메뉴 건너뛰기




Volumn 18, Issue 5, 2013, Pages 878-887

Purification and biochemical characterization of a detergent stable α-amylase from Pseudomonas stutzeri AS22

Author keywords

biochemical characterization; detergent industry; G4 amylase; P. stutzeri AS22; PSA; purification

Indexed keywords

ANION EXCHANGE CHROMATOGRAPHY; BIOCHEMICAL CHARACTERIZATION; CULTURE SUPERNATANT; DETERGENT INDUSTRY; N-TERMINAL AMINO ACID SEQUENCE; P. STUTZERI AS22; PSA; PSEUDOMONAS STUTZERI;

EID: 84887109687     PISSN: 12268372     EISSN: 19763816     Source Type: Journal    
DOI: 10.1007/s12257-012-0862-z     Document Type: Article
Times cited : (17)

References (40)
  • 1
    • 35148863942 scopus 로고    scopus 로고
    • Fortified complementary foods with or without alpha amylase treatment increase hemoglobin but do not reduce breast milk intake of 9-mo-old Zambian infants
    • 1:CAS:528:DC%2BD2sXhtFyksL7L
    • Owino, V. O, L. M. Kasonka, M. M. Sinkala, J. K. Wells, S. Eaton, T. Darch, A. Coward, A. M. Tomkins, and S. M. Filteau (2007) Fortified complementary foods with or without alpha amylase treatment increase hemoglobin but do not reduce breast milk intake of 9-mo-old Zambian infants. Am. J. Clin. Nutr. 86: 1094-1103.
    • (2007) Am. J. Clin. Nutr. , vol.86 , pp. 1094-1103
    • Owino, V.O.1    Kasonka, L.M.2    Sinkala, M.M.3    Wells, J.K.4    Eaton, S.5    Darch, T.6    Coward, A.7    Tomkins, A.M.8    Filteau, S.M.9
  • 4
    • 29644437685 scopus 로고    scopus 로고
    • Amylases and their applications
    • 1:CAS:528:DC%2BD28XhsF2rtrg%3D
    • Aiyer, P. V. (2005) Amylases and their applications. Afri. J. Biotechnol. 4: 1525-1529.
    • (2005) Afri. J. Biotechnol. , vol.4 , pp. 1525-1529
    • Aiyer, P.V.1
  • 5
    • 0038301861 scopus 로고    scopus 로고
    • Microbial α-amylase: A biotechnological perspective
    • 10.1016/S0032-9592(03)00053-0 1:CAS:528:DC%2BD3sXkvFGrsLY%3D
    • Gupta, R., P. Gigras, H. Mohapatra, V. K. Goswami, and B. Chauhan (2003) Microbial α-amylase: A biotechnological perspective. Proc. Biochem. 38: 1599-1616.
    • (2003) Proc. Biochem. , vol.38 , pp. 1599-1616
    • Gupta, R.1    Gigras, P.2    Mohapatra, H.3    Goswami, V.K.4    Chauhan, B.5
  • 7
    • 84861715330 scopus 로고    scopus 로고
    • Salt-independent thermophilic α-amylase from Bacillus megaterium VUMB109: An efficacy testing for preparation of maltooligosaccharides
    • 10.1016/j.indcrop.2012.04.048
    • Malabendu, J., M. Chiranjit, S. Saptadip, R. P. Bikas, I. S. Syed, K. D. M. Pradeep, and C. M. Keshab (2013) Salt-independent thermophilic α-amylase from Bacillus megaterium VUMB109: An efficacy testing for preparation of maltooligosaccharides. Ind. Crops. Prod. 41: 386-391.
    • (2013) Ind. Crops. Prod. , vol.41 , pp. 386-391
    • Malabendu, J.1    Chiranjit, M.2    Saptadip, S.3    Bikas, R.P.4    Syed, I.S.5    Pradeep, K.D.M.6    Keshab, C.M.7
  • 8
    • 80054883655 scopus 로고    scopus 로고
    • α-Amylase immobilization on the silica nanoparticles for cleaning performance towards starch soils in laundry detergents
    • 10.1016/j.molcatb.2011.07.011 1:CAS:528:DC%2BC3MXhtlKhsrzP
    • Soleimani, M., A. Khani, and K. Najafzadeh (2012) α-Amylase immobilization on the silica nanoparticles for cleaning performance towards starch soils in laundry detergents. J. Mol. Catal. B: Enzym. 74: 1-5.
    • (2012) J. Mol. Catal. B: Enzym. , vol.74 , pp. 1-5
    • Soleimani, M.1    Khani, A.2    Najafzadeh, K.3
  • 9
    • 64249084104 scopus 로고    scopus 로고
    • Immobilized bacterial α-amylase for effective hydrolysis of raw and soluble starch
    • 10.1016/j.foodres.2009.02.008 1:CAS:528:DC%2BD1MXkslKmsLc%3D
    • Gangadharan, D., K. M. Nampoothiri, S. Sivaramakrishnan, and A. Pandey (2009) Immobilized bacterial α-amylase for effective hydrolysis of raw and soluble starch. Food Res. Int. 42: 436-442.
    • (2009) Food Res. Int. , vol.42 , pp. 436-442
    • Gangadharan, D.1    Nampoothiri, K.M.2    Sivaramakrishnan, S.3    Pandey, A.4
  • 10
    • 0015086333 scopus 로고
    • Isolation, purification and characterization of a maltotetraose-producing amylase from Pseudomonas stuzeri
    • 10.1016/0003-9861(71)90015-4 1:CAS:528:DyaE3MXkslWlsrk%3D
    • Robyt, J. F. and R. J. Ackerman (1971) Isolation, purification and characterization of a maltotetraose-producing amylase from Pseudomonas stuzeri. Arch. Biochem. Biophys. 145: 105-114.
    • (1971) Arch. Biochem. Biophys. , vol.145 , pp. 105-114
    • Robyt, J.F.1    Ackerman, R.J.2
  • 11
    • 0025397229 scopus 로고
    • Purification and characterization of two forms of maltotetraose-forming amylase from Pseudomonas stutzeri
    • 10.1271/bbb1961.54.737 1:CAS:528:DyaK3cXitFaru7g%3D
    • Nakada, T., M. Kubota, S. Sakai, and Y. Tsujisaka (1990) Purification and characterization of two forms of maltotetraose-forming amylase from Pseudomonas stutzeri. Agric. Biol. Chem. 54: 737-743.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 737-743
    • Nakada, T.1    Kubota, M.2    Sakai, S.3    Tsujisaka, Y.4
  • 12
    • 0000139122 scopus 로고
    • Purification and properties of an exo-α-amylase from Pseudomonas stutzeri
    • 10.1271/bbb1961.46.639 1:CAS:528:DyaL38XhsFyjt7w%3D
    • Sakano, Y., Y. Kashiwagi, and T. Kobayashi (1982) Purification and properties of an exo-α-amylase from Pseudomonas stutzeri. Agric. Biol. Chem. 46: 639-646.
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 639-646
    • Sakano, Y.1    Kashiwagi, Y.2    Kobayashi, T.3
  • 13
    • 0011202301 scopus 로고
    • Purification of a maltotetraose-forming exo-amylase of Pseudomonas stutzeri: Two-forms of the amylase and their enzymatic properties
    • 10.1271/bbb1961.47.1761 1:CAS:528:DyaL3sXltFyhu7c%3D
    • Sakano, Y., Y. Kashiwagi, and T. Kobayashi (1983) Purification of a maltotetraose-forming exo-amylase of Pseudomonas stutzeri: Two-forms of the amylase and their enzymatic properties. Agric. Biol. Chem. 47: 1761-1768.
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 1761-1768
    • Sakano, Y.1    Kashiwagi, Y.2    Kobayashi, T.3
  • 14
    • 0024513280 scopus 로고
    • Cloning and nucleotide sequence of the gene (amyP) for maltotetraose-forming amylase from Pseudomonas stutzeri MO-19
    • 1:CAS:528:DyaK3cXhsFWk
    • Fujita, M., K. Torigoe, T. Nakada, K. Tsusaki, M. Kubota, S. Sakai, and Y. Tsujisaka (1989) Cloning and nucleotide sequence of the gene (amyP) for maltotetraose-forming amylase from Pseudomonas stutzeri MO-19. J. bacteriol. 171: 1333-1339.
    • (1989) J. Bacteriol. , vol.171 , pp. 1333-1339
    • Fujita, M.1    Torigoe, K.2    Nakada, T.3    Tsusaki, K.4    Kubota, M.5    Sakai, S.6    Tsujisaka, Y.7
  • 15
    • 79952573679 scopus 로고    scopus 로고
    • Molecular cloning and expression of an extracellular α-amylase gene from an Antarctic deep sea psychrotolerant Pseudomonas stutzeri strain 7193
    • 10.1007/s11274-010-0526-0
    • Zhang, J. and R. Zeng (2011) Molecular cloning and expression of an extracellular α-amylase gene from an Antarctic deep sea psychrotolerant Pseudomonas stutzeri strain 7193. World J. Microb. Biot. 27: 841-850.
    • (2011) World J. Microb. Biot. , vol.27 , pp. 841-850
    • Zhang, J.1    Zeng, R.2
  • 16
    • 0028339244 scopus 로고
    • Extracellular maltotetraose-forming amylase of Pseudomonas sp. IMD 353
    • 1:CAS:528:DyaK2cXlt1ynsLw%3D
    • Fogarty, W. M., C. T. Kelly, A. C. Bourke, and E. M. Doyle (1994) Extracellular maltotetraose-forming amylase of Pseudomonas sp. IMD 353. Biotechnol. 16: 473-478.
    • (1994) Biotechnol. , vol.16 , pp. 473-478
    • Fogarty, W.M.1    Kelly, C.T.2    Bourke, A.C.3    Doyle, E.M.4
  • 17
    • 0024465379 scopus 로고
    • Nucleotide sequence of the maltotetraohydrolase gene from Pseudomonas saccharophila
    • 10.1016/0014-5793(89)81056-7 1:CAS:528:DyaK3cXhvFakt74%3D
    • Zhou, J., T. Baba, T. Takano, S. Kobayashi, and Y. Arai (1989) Nucleotide sequence of the maltotetraohydrolase gene from Pseudomonas saccharophila. FEBS. Lett. 255: 37-41.
    • (1989) FEBS. Lett. , vol.255 , pp. 37-41
    • Zhou, J.1    Baba, T.2    Takano, T.3    Kobayashi, S.4    Arai, Y.5
  • 18
    • 0000220157 scopus 로고
    • Production of amylase and pullulanase by an alkalopsychrotrophic Micrococcus sp
    • 10.1271/bbb1961.53.2963 1:CAS:528:DyaK3cXltFykug%3D%3D
    • Kimura, T. and K. Horikoshi (1989) Production of amylase and pullulanase by an alkalopsychrotrophic Micrococcus sp. Agric. Biol. Chem. 53: 2963-2968.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 2963-2968
    • Kimura, T.1    Horikoshi, K.2
  • 19
    • 84954873322 scopus 로고
    • An amylase producing maltotetraose and maltopentaose from Bacillus circulans
    • 10.1271/bbb1961.47.2193 1:CAS:528:DyaL2cXhvFKkug%3D%3D
    • Takasaki, Y. (1983) An amylase producing maltotetraose and maltopentaose from Bacillus circulans. Agric. Biol. Chem. 47: 2193-2199.
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 2193-2199
    • Takasaki, Y.1
  • 20
    • 0029119475 scopus 로고
    • Purification and characterization of a maltotetraose-forming alkaline α-amylase from an alkalophilic Bacillus strain GM8901
    • 1:CAS:528:DyaK2MXnt1ahsr8%3D
    • Kim, T. U., B. G. Gu, J. Y. Jeong, S. M. Byun, and Y. C. Shin (1995) Purification and characterization of a maltotetraose-forming alkaline α-amylase from an alkalophilic Bacillus strain GM8901. Appl. Environ. Microbiol. 61: 3105-3112.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3105-3112
    • Kim, T.U.1    Gu, B.G.2    Jeong, J.Y.3    Byun, S.M.4    Shin, Y.C.5
  • 21
    • 49749105587 scopus 로고    scopus 로고
    • Purification and characterization of five alkaline, thermotolerant, and maltotetraose-producing α-amylases from Bacillus halodurans MS-2-5, and production of recombinant enzymes in Escherichia coli
    • 10.1016/j.enzmictec.2008.05.006 1:CAS:528:DC%2BD1cXhtVejsrjE
    • Murakami, S., K. Nagasaki, H. Nishimoto, R. Shigematu, J. Umesaki, S. Takenaka, J. Kaulpiboon, M. Prousoontorn, T. Limpaseni, P. Pongsawasdi, and K. Aoki (2008) Purification and characterization of five alkaline, thermotolerant, and maltotetraose-producing α-amylases from Bacillus halodurans MS-2-5, and production of recombinant enzymes in Escherichia coli. Enz. Microbiol. Technol. 43: 321-328.
    • (2008) Enz. Microbiol. Technol. , vol.43 , pp. 321-328
    • Murakami, S.1    Nagasaki, K.2    Nishimoto, H.3    Shigematu, R.4    Umesaki, J.5    Takenaka, S.6    Kaulpiboon, J.7    Prousoontorn, M.8    Limpaseni, T.9    Pongsawasdi, P.10    Aoki, K.11
  • 23
    • 0003785155 scopus 로고
    • Cold spring Harbor Laboratory Cold Spring Harbor, NY, USA
    • Miller, J. H. (1972) Experiments in Molecular Genetics. pp. 431-435. Cold spring Harbor Laboratory, Cold Spring Harbor, NY, USA.
    • (1972) Experiments in Molecular Genetics , pp. 431-435
    • Miller, J.H.1
  • 24
    • 33747333106 scopus 로고
    • Use of dinitrosalycilic acid reagent for determination of reducing sugars
    • 10.1021/ac60147a030 1:CAS:528:DyaG1MXmtFKiuw%3D%3D
    • Miller, G. L. (1959) Use of dinitrosalycilic acid reagent for determination of reducing sugars. Anal. Chem. 31: 426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding
    • 10.1016/0003-2697(76)90527-3 1:CAS:528:DyaE28XksVehtrY%3D
    • Bradford, M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 27
    • 84887038163 scopus 로고    scopus 로고
    • Characterization of α-maltotetraohydrolase produced by Pseudomonas sp. MS300 isolated from the deepest site of Mariana trench
    • Kobayashi, H., Y. Takaki, H. Takami, and A. Inoue (2000) Characterization of α-maltotetraohydrolase produced by Pseudomonas sp. MS300 isolated from the deepest site of Mariana trench. Deep Sea Res. 16: 109-116.
    • (2000) Deep Sea Res. , vol.16 , pp. 109-116
    • Kobayashi, H.1    Takaki, Y.2    Takami, H.3    Inoue, A.4
  • 28
    • 0026634725 scopus 로고
    • α-Amylases and approaches leading to their enhanced stability
    • 10.1016/0014-5793(92)80575-2
    • Janeek, Š. and B. Štefan (1992) α-Amylases and approaches leading to their enhanced stability. FEBS Lett. 304: 1-3.
    • (1992) FEBS Lett. , vol.304 , pp. 1-3
    • Janeek1    Štefan, B.2
  • 29
    • 0035050561 scopus 로고    scopus 로고
    • Crystal structure of Bacillus Stearothermophilus α-amylase: Possible factors determining the thermostability
    • 10.1093/oxfordjournals.jbchem.a002878 1:CAS:528:DC%2BD3MXjtlSisr0%3D
    • Suvd, D., Z. Fujimoto, K. Takase, M. Matsumura, and H. Mizuno (2001) Crystal structure of Bacillus Stearothermophilus α-amylase: Possible factors determining the thermostability. J. Biochem. 129: 461-468.
    • (2001) J. Biochem. , vol.129 , pp. 461-468
    • Suvd, D.1    Fujimoto, Z.2    Takase, K.3    Matsumura, M.4    Mizuno, H.5
  • 30
    • 14544282884 scopus 로고    scopus 로고
    • A calcium independent α-amylase that is active and stable at low pH from the Bacillus sp. KR-8104
    • 10.1016/j.enzmictec.2004.11.003 1:CAS:528:DC%2BD2MXhvVSnu7o%3D
    • Sajedi, R. H., H. Naderi-Mahesh, K. Khajeh, R. Ahmadvand, B. A. Ranjbar, A. Asoodeh, and F. Moradian (2005) A calcium independent α-amylase that is active and stable at low pH from the Bacillus sp. KR-8104. Enz. Microb. Technol. 36: 666-671.
    • (2005) Enz. Microb. Technol. , vol.36 , pp. 666-671
    • Sajedi, R.H.1    Naderi-Mahesh, H.2    Khajeh, K.3    Ahmadvand, R.4    Ranjbar, B.A.5    Asoodeh, A.6    Moradian, F.7
  • 31
    • 84867612246 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of recombinant acidic and thermostable raw-starch hydrolyzing α-amylase from an extreme thermophile Geobacillus thermoleovorans
    • 10.1016/j.molcatb.2012.08.017
    • Mehta, M. and T. Satyanarayana (2013) Biochemical and molecular characterization of recombinant acidic and thermostable raw-starch hydrolyzing α-amylase from an extreme thermophile Geobacillus thermoleovorans. J. Mol. Catal. B: Enzym. 85: 229-238.
    • (2013) J. Mol. Catal. B: Enzym. , vol.85 , pp. 229-238
    • Mehta, M.1    Satyanarayana, T.2
  • 32
    • 84870845185 scopus 로고    scopus 로고
    • The stability and thermodynamic parameters of a very thermostable and calcium-independent α-amylase from a newly isolated bacterium, Anoxybacillus beppuensis TSSC-1
    • 10.1016/j.procbio.2012.06.005 1:CAS:528:DC%2BC38XpvVOgtL0%3D
    • Kikani, B. A. and S. P. Singh (2012) The stability and thermodynamic parameters of a very thermostable and calcium-independent α-amylase from a newly isolated bacterium, Anoxybacillus beppuensis TSSC-1. Proc. Biochem. 47: 1791-1798.
    • (2012) Proc. Biochem. , vol.47 , pp. 1791-1798
    • Kikani, B.A.1    Singh, S.P.2
  • 33
    • 0000758153 scopus 로고
    • Metal content of α-amylases of various origins
    • 1:CAS:528:DyaF3cXitlGnuw%3D%3D
    • Vallee, B. L., E. A. Stein, W. N. Sumerwell, and E. H. Fischer (1959) Metal content of α-amylases of various origins. J. Biol. Chem. 234: 2901-2905.
    • (1959) J. Biol. Chem. , vol.234 , pp. 2901-2905
    • Vallee, B.L.1    Stein, E.A.2    Sumerwell, W.N.3    Fischer, E.H.4
  • 34
    • 0023644668 scopus 로고
    • Thermal destruction processes in proteins involving cysteine
    • Volkin, D. B. and A. M. Klibanov (1989) Thermal destruction processes in proteins involving cysteine. J. Biol. Chem. 89: 2945-2950.
    • (1989) J. Biol. Chem. , vol.89 , pp. 2945-2950
    • Volkin, D.B.1    Klibanov, A.M.2
  • 35
    • 0141922989 scopus 로고    scopus 로고
    • Secondary calcium-binding parameter of Bacillus amyloliquefaciens α-amylase obtained from inhibition kinetics
    • 1:CAS:528:DC%2BD3sXptVygsLY%3D
    • Tanaka, A. and E. Hoshino (2003) Secondary calcium-binding parameter of Bacillus amyloliquefaciens α-amylase obtained from inhibition kinetics. J. Biosci. Bioeng. 96: 262-267.
    • (2003) J. Biosci. Bioeng. , vol.96 , pp. 262-267
    • Tanaka, A.1    Hoshino, E.2
  • 36
    • 0031552349 scopus 로고    scopus 로고
    • Crystal structure of a maltotetraoseforming exo-amylase from Pseudomonas stutzeri
    • 10.1006/jmbi.1996.0887 1:CAS:528:DyaK2sXis1KgtLw%3D
    • Morishita, Y., K. Hasegawa, Y. Matsuura, Y. Katsube, M. Kubota, and S. Sakai (1997) Crystal structure of a maltotetraoseforming exo-amylase from Pseudomonas stutzeri. J. Mol. Biol. 267: 661-672.
    • (1997) J. Mol. Biol. , vol.267 , pp. 661-672
    • Morishita, Y.1    Hasegawa, K.2    Matsuura, Y.3    Katsube, Y.4    Kubota, M.5    Sakai, S.6
  • 37
    • 0016908848 scopus 로고
    • Amylase activity and stability at high and low temperature depending on calcium and other divalent cations
    • 10.1007/978-3-0348-7675-9-7 1:CAS:528:DyaE28XksVaqsb4%3D
    • Heinen, W. and A. M. Lauwers (1976) Amylase activity and stability at high and low temperature depending on calcium and other divalent cations. Experientia Suppl. 26: 77-89.
    • (1976) Experientia Suppl. , vol.26 , pp. 77-89
    • Heinen, W.1    Lauwers, A.M.2
  • 39
    • 0035318737 scopus 로고    scopus 로고
    • Novel α-amylase that is highly resistant to chelating reagents and chemical oxidants from the alkaliphilic Bacillus isolate KSM-K38
    • 10.1128/AEM.67.4.1744-1750.2001 1:CAS:528:DC%2BD3MXis1egtL8%3D
    • Hagihara, H., K. Igarashi, Y. Hayashi, K. Endo, K. Ikawa, K. Ozaki, S. Kawai, and S. Ito (2001) Novel α-amylase that is highly resistant to chelating reagents and chemical oxidants from the alkaliphilic Bacillus isolate KSM-K38. Appl. Environ. Microbiol. 67: 1744-1750.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 1744-1750
    • Hagihara, H.1    Igarashi, K.2    Hayashi, Y.3    Endo, K.4    Ikawa, K.5    Ozaki, K.6    Kawai, S.7    Ito, S.8
  • 40
    • 33747366714 scopus 로고    scopus 로고
    • Oxidatively stable maltopentaose-producing α-amylase from a deep-sea Bacillus isolate, and mechanism of its oxidative stability validated by site-directed mutagenesis
    • 10.1016/j.enzmictec.2006.03.022 1:CAS:528:DC%2BD28Xosl2rtLw%3D
    • Hatada, Y., N. Masuda, M. Akita, M. Miyazaki, Y. Ohta, and K. Horikoshi (2006) Oxidatively stable maltopentaose-producing α-amylase from a deep-sea Bacillus isolate, and mechanism of its oxidative stability validated by site-directed mutagenesis. Enz. Microb. Technol. 39: 1333-1340.
    • (2006) Enz. Microb. Technol. , vol.39 , pp. 1333-1340
    • Hatada, Y.1    Masuda, N.2    Akita, M.3    Miyazaki, M.4    Ohta, Y.5    Horikoshi, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.