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Volumn 63, Issue 9, 1999, Pages 1535-1540

Thermostabilization by Proline Substitution in an Alkaline, Liquefying α-Amylase from Bacillus sp. Strain KSM-1378

Author keywords

Alkaliphile; Bacillus; Site directed mutagenesis; Thermostability; amylase

Indexed keywords

AMYLASE; PRIMER DNA; PROLINE;

EID: 0033192099     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.1535     Document Type: Article
Times cited : (26)

References (37)
  • 1
    • 0002195786 scopus 로고    scopus 로고
    • Application of amylases in detergents
    • “, ”, eds. van Ee, J. H., Misset, O., and Baars, E. J., Marcel Decker, Inc., New York
    • UpaDek, H. and Kottwitz, B., Application of amylases in detergents. In “Enzymes in Detergency”, eds. van Ee, J. H., Misset, O., and Baars, E. J., Marcel Decker, Inc., New York, pp. 203-212 (1997).
    • (1997) Enzymes in Detergency , pp. 203-212
    • Upadek, H.1    Kottwitz, B.2
  • 2
    • 0001763247 scopus 로고
    • Purification and some properties of an alkaline pullulanase from alkalophilic Bacillus sp. KSM-1876
    • Ara, K., Igarashi, K., Saeki, K., Kawai, S., and Ito, S., Purification and some properties of an alkaline pullulanase from alkalophilic Bacillus sp. KSM-1876. Biosci. Biotechnol. Biochem., 56, 62-65 (1992).
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 62-65
    • Ara, K.1    Igarashi, K.2    Saeki, K.3    Kawai, S.4    Ito, S.5
  • 3
    • 0027189614 scopus 로고
    • Purification and characterization of an alkaline isoamylase from an alkalophilic strain of Bacillus
    • Ara, K., Saeki, K., and Ito, S., Purification and characterization of an alkaline isoamylase from an alkalophilic strain of Bacillus. J. Gen. Microbiol., 139, 781-786 (1994).
    • (1994) J. Gen. Microbiol. , vol.139 , pp. 781-786
    • Ara, K.1    Saeki, K.2    Ito, S.3
  • 4
    • 0026828477 scopus 로고
    • Nucleotide sequence of the gene that encodes a neopul-lulanase from an alkalophilic Bacillus
    • Igarashi, K., Ara, K., Saeki, K., Ozaki, K., Kawai, S., and Ito, S., Nucleotide sequence of the gene that encodes a neopul-lulanase from an alkalophilic Bacillus. Biosci. Biotechnol. Biochem., 56, 514-516 (1992).
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 514-516
    • Igarashi, K.1    Ara, K.2    Saeki, K.3    Ozaki, K.4    Kawai, S.5    Ito, S.6
  • 5
    • 0028904973 scopus 로고
    • Purification and characterization of an alkaline amylopullulanase with both α-1,4 and α-1,6 hydrolytic activity from alkalophilic Bacillus sp. KSM-1378
    • Ara, K., Saeki, K., Igarashi, K., Takaiwa, M., Uemura, T., Hagihara, H., Kawai, S., and Ito, S., Purification and characterization of an alkaline amylopullulanase with both α-1,4 and α-1,6 hydrolytic activity from alkalophilic Bacillus sp. KSM-1378. Biochim. Biophys. Acta, 1243, 315-324 (1995).
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 315-324
    • Ara, K.1    Saeki, K.2    Igarashi, K.3    Takaiwa, M.4    Uemura, T.5    Hagihara, H.6    Kawai, S.7    Ito, S.8
  • 6
    • 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., Kawai, S., Watanabe, T., and Ito, S., 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, 24075-24083 (1996).
    • (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    Kawai, S.7    Watanabe, T.8    Ito, S.9
  • 7
    • 0031129746 scopus 로고    scopus 로고
    • Alkaline cellulases from alkaliphilic Bacillus: Enzymatic properties, genetics, and application to detergents
    • Ito, S., Alkaline cellulases from alkaliphilic Bacillus: Enzymatic properties, genetics, and application to detergents. Ex-tremophiles, 1, 61-66 (1997).
    • (1997) Ex-Tremophiles , vol.1 , pp. 61-66
    • Ito, S.1
  • 10
    • 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, 290-298 (1973).
    • (1973) Arch. Biochem. Biophys. , vol.155 , pp. 290-298
    • Saito, N.1
  • 11
    • 0014136452 scopus 로고
    • Unrelatedness of Bacillus amyloliquefaciens and Bacillus subtilis
    • Welker N. E. and Campbell, L. L., Unrelatedness of Bacillus amyloliquefaciens and Bacillus subtilis. J. Bacteriol., 94, 1124-1130 (1967).
    • (1967) J. Bacteriol. , vol.94 , pp. 1124-1130
    • Welker, N.E.1    Campbell, L.L.2
  • 12
    • 0021348996 scopus 로고
    • Cloning and expression of a thermophilic α-amylase gene from Bacillus stearothermophilus in Escherichia coli
    • Tsukagoshi, N., Ihara, H., Yamagata, H., and Udaka, S., Cloning and expression of a thermophilic α-amylase gene from Bacillus stearothermophilus in Escherichia coli. Mol. Gen. Genet., 193, 58-63 (1984).
    • (1984) Mol. Gen. Genet. , vol.193 , pp. 58-63
    • Tsukagoshi, N.1    Ihara, H.2    Yamagata, H.3    Udaka, S.4
  • 13
    • 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, 281-292 (1998).
    • (1998) Structure , vol.6 , pp. 281-292
    • Machius, M.1    Declerck, N.2    Huber, R.3    Wiegand, G.4
  • 14
    • 0025082333 scopus 로고
    • Use of amber suppressors to investigate the thermostability of Bacillus licheniformis α-amylase
    • Declerck, N., Joyet, P., Gaillardin, C., and Masson, J., Use of amber suppressors to investigate the thermostability of Bacillus licheniformis α-amylase. J. Biol. Chem., 265, 15481-15488 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 15481-15488
    • Declerck, N.1    Joyet, P.2    Gaillardin, C.3    Masson, J.4
  • 15
    • 0027033801 scopus 로고
    • Hyperthermostable variants of highly thermostable Alpha-amylase
    • Joyet, P., Declerck, N., and Gaillardin, C., Hyperthermostable variants of highly thermostable Alpha-amylase. Biotechnology, 10, 1579-1583 (1992).
    • (1992) Biotechnology , vol.10 , pp. 1579-1583
    • Joyet, P.1    Declerck, N.2    Gaillardin, C.3
  • 16
    • 0024795242 scopus 로고
    • Amino acid residues stabilizing a Bacillus α-amylase against irreversible thermoinactivation
    • Suzuki, Y., Ito, N., Yuuki, T., Yamagata, H., and Udaka, S., Amino acid residues stabilizing a Bacillus α-amylase against irreversible thermoinactivation. J. Biol. Chem., 264, 18933-18938 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 18933-18938
    • Suzuki, Y.1    Ito, N.2    Yuuki, T.3    Yamagata, H.4    Udaka, S.5
  • 17
    • 0032551748 scopus 로고    scopus 로고
    • Improved thermostability of a Bacillus α-amylase by deletion of an arginine-glycine residue is caused by enhanced calcium binding
    • Igarashi, K., Hatada, Y., Ikawa, K., Araki, H., Ozawa, T., Kobayashi, T., Kawai, S., and Ito, S., Improved thermostability of a Bacillus α-amylase by deletion of an arginine-glycine residue is caused by enhanced calcium binding. Biochem. Biophys. Res. Commun., 248, 372-377(1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 372-377
    • Igarashi, K.1    Hatada, Y.2    Ikawa, K.3    Araki, H.4    Ozawa, T.5    Kobayashi, T.6    Kawai, S.7    Ito, S.8
  • 18
    • 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. Chem., 31, 426-428 (1959).
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 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, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 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, 619-629 (1963).
    • (1963) Biochim. Biophys. Acta , vol.72 , pp. 619-629
    • Saito, H.1    Miura, K.2
  • 22
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim H. C. and Dolly, J., A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucl. Acids Res., 7, 1513-1523 (1979).
    • (1979) Nucl. Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Dolly, J.2
  • 23
    • 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, 557-580 (1983).
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 24
    • 0018287541 scopus 로고
    • High frequency transformation of Bacillus subtilis protoplasts by plasmid DNA
    • Chang S. and Cohen, S. N., High frequency transformation of Bacillus subtilis protoplasts by plasmid DNA. Mol. Gen. Genet., 168, 111-115 (1979).
    • (1979) Mol. Gen. Genet. , vol.168 , pp. 111-115
    • Chang, S.1    Cohen, S.N.2
  • 25
    • 0026873299 scopus 로고
    • Nucleotide sequence of the gene for an alkaline endoglucanase from an alkalophilic Bacillus and its expression in Escherichia coli and Bacillus subtilis
    • Sumitomo, N., Ozaki, K., Kawai, S., and Ito, S., Nucleotide sequence of the gene for an alkaline endoglucanase from an alkalophilic Bacillus and its expression in Escherichia coli and Bacillus subtilis. Biosci. Biotechnol. Biochem., 56, 872-877(1992).
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 872-877
    • Sumitomo, N.1    Ozaki, K.2    Kawai, S.3    Ito, S.4
  • 26
    • 0029400980 scopus 로고
    • Application of the upstream region of a Bacillus endoglucanase gene to high-level expression of foreign genes in Bacillus subtilis
    • Sumitomo, N., Ozaki, K., Hitomi, J., Kawaminami, S., Kobayashi, T., Kawai, S., and Ito, S., Application of the upstream region of a Bacillus endoglucanase gene to high-level expression of foreign genes in Bacillus subtilis. Biosci. Biotechnol. Biochem., 59, 2172-2175 (1995).
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 2172-2175
    • Sumitomo, N.1    Ozaki, K.2    Hitomi, J.3    Kawaminami, S.4    Kobayashi, T.5    Kawai, S.6    Ito, S.7
  • 28
    • 0023834870 scopus 로고
    • Mechanisms of irreversible thermal inactivation of Bacillus α-amylases
    • Tomazic, S. J. and Klibanov A. M., Mechanisms of irreversible thermal inactivation of Bacillus α-amylases. J. Biol. Chem., 263, 3086-3091 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 3086-3091
    • Tomazic, S.J.1    Klibanov, A.M.2
  • 29
    • 0030986231 scopus 로고    scopus 로고
    • Hyperthermostable mutants of Bacillus licheniformis α-amylase: Thermodynamic studies and structural interpretation
    • Declerck, N., Machius, M., Chambert, R., Wiegand, G., Huber, R., and Gaillardin, C., Hyperthermostable mutants of Bacillus licheniformis α-amylase: thermodynamic studies and structural interpretation. Protein Eng., 10, 541-549 (1997).
    • (1997) Protein Eng. , vol.10 , pp. 541-549
    • Declerck, N.1    Machius, M.2    Chambert, R.3    Wiegand, G.4    Huber, R.5    Gaillardin, C.6
  • 30
    • 85024418791 scopus 로고
    • A general principle of increasing protein thermostability
    • Suzuki, Y., A general principle of increasing protein thermostability. Proc. Jpn. Acad. Ser. B Phys. Biol. Sci., 65, 146-148 (1989).
    • (1989) Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. , vol.65 , pp. 146-148
    • Suzuki, Y.1
  • 31
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutation that decrease the entropy of unfolding
    • Matthews, B. W., Nicholson, H., and Becktel, W. J., Enhanced protein thermostability from site-directed mutation that decrease the entropy of unfolding. Proc. Natl. Acad. Sci. USA, 84, 6663-6667 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 32
    • 0026091723 scopus 로고
    • Effects of proline mutation on the unfolding and refolding of human lysozyme: The slow refolding kinetic phase does not result from proline cis-trans isomerization
    • Herning, T., Yutani, K., Taniyama, Y., and Kikuchi, M., Effects of proline mutation on the unfolding and refolding of human lysozyme: the slow refolding kinetic phase does not result from proline cis-trans isomerization. Biochemistry, 30, 9882-9891 (1991).
    • (1991) Biochemistry , vol.30 , pp. 9882-9891
    • Herning, T.1    Yutani, K.2    Taniyama, Y.3    Kikuchi, M.4
  • 33
    • 0027410087 scopus 로고
    • Stabilization of Bacillus stearothermophilus neutral protease by introduction of prolines
    • Hardy, F., Vriend, G., Veltman, O. R., van der Vinne, B., Venema, G., and Eijsink, V. G. H., Stabilization of Bacillus stearothermophilus neutral protease by introduction of prolines. FEBS Lett., 317, 89-92 (1993).
    • (1993) FEBS Lett. , vol.317 , pp. 89-92
    • Hardy, F.1    Vriend, G.2    Veltman, O.R.3    Van Der Vinne, B.4    Venema, G.5    Eijsink, V.G.H.6
  • 34
    • 0027994512 scopus 로고
    • Stabilization and rational design of serine protease AprM under highly alkaline and high-temperature conditions
    • Matsui, A., Fujiwara, N., and Imanaka, T., Stabilization and rational design of serine protease AprM under highly alkaline and high-temperature conditions. Appl. Environ. Microbiol., 60, 3579-3584 (1994).
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3579-3584
    • Matsui, A.1    Fujiwara, N.2    Imanaka, T.3
  • 35
    • 0029318605 scopus 로고
    • Increase in thermostability of recombinant barley /1-amylase by random mutagenesis
    • Okada, Y., Yoshigi, N., Sahara, H., and Koshino, S., Increase in thermostability of recombinant barley /1-amylase by random mutagenesis. Biosci. Biotechnol. Biochem., 59,1152-1153(1995).
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 1152-1153
    • Okada, Y.1    Yoshigi, N.2    Sahara, H.3    Koshino, S.4
  • 36
    • 0031468694 scopus 로고    scopus 로고
    • Effect of introducing proline residues on the stability of Aspergillus awamori
    • Li, Y., Reilly, P. J., and Ford, C., Effect of introducing proline residues on the stability of Aspergillus awamori. Protein Eng., 10, 1199-1204(1997).
    • (1997) Protein Eng. , vol.10 , pp. 1199-1204
    • Li, Y.1    Reilly, P.J.2    Ford, C.3
  • 37
    • 0028130117 scopus 로고
    • Multiple proline substitutions cumulatively ther-mostabilize Bacillus cereus ATCC 7064 oligo-l,6-glucosidase
    • Watanabe, K., Masuda, T., Ohashi, H., Mihara, H., and Suzuki, Y., Multiple proline substitutions cumulatively ther-mostabilize Bacillus cereus ATCC 7064 oligo-l,6-glucosidase. Eur. J. Biochem., 226, 277-283 (1994).
    • (1994) Eur. J. Biochem. , vol.226 , pp. 277-283
    • Watanabe, K.1    Masuda, T.2    Ohashi, H.3    Mihara, H.4    Suzuki, Y.5


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