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Volumn 39, Issue 6, 2006, Pages 1333-1340

Oxidatively stable maltopentaose-producing α-amylase from a deep-sea Bacillus isolate, and mechanism of its oxidative stability validated by site-directed mutagenesis

Author keywords

Amylase; Bacillus; Deep sea; Homology modeling; Maltopentaose; Oxidative stability; Site directed mutagenesis

Indexed keywords

CARBOHYDRATES; ELECTROPHORESIS; GENES; MICROBIOLOGY; MICROORGANISMS; MUTAGENESIS;

EID: 33747366714     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2006.03.022     Document Type: Article
Times cited : (20)

References (32)
  • 1
    • 84987193611 scopus 로고
    • A novel debranching enzyme for application in the glucose syrup industry
    • Norman B.E. A novel debranching enzyme for application in the glucose syrup industry. Starch/Stärke 34 (1982) 340-346
    • (1982) Starch/Stärke , vol.34 , pp. 340-346
    • Norman, B.E.1
  • 2
    • 0002195786 scopus 로고    scopus 로고
    • Application of amylases in detergents
    • van Ee J.H., Misset O., and Baas E.J. (Eds), Marcel Dekker Inc., New York
    • UpaDek H., and Kottwitz B. Application of amylases in detergents. In: van Ee J.H., Misset O., and Baas E.J. (Eds). Enzymes in detergency (1997), Marcel Dekker Inc., New York 203-212
    • (1997) Enzymes in detergency , pp. 203-212
    • UpaDek, H.1    Kottwitz, B.2
  • 3
    • 0032712358 scopus 로고    scopus 로고
    • Alkaliphiles: some applications of their products for biotechnology
    • Horikoshi K. Alkaliphiles: some applications of their products for biotechnology. Microbiol Mol Biol Rev 63 (1999) 735-750
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 735-750
    • Horikoshi, K.1
  • 4
    • 0015606538 scopus 로고
    • A thermophilic extracellular α-amylase from Bacillus licheniformis
    • Saito N. A thermophilic extracellular α-amylase from Bacillus licheniformis. Arch Biochem Biophys 155 (1973) 290-298
    • (1973) Arch Biochem Biophys , vol.155 , pp. 290-298
    • Saito, N.1
  • 5
    • 0022577918 scopus 로고
    • Structural genes encoding the thermophilic alpha-amylases of Bacillus stearothermophilus and Bacillus licheniformis
    • Gray G.L., Mainzer S.E., Rey M.W., Lamsa M.H., Kindle K.L., Carmona C., et al. Structural genes encoding the thermophilic alpha-amylases of Bacillus stearothermophilus and Bacillus licheniformis. J Bacteriol 166 (1986) 635-643
    • (1986) J Bacteriol , vol.166 , pp. 635-643
    • Gray, G.L.1    Mainzer, S.E.2    Rey, M.W.3    Lamsa, M.H.4    Kindle, K.L.5    Carmona, C.6
  • 6
    • 0020691269 scopus 로고
    • Amino acid sequence of α-amylase from Bacillus amyloliquefaciens deduced from the nucleotide sequence of the cloned gene
    • Takkinen K., Pettersson R.F., Kalkkinen N., Palva I., Söderlund H., and Kääriäinen L. Amino acid sequence of α-amylase from Bacillus amyloliquefaciens deduced from the nucleotide sequence of the cloned gene. J Biol Chem 258 (1983) 1007-1013
    • (1983) J Biol Chem , vol.258 , pp. 1007-1013
    • Takkinen, K.1    Pettersson, R.F.2    Kalkkinen, N.3    Palva, I.4    Söderlund, H.5    Kääriäinen, L.6
  • 7
    • 0021837957 scopus 로고
    • Nucleotide sequence of the Bacillus stearothermophilus α-amylase gene
    • Nakajima R., Imanaka T., and Aiba S. Nucleotide sequence of the Bacillus stearothermophilus α-amylase gene. J Bacteriol 163 (1985) 401-406
    • (1985) J Bacteriol , vol.163 , pp. 401-406
    • Nakajima, R.1    Imanaka, T.2    Aiba, S.3
  • 8
    • 0031657848 scopus 로고    scopus 로고
    • Enzymatic properties of a novel liquefying α-amylase from an alkaliphilic Bacillus isolate and entire nucleotide and amino acid sequences
    • Igarashi K., Hatada Y., Hagihara H., Saeki K., Takaiwa M., Uemura T., et al. Enzymatic properties of a novel liquefying α-amylase from an alkaliphilic Bacillus isolate and entire nucleotide and amino acid sequences. Appl Environ Microbiol 64 (1998) 3282-3289
    • (1998) Appl Environ Microbiol , vol.64 , pp. 3282-3289
    • Igarashi, K.1    Hatada, Y.2    Hagihara, H.3    Saeki, K.4    Takaiwa, M.5    Uemura, T.6
  • 9
    • 0036301253 scopus 로고    scopus 로고
    • Cloning of a gene encoding raw-starch-digesting amylase from a Cytophaga sp. and its expression in Escherichia coli
    • Jeang C.L., Chen L.S., Chen M.Y., and Shiau R.J. Cloning of a gene encoding raw-starch-digesting amylase from a Cytophaga sp. and its expression in Escherichia coli. Appl Environ Microbiol 68 (2002) 3651-3654
    • (2002) Appl Environ Microbiol , vol.68 , pp. 3651-3654
    • Jeang, C.L.1    Chen, L.S.2    Chen, M.Y.3    Shiau, R.J.4
  • 10
    • 0028933531 scopus 로고
    • Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution
    • Machius M., Wiegand G., and Huber R. Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution. J Mol Biol 246 (1995) 545-559
    • (1995) J Mol Biol , vol.246 , pp. 545-559
    • Machius, M.1    Wiegand, G.2    Huber, R.3
  • 12
    • 0014670698 scopus 로고
    • The effect on subtilis in activity of oxidizing a methionine residue
    • Stauffer C.E., and Etson D. The effect on subtilis in activity of oxidizing a methionine residue. J Biol Chem 244 (1969) 5333-5338
    • (1969) J Biol Chem , vol.244 , pp. 5333-5338
    • Stauffer, C.E.1    Etson, D.2
  • 13
    • 0020582583 scopus 로고
    • Biochemistry and physiological role of methionine sulfoxide residues in proteins
    • Brot N., and Weissbach H. Biochemistry and physiological role of methionine sulfoxide residues in proteins. Arch Biochem Biophys 223 (1983) 271-281
    • (1983) Arch Biochem Biophys , vol.223 , pp. 271-281
    • Brot, N.1    Weissbach, H.2
  • 14
    • 0021830125 scopus 로고
    • Engineering an enzyme by site-directed mutagenesis to be resistant to chemical oxidation
    • Estell D.A., Graycar T.P., and Wells J.A. Engineering an enzyme by site-directed mutagenesis to be resistant to chemical oxidation. J Biol Chem 260 (1985) 6518-6521
    • (1985) J Biol Chem , vol.260 , pp. 6518-6521
    • Estell, D.A.1    Graycar, T.P.2    Wells, J.A.3
  • 15
    • 13844316356 scopus 로고    scopus 로고
    • Generating oxidation-resistant variants of Bacillus kaustophilus leucine aminopeptidase by substitution of the critical methionine residues with leucine
    • Chi M.C., Chou W.M., Wang C.H., Chen W., Hsu W.H., and Lin L.L. Generating oxidation-resistant variants of Bacillus kaustophilus leucine aminopeptidase by substitution of the critical methionine residues with leucine. Antonie Van Leeuwenhoek 86 (2004) 355-362
    • (2004) Antonie Van Leeuwenhoek , vol.86 , pp. 355-362
    • Chi, M.C.1    Chou, W.M.2    Wang, C.H.3    Chen, W.4    Hsu, W.H.5    Lin, L.L.6
  • 16
    • 2542491250 scopus 로고    scopus 로고
    • Enzyme properties and nucleotide and amino acid sequences of a thermostable β-agarase from a novel species of deep-sea Microbulbifer
    • Ohta Y., Hatada Y., Nogi Y., Miyazaki M., Li Z., Akita M., et al. Enzyme properties and nucleotide and amino acid sequences of a thermostable β-agarase from a novel species of deep-sea Microbulbifer. Appl Microbiol Biotechnol 64 (2004) 505-514
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 505-514
    • Ohta, Y.1    Hatada, Y.2    Nogi, Y.3    Miyazaki, M.4    Li, Z.5    Akita, M.6
  • 17
    • 11244293766 scopus 로고    scopus 로고
    • Cloning expression, and characterization of a glycoside hydrolase family 86 β-agarase from a of deep-sea Microbulbier-like isolate
    • Ohta Y., Hatada Y., Nogi Y., Li Z., Ito S., and Horikoshi K. Cloning expression, and characterization of a glycoside hydrolase family 86 β-agarase from a of deep-sea Microbulbier-like isolate. Appl Microbiol Biotechnol 66 (2004) 266-275
    • (2004) Appl Microbiol Biotechnol , vol.66 , pp. 266-275
    • Ohta, Y.1    Hatada, Y.2    Nogi, Y.3    Li, Z.4    Ito, S.5    Horikoshi, K.6
  • 18
    • 17144381631 scopus 로고    scopus 로고
    • High-level expression of a neoagarobiose-producing β-agarase gene from Agarivorans sp. JAMB-A11 in Bacillus subtilis and enzymic properties of the recombinant enzyme
    • Ohta Y., Hatada Y., Ito S., and Horikoshi K. High-level expression of a neoagarobiose-producing β-agarase gene from Agarivorans sp. JAMB-A11 in Bacillus subtilis and enzymic properties of the recombinant enzyme. Biotechnol Appl Biochem 41 (2005) 183-191
    • (2005) Biotechnol Appl Biochem , vol.41 , pp. 183-191
    • Ohta, Y.1    Hatada, Y.2    Ito, S.3    Horikoshi, K.4
  • 19
    • 20044376314 scopus 로고    scopus 로고
    • Purification and characterization of a novel α-agarase from a Thalassomonas sp.
    • Ohta Y., Hatada Y., Miyazaki M., Nogi Y., Ito S., and Horikoshi K. Purification and characterization of a novel α-agarase from a Thalassomonas sp. Curr Microbiol 50 (2005) 212-216
    • (2005) Curr Microbiol , vol.50 , pp. 212-216
    • Ohta, Y.1    Hatada, Y.2    Miyazaki, M.3    Nogi, Y.4    Ito, S.5    Horikoshi, K.6
  • 20
    • 18844388727 scopus 로고    scopus 로고
    • Maltose phosphorylase from a deep-sea Paenibacillus sp.: enzymatic properties and nucleotide and amino acid sequences.
    • Hidaka Y., Hatada Y., Akita M., Yoshida M., Nakamura N., Takada M., et al. Maltose phosphorylase from a deep-sea Paenibacillus sp.: enzymatic properties and nucleotide and amino acid sequences. Enzyme Microb Technol 37 (2005) 185-194
    • (2005) Enzyme Microb Technol , vol.37 , pp. 185-194
    • Hidaka, Y.1    Hatada, Y.2    Akita, M.3    Yoshida, M.4    Nakamura, N.5    Takada, M.6
  • 21
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Biochem 31 (1959) 426-428
    • (1959) Anal Biochem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli 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
    • Laemmli, U.K.1
  • 23
    • 0029661443 scopus 로고    scopus 로고
    • Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyze α-1,4 and α-1,6 linkages in polysaccharides at different active site
    • Hatada Y., Igarashi K., Ozaki K., Ara K., Hitomi J., Kobayashi T., et al. Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyze α-1,4 and α-1,6 linkages in polysaccharides at different active site. J Biol Chem 271 (1996) 24075-24083
    • (1996) J Biol Chem , vol.271 , pp. 24075-24083
    • Hatada, Y.1    Igarashi, K.2    Ozaki, K.3    Ara, K.4    Hitomi, J.5    Kobayashi, T.6
  • 24
    • 50549178319 scopus 로고
    • Preparation of transforming deoxyribonucleic acid by phenol treatment
    • Saito H., and Miura K. Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochim Biophys Acta 72 (1963) 619-629
    • (1963) Biochim Biophys Acta , vol.72 , pp. 619-629
    • Saito, H.1    Miura, K.2
  • 25
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim H.C., and Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucl Acids Res 7 (1979) 1513-1523
    • (1979) Nucl Acids Res , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 26
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D. Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166 (1983) 557-580
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 27
    • 0016230593 scopus 로고
    • Subsite affinity of bacterial liquefying α-amylase evaluated from the rate parameter of linear substrates
    • Iwasa S., Aoshima H., Hiromi K., and Hatano H. Subsite affinity of bacterial liquefying α-amylase evaluated from the rate parameter of linear substrates. J Biochem 75 (1974) 969-978
    • (1974) J Biochem , vol.75 , pp. 969-978
    • Iwasa, S.1    Aoshima, H.2    Hiromi, K.3    Hatano, H.4
  • 29
    • 0020638192 scopus 로고
    • A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides
    • Perlman D., and Halvorson H.O. A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. J Mol Biol 167 (1983) 391-409
    • (1983) J Mol Biol , vol.167 , pp. 391-409
    • Perlman, D.1    Halvorson, H.O.2
  • 30
    • 0022670999 scopus 로고
    • Comparison of amino acid sequences of eleven different α-amylase
    • Nakajima R., Imanaka T., and Aiba S. Comparison of amino acid sequences of eleven different α-amylase. Appl Microbiol Biotechnol 23 (1986) 355-360
    • (1986) Appl Microbiol Biotechnol , vol.23 , pp. 355-360
    • Nakajima, R.1    Imanaka, T.2    Aiba, S.3
  • 31
    • 0028198814 scopus 로고
    • The active center of a mammalian α-amylase structure of the coplex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2 Å
    • Qian M., Haser R., Buisson G., Duée E., and Payan F. The active center of a mammalian α-amylase structure of the coplex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2 Å. Biochemistry 33 (1994) 6284-6294
    • (1994) Biochemistry , vol.33 , pp. 6284-6294
    • Qian, M.1    Haser, R.2    Buisson, G.3    Duée, E.4    Payan, F.5
  • 32
    • 13144305048 scopus 로고    scopus 로고
    • Activation of Bacillus licheniformis α-amylase through a disorder → order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad
    • Machius M., Declerck N., Huber R., and Wiegand G. Activation of Bacillus licheniformis α-amylase through a disorder → order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad. Structure 6 (1998) 281-292
    • (1998) Structure , vol.6 , pp. 281-292
    • Machius, M.1    Declerck, N.2    Huber, R.3    Wiegand, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.