt, J.F.3
  • 19
    • 0021153574 scopus 로고
    • Separation of yeast chromosome-sized DNAs by pulsed filed gel electrophoresis
    • Schwartz D.C., Cantor C.R. Separation of yeast chromosome-sized DNAs by pulsed filed gel electrophoresis. Cell. 37:1984;67-75.
    • (1984) Cell , vol.37 , pp. 67-75
    • Schwartz, D.C.1    Cantor, C.R.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmi U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmi, U.K.1
  • 21
    • 0242659251 scopus 로고    scopus 로고
    • Directed evolution of a dextransucrase for increased constitutive activity and the synthesis of a highly branched dextran
    • Kang H.K., Seo E.S., Robyt J.F., Kim D. Directed evolution of a dextransucrase for increased constitutive activity and the synthesis of a highly branched dextran. J. Mol. Cat. B: Enzymatic. 26:2003;167-176.
    • (2003) J. Mol. Cat. B: Enzymatic , vol.26 , pp. 167-176
    • Kang, H.K.1    Seo, E.S.2    Robyt, J.F.3    Kim, D.4
  • 22
    • 0028860703 scopus 로고
    • Characterization of a novel α-amylase from Lipomyces kononenkoae expression of its gene (LKA1) in Saccharomyces cerevisiae
    • Steyn A.J.C., Pretorius I.S. Characterization of a novel α-amylase from Lipomyces kononenkoae expression of its gene (LKA1) in Saccharomyces cerevisiae. Curr. Genet. 28:1995;526-533.
    • (1995) Curr. Genet. , vol.28 , pp. 526-533
    • Steyn, A.J.C.1    Pretorius, I.S.2
  • 23
    • 0033044637 scopus 로고    scopus 로고
    • Machine learning approaches for the prediction of signal peptides and other protein sorting signals
    • Nielsen H., Brunak S., von Heijne G. Machine learning approaches for the prediction of signal peptides and other protein sorting signals. Prot. Eng. 12:1999;3-9.
    • (1999) Prot. Eng. , vol.12 , pp. 3-9
    • Nielsen, H.1    Brunak, S.2    Von Heijne, G.3
  • 24
    • 0023666444 scopus 로고
    • Nucleotide sequence of the α-amylase gene (ALP1) in the yeast Saccharomycopsis fibuligera
    • Ito T., Yamashita I., Fukui S. Nucleotide sequence of the α-amylase gene (ALP1) in the yeast Saccharomycopsis fibuligera. FEBS Lett. 219:1987;339-342.
    • (1987) FEBS Lett. , vol.219 , pp. 339-342
    • Ito, T.1    Yamashita, I.2    Fukui, S.3
  • 25
    • 0037438660 scopus 로고    scopus 로고
    • Cloning and characterization of a second α-amylase gene (LKA2) from Lipomyces kononenkoae IGC4052B and its expression in Saccharomyces cerevisiae
    • Eksteen J.M., Steyn A.J.C., Rensburg P., Otero R.R.C. Cloning and characterization of a second α-amylase gene (LKA2) from Lipomyces kononenkoae IGC4052B and its expression in Saccharomyces cerevisiae. Yeast. 20:2003;69-78.
    • (2003) Yeast , vol.20 , pp. 69-78
    • Eksteen, J.M.1    Steyn, A.J.C.2    Rensburg, P.3    Otero, R.R.C.4
  • 26
    • 0021801196 scopus 로고
    • Thermostable extracellular α-amylase and α-glucosidase of Lipomyces starkeyi
    • Kelly C.T., Moriarty M.E., Fogarty W.M. Thermostable extracellular α-amylase and α-glucosidase of Lipomyces starkeyi. Appl. Microbiol. Biotechnol. 22:1985;352-358.
    • (1985) Appl. Microbiol. Biotechnol. , vol.22 , pp. 352-358
    • Kelly, C.T.1    Moriarty, M.E.2    Fogarty, W.M.3
  • 27
    • 0023683574 scopus 로고    scopus 로고
    • Molecular cloning and nucleotide sequence of the cyclomaltodextrin glucanotransferase gene from the alkalophilic Bacillus sp. Strain no. 38-2
    • Kaneko T., Hamamoto T., Horikoshi K. Molecular cloning and nucleotide sequence of the cyclomaltodextrin glucanotransferase gene from the alkalophilic Bacillus sp. Strain no. 38-2. J. Gen. Microbiol. 134:1998;97-105.
    • (1998) J. Gen. Microbiol. , vol.134 , pp. 97-105
    • Kaneko, T.1    Hamamoto, T.2    Horikoshi, K.3
  • 28
    • 0023234645 scopus 로고
    • Cloning and nucleotide sequence of the gene coding for enzymatically active fragments of the Bacillus polymyxa beta-amylase
    • Kawazu T., Nakanishi Y., Uozumi N., Sasaki T., Yamagata H., Tsukagoshi N., Udaka S. Cloning and nucleotide sequence of the gene coding for enzymatically active fragments of the Bacillus polymyxa beta-amylase. J. Bacteriol. 169:1987;1564-1570.
    • (1987) J. Bacteriol. , vol.169 , pp. 1564-1570
    • Kawazu, T.1    Nakanishi, Y.2    Uozumi, N.3    Sasaki, T.4    Yamagata, H.5    Tsukagoshi, N.6    Udaka, S.7
  • 29
    • 0021964980 scopus 로고
    • Cloning of the pullulanase gene and overproduction of pullulanase in Escherichia coli and Klebsiella aerogenes
    • Takizawa N., Murooka Y. Cloning of the pullulanase gene and overproduction of pullulanase in Escherichia coli and Klebsiella aerogenes. Appl. Environ. Microbiol. 49:1985;294-298.
    • (1985) Appl. Environ. Microbiol. , vol.49 , pp. 294-298
    • Takizawa, N.1    Murooka, Y.2
  • 30
    • 0001785242 scopus 로고
    • A new concept of the criteria for classification of various amylolytic enzymes and related enzymes; Similarities in specificities and structures
    • Y. Takehiko. Boca Raton, FL: CRC Press
    • Kuriki T., Okada S. A new concept of the criteria for classification of various amylolytic enzymes and related enzymes; similarities in specificities and structures. Takehiko Y. Enzyme chemistry and molecular biology of amylases and related enzymes. 1995;87-92 CRC Press, Boca Raton, FL.
    • (1995) Enzyme Chemistry and Molecular Biology of Amylases and Related Enzymes , pp. 87-92
    • Kuriki, T.1    Okada, S.2
  • 31
    • 0033112356 scopus 로고    scopus 로고
    • Characterization of the Bacillus mar cerans cyclodextrin glucanotransferase overexpressed in Escherichia coli
    • Jeang C.L., Wung C.H., Chang B.Y., Yeh S.S., Lour D.W. Characterization of the Bacillus mar cerans cyclodextrin glucanotransferase overexpressed in Escherichia coli. Proc. Natl. Sci. Counc. Repub. China B. 23:1999;62-68.
    • (1999) Proc. Natl. Sci. Counc. Repub. China B , vol.23 , pp. 62-68
    • Jeang, C.L.1    Wung, C.H.2    Chang, B.Y.3    Yeh, S.S.4    Lour, D.W.5
  • 32
    • 0029770112 scopus 로고    scopus 로고
    • Cloning mapping and characterization of a genomic copy of the Lipomyces kononenkoae α-amylase-encoding gene (LKA1)
    • Steyn A.J.C., Marmur J., Pretorius I.S. Cloning mapping and characterization of a genomic copy of the Lipomyces kononenkoae α-amylase-encoding gene (LKA1). Yeast. 12:1996;925-937.
    • (1996) Yeast , vol.12 , pp. 925-937
    • Steyn, A.J.C.1    Marmur, J.2    Pretorius, I.S.3
  • 33
    • 0029740660 scopus 로고    scopus 로고
    • Raw-starch-digesting and thermostable α-amylase from the yeast Cryptococcus sp. S-2: Purification, characterization, cloning and sequencing
    • Iefuji H., Chino M., Kato M., Iimura Y. Raw-starch-digesting and thermostable α-amylase from the yeast Cryptococcus sp. S-2: purification, characterization, cloning and sequencing. Biochem. J. 318:1996;989-996.
    • (1996) Biochem. J. , vol.318 , pp. 989-996
    • Iefuji, H.1    Chino, M.2    Kato, M.3    Iimura, Y.4
  • 34
    • 0026522467 scopus 로고
    • Architectural features of pre-mRNA introns in the fission yeast schizosaccharomyces pombe
    • Prabhala G., Rosenberg G.H., Kaufer N.F. Architectural features of pre-mRNA introns in the fission yeast schizosaccharomyces pombe. Yeast. 8:1992;171-182.
    • (1992) Yeast , vol.8 , pp. 171-182
    • Prabhala, G.1    Rosenberg, G.H.2    Kaufer, N.F.3
  • 35
    • 0024489684 scopus 로고
    • Three α-amylase genes of Aspergillus oryzae exhibit identical intron-exon organization
    • Wirsel W., Lachmund A., Wildhardt G., Ruttowski E. Three α-amylase genes of Aspergillus oryzae exhibit identical intron-exon organization. Mol. Microbiol. 3:1989;3-14.
    • (1989) Mol. Microbiol. , vol.3 , pp. 3-14
    • Wirsel, W.1    Lachmund, A.2    Wildhardt, G.3    Ruttowski, E.4
  • 36
    • 0024763496 scopus 로고
    • Yeast pre-mRNA splicing
    • Woolford J.L. Yeast pre-mRNA splicing. Yeast. 5:1989;439-457.
    • (1989) Yeast , vol.5 , pp. 439-457
    • Woolford, J.L.1
  • 37
    • 0026670431 scopus 로고
    • Interactions of small nuclear RNAs with precursor messenger RNA during in vitro splicing
    • Wasserman D.A., Steitz J.A. Interactions of small nuclear RNAs with precursor messenger RNA during in vitro splicing. Science. 257:1992;1918-1925.
    • (1992) Science , vol.257 , pp. 1918-1925
    • Wasserman, D.A.1    Steitz, J.A.2
  • 38
    • 0028233256 scopus 로고
    • Fission yeast gene structure and recognition
    • Zhang M.Q., Marr T.G. Fission yeast gene structure and recognition. Nucl. Acids Res. 22:1994;1750-1759.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 1750-1759
    • Zhang, M.Q.1    Marr, T.G.2
  • 39
    • 1642274367 scopus 로고    scopus 로고
    • Properties of carbohydrase prepared from Lipomyces starkeyi JLC26
    • Jun S.M., Kim D., Kim D.W. Properties of carbohydrase prepared from Lipomyces starkeyi JLC26. Korean J. Biotechnol. Bioeng. 14:1999;713-717.
    • (1999) Korean J. Biotechnol. Bioeng. , vol.14 , pp. 713-717
    • Jun, S.M.1    Kim, D.2    Kim, D.W.3
  • 40
  • 41
    • 0024971705 scopus 로고
    • The calcium requirement for stability and enzymatic activity of two isoforms of barley aleuron α-amylase
    • Bush D.S., Sticher L., Hwystee R.V., Wegner D., Jones R.L. The calcium requirement for stability and enzymatic activity of two isoforms of barley aleuron α-amylase. J. Biol. Chem. 264:1989;19392-19398.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19392-19398
    • Bush, D.S.1    Sticher, L.2    Hwystee, R.V.3    Wegner, D.4    Jones, R.L.5
  • 43
    • 0031827710 scopus 로고    scopus 로고
    • Acarbose effect for dextran synthesis, acceptor and disproportionation reactions of Leuconostoc mesenteroides B-512FMCM dextransucrase
    • Kim D., Park K.H., Robyt J.F. Acarbose effect for dextran synthesis, acceptor and disproportionation reactions of Leuconostoc mesenteroides B-512FMCM dextransucrase. J. Microbiol. Biotechnol. 8:1998;287-290.
    • (1998) J. Microbiol. Biotechnol. , vol.8 , pp. 287-290
    • Kim, D.1    Park, K.H.2    Robyt, J.F.3
  • 44
    • 0029953633 scopus 로고    scopus 로고
    • Crystal structure of pig pancreatic α-amylase isoenzyme II in complex with carbohydrate inhibitor acarbose
    • Gilles C., Astier J.P., Marchis-Mouren G., Cambillan C., Payan F. Crystal structure of pig pancreatic α-amylase isoenzyme II in complex with carbohydrate inhibitor acarbose. Eur. J. Biochem. 238:1996;561-569.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 561-569
    • Gilles, C.1    Astier, J.P.2    Marchis-Mouren, G.3    Cambillan, C.4    Payan, F.5
  • 45
    • 0029957475 scopus 로고    scopus 로고
    • The mechanism of porcine pancreatic α-amylase. Kinetic evidence for two additional carbohydrate-binding sites
    • Al Kazaz M., Desseaux V., Marchis-Mouren G., Payan F., Eorest E., Santimore M. The mechanism of porcine pancreatic α-amylase. Kinetic evidence for two additional carbohydrate-binding sites. Eur. J. Biochem. 241:1996;787-796.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 787-796
    • Al Kazaz, M.1    Desseaux, V.2    Marchis-Mouren, G.3    Payan, F.4    Eorest, E.5    Santimore, M.6


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