메뉴 건너뛰기




Volumn 24, Issue 11, 2008, Pages 2517-2524

Atypical Ca2+-independent, raw-starch hydrolysing α-amylase from Bacillus sp. GRE1: Characterization and gene isolation

Author keywords

Bacillus sp. GRE1; Ca2+ independent amylase; Raw starch hydrolysis

Indexed keywords

BACTERIOLOGY;

EID: 52449123053     PISSN: 09593993     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11274-008-9775-6     Document Type: Article
Times cited : (18)

References (36)
  • 1
    • 0023268885 scopus 로고
    • Metal binding characteristics of human salivary and porcine pancreatic amylase
    • RP Agarwal RI Henkin 1987 Metal binding characteristics of human salivary and porcine pancreatic amylase J Biol Chem 262 2568 2575
    • (1987) J Biol Chem , vol.262 , pp. 2568-2575
    • Agarwal, R.P.1    Henkin, R.I.2
  • 2
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • 10.1093/nar/25.17.3389
    • SF Altschul TL Madden AA Schaffer J Zhang Z Zhang W Miller 1997 Gapped BLAST and PSI-BLAST: a new generation of protein database search programs Nucleic Acids Res 25 3389 3402 10.1093/nar/25.17.3389
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6
  • 3
    • 0025784988 scopus 로고
    • Development and optimization of a defined medium for aerobic growth of Bacillus stearothermophilus LLD-15
    • 10.1007/BF01086315
    • SA Amartey DJ Leak BS Hartley 1991 Development and optimization of a defined medium for aerobic growth of Bacillus stearothermophilus LLD-15 Biotechnol Lett 13 621 626 10.1007/BF01086315
    • (1991) Biotechnol Lett , vol.13 , pp. 621-626
    • Amartey, S.A.1    Leak, D.J.2    Hartley, B.S.3
  • 4
    • 0032896156 scopus 로고    scopus 로고
    • A thermostable α-amylase producing maltohexaose from a new isolated Bacillus sp. US100: Study of activity and molecular cloning of the corresponding gene
    • 10.1016/S0141-0229(98)00165-3
    • M Ben Ali M Mezghani S Bejar 1999 A thermostable α-amylase producing maltohexaose from a new isolated Bacillus sp. US100: study of activity and molecular cloning of the corresponding gene Enzyme Microb Technol 24 584 589 10.1016/S0141-0229(98)00165-3
    • (1999) Enzyme Microb Technol , vol.24 , pp. 584-589
    • Ben Ali, M.1    Mezghani, M.2    Bejar, S.3
  • 5
    • 0035810297 scopus 로고    scopus 로고
    • Purification and sequence analysis of the atypical maltohexaose-forming α-amylase of the Bacillus stearothermophilus US100
    • 10.1016/S0141-0229(01)00294-0
    • M Ben Ali S Mhiri M Mezghani S Bejar 2001 Purification and sequence analysis of the atypical maltohexaose-forming α-amylase of the Bacillus stearothermophilus US100 Enzyme Microb Technol 28 537 542 10.1016/S0141-0229(01) 00294-0
    • (2001) Enzyme Microb Technol , vol.28 , pp. 537-542
    • Ben Ali, M.1    Mhiri, S.2    Mezghani, M.3    Bejar, S.4
  • 6
    • 33748037939 scopus 로고
    • Amylases α and β
    • 10.1016/0076-6879(55) 01021-5
    • P Bernfeld 1955 Amylases α and β Methods Enzymol 1 149 158 10.1016/0076-6879(55) 01021-5
    • (1955) Methods Enzymol , vol.1 , pp. 149-158
    • Bernfeld, P.1
  • 7
    • 25444445001 scopus 로고    scopus 로고
    • A novel raw starch digesting thermostable α-amylase from Bacillus sp. I-3 and its use in the direct hydrolysis of raw potato starch
    • 10.1016/j.enzmictec.2005.04.017
    • N Goyal JK Gupta SK Soni 2005 A novel raw starch digesting thermostable α-amylase from Bacillus sp. I-3 and its use in the direct hydrolysis of raw potato starch Enzyme Microb Technol 37 723 734 10.1016/j.enzmictec.2005.04. 017
    • (2005) Enzyme Microb Technol , vol.37 , pp. 723-734
    • Goyal, N.1    Gupta, J.K.2    Soni, S.K.3
  • 8
    • 0034836495 scopus 로고    scopus 로고
    • Deduced amino-acid sequence of a calcium-free α-amylase from a strain of Bacillus
    • 10.1046/j.1432-1327.2001.02308.x
    • H Hagihara Y Hayashi K Endo K Igarashi T Ozawa S Kawai 2001 Deduced amino-acid sequence of a calcium-free α-amylase from a strain of Bacillus Eur J Biochem 268 3974 3982 10.1046/j.1432-1327.2001.02308.x
    • (2001) Eur J Biochem , vol.268 , pp. 3974-3982
    • Hagihara, H.1    Hayashi, Y.2    Endo, K.3    Igarashi, K.4    Ozawa, T.5    Kawai, S.6
  • 9
    • 0037411739 scopus 로고    scopus 로고
    • Developments in industrially important thermostable enzymes: A review
    • GD Haki SK Rakshit 2003 Developments in industrially important thermostable enzymes: a review Bioresour Techno1 89 17 34
    • (2003) Bioresour Techno1 , vol.89 , pp. 17-34
    • Haki, G.D.1    Rakshit, S.K.2
  • 10
    • 0032424629 scopus 로고    scopus 로고
    • Raw starch degradation by the non-raw starch-adsorbing bacterial alpha amylase of Bacillus sp. IMD 434
    • 10.1016/S0008-6215(98)00300-0
    • LM Hamilton CT Kelly WM Fogarty 1998 Raw starch degradation by the non-raw starch-adsorbing bacterial alpha amylase of Bacillus sp. IMD 434 Carbohydr Res 314 251 257 10.1016/S0008-6215(98)00300-0
    • (1998) Carbohydr Res , vol.314 , pp. 251-257
    • Hamilton, L.M.1    Kelly, C.T.2    Fogarty, W.M.3
  • 11
    • 0032719377 scopus 로고    scopus 로고
    • Production and properties of the raw starch-digesting α-amylase of Bacillus sp. IMD 435
    • 10.1016/S0032-9592(99)00028-X
    • LM Hamilton CT Kelly WM Fogarty 1999 Production and properties of the raw starch-digesting α-amylase of Bacillus sp. IMD 435 Process Biochem 35 27 31 10.1016/S0032-9592(99)00028-X
    • (1999) Process Biochem , vol.35 , pp. 27-31
    • Hamilton, L.M.1    Kelly, C.T.2    Fogarty, W.M.3
  • 12
    • 0029740660 scopus 로고    scopus 로고
    • Raw-starch digesting and thermostable α-amylase from the yeast Cryptococcus sp. S-2: Purification, characterization, cloning and sequencing
    • H Iefugi M Chino M Kato Y Imura 1996 Raw-starch digesting and thermostable α-amylase from the yeast Cryptococcus sp. S-2: purification, characterization, cloning and sequencing Biochem J 318 989 996
    • (1996) Biochem J , vol.318 , pp. 989-996
    • Iefugi, H.1    Chino, M.2    Kato, M.3    Imura, Y.4
  • 13
    • 0001440381 scopus 로고
    • Purification and properties of divalent cation-dependent raw-starch-digesting α-amylase from Bacillus sp. B1018
    • 10.1016/0922-338X(89)90024-X
    • P Itkor N Tsukagoshi S Udaka 1989 Purification and properties of divalent cation-dependent raw-starch-digesting α-amylase from Bacillus sp. B1018 J Ferment Bioeng 68 247 251 10.1016/0922-338X(89)90024-X
    • (1989) J Ferment Bioeng , vol.68 , pp. 247-251
    • Itkor, P.1    Tsukagoshi, N.2    Udaka, S.3
  • 14
    • 0029598794 scopus 로고
    • The raw starch-degrading alkaline amylase of Bacillus sp. IMD 370
    • 10.1007/BF01569973
    • CT Kelly MA McTigue EM Doyle WM Fogarty 1995 The raw starch-degrading alkaline amylase of Bacillus sp. IMD 370 J Ind Microbiol 15 446 448 10.1007/BF01569973
    • (1995) J Ind Microbiol , vol.15 , pp. 446-448
    • Kelly, C.T.1    McTigue, M.A.2    Doyle, E.M.3    Fogarty, W.M.4
  • 15
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment
    • 10.1093/bib/5.2.150
    • S Kumar K Tamura M Nei 2004 MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment Brief Bioinform 5 150 163 10.1093/bib/5.2.150
    • (2004) Brief Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 10.1038/227680a0
    • UK Laemmli 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 680 685 10.1038/227680a0
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 2542509338 scopus 로고    scopus 로고
    • Thermophilic archaeal amylolytic enzymes
    • 10.1016/S0141-0229(99)00142-8
    • E Leveque S Janecek B Haye A Belarbi 2000 Thermophilic archaeal amylolytic enzymes Enzyme Microb Technol 26 3 14 10.1016/S0141-0229(99)00142-8
    • (2000) Enzyme Microb Technol , vol.26 , pp. 3-14
    • Leveque, E.1    Janecek, S.2    Haye, B.3    Belarbi, A.4
  • 18
    • 40749092049 scopus 로고    scopus 로고
    • A novel raw starch digesting a-amylase from a newly isolated Bacillus sp. YX-1: Purification and characterization
    • 10.1016/j.biortech.2007.08.040
    • XD Liu Y Xu 2008 A novel raw starch digesting a-amylase from a newly isolated Bacillus sp. YX-1: purification and characterization Bioresour Technol 99 4315 4320 10.1016/j.biortech.2007.08.040
    • (2008) Bioresour Technol , vol.99 , pp. 4315-4320
    • Liu, X.D.1    Xu, Y.2
  • 19
    • 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
    • 10.1016/S0969-2126(98)00032-X
    • M Machius N Declerck R Huber G Wiegand 1998 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 10.1016/S0969-2126(98)00032-X
    • (1998) Structure , vol.6 , pp. 281-292
    • MacHius, M.1    Declerck, N.2    Huber, R.3    Wiegand, G.4
  • 21
    • 0033180538 scopus 로고    scopus 로고
    • Purification and characterization of two raw starch digesting thermostable α-amylase from a thermophilic Bacillus
    • 10.1016/S0141-0229(99)00068-X
    • G Mamo A Gessese 1999 Purification and characterization of two raw starch digesting thermostable α-amylase from a thermophilic Bacillus Enzyme Microb Technol 25 433 438 10.1016/S0141-0229(99)00068-X
    • (1999) Enzyme Microb Technol , vol.25 , pp. 433-438
    • Mamo, G.1    Gessese, A.2
  • 22
    • 0042090311 scopus 로고    scopus 로고
    • Crystal structure of calcium-free α-amylase from Bacillus sp. strain KSM-K38 (AmyK38) and its sodium ion binding sites
    • 10.1074/jbc.M212763200
    • T Nonaka M Fujihashi A Kita H Hagihara K Ozaki S Ito 2003 Crystal structure of calcium-free α-amylase from Bacillus sp. strain KSM-K38 (AmyK38) and its sodium ion binding sites J Biol Chem 278 24818 24824 10.1074/jbc.M212763200
    • (2003) J Biol Chem , vol.278 , pp. 24818-24824
    • Nonaka, T.1    Fujihashi, M.2    Kita, A.3    Hagihara, H.4    Ozaki, K.5    Ito, S.6
  • 25
    • 0031048240 scopus 로고    scopus 로고
    • The utilization of RAPD-PCR for identifying thermophilic and mesophilic Bacillus species
    • 10.1111/j.1574-6968.1997.tb10223.x
    • RS Ronimus LE Parker HW Morgan 1997 The utilization of RAPD-PCR for identifying thermophilic and mesophilic Bacillus species FEMS Microbiol Lett 47 75 79 10.1111/j.1574-6968.1997.tb10223.x
    • (1997) FEMS Microbiol Lett , vol.47 , pp. 75-79
    • Ronimus, R.S.1    Parker, L.E.2    Morgan, H.W.3
  • 26
    • 14544282884 scopus 로고    scopus 로고
    • A Ca-independent α-amylase that is active and stable at low pH from the Bacillus sp. KR-8104
    • 10.1016/j.enzmictec.2004.11.003
    • RH Sajedi H Naderi-Manesh K Khajeh R Ahmadvand B Ranjbar A Asoodeh 2005 A Ca-independent α-amylase that is active and stable at low pH from the Bacillus sp. KR-8104 Enzyme Microb Technol 36 666 671 10.1016/j.enzmictec.2004. 11.003
    • (2005) Enzyme Microb Technol , vol.36 , pp. 666-671
    • Sajedi, R.H.1    Naderi-Manesh, H.2    Khajeh, K.3    Ahmadvand, R.4    Ranjbar, B.5    Asoodeh, A.6
  • 28
    • 0017681196 scopus 로고
    • DNA sequencing with chain-terminating inhibitors
    • 10.1073/pnas.74.12.5463
    • F Sanger S Nicklen AR Coulson 1977 DNA sequencing with chain-terminating inhibitors Proc Natl Acad Sci USA 74 5463 5467 10.1073/pnas.74.12.5463
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5463-5467
    • Sanger, F.1    Nicklen, S.2    Coulson, A.R.3
  • 29
    • 0033958836 scopus 로고    scopus 로고
    • Comparison of degradation abilities of α- And β-amylases on raw starch granules
    • 10.1016/S0032-9592(99) 00133-8
    • E Sarikaya T Higassa M Adachi B Mikami 2000 Comparison of degradation abilities of α- and β-amylases on raw starch granules Process Biochem 35 711 715 10.1016/S0032-9592(99) 00133-8
    • (2000) Process Biochem , vol.35 , pp. 711-715
    • Sarikaya, E.1    Higassa, T.2    Adachi, M.3    Mikami, B.4
  • 30
    • 7444246845 scopus 로고    scopus 로고
    • Production of a thermostable α-amylase from Bacillus sp. PS-7 by solid state fermentation and its synergistic use in the hydrolysis of malt starch for alcohol production
    • 10.1016/j.procbio.2003.10.008
    • HK Sodhi K Sharma JK Gupta SK Soni 2005 Production of a thermostable α-amylase from Bacillus sp. PS-7 by solid state fermentation and its synergistic use in the hydrolysis of malt starch for alcohol production Process Biochem 40 525 534 10.1016/j.procbio.2003.10.008
    • (2005) Process Biochem , vol.40 , pp. 525-534
    • Sodhi, H.K.1    Sharma, K.2    Gupta, J.K.3    Soni, S.K.4
  • 31
    • 0242473815 scopus 로고    scopus 로고
    • Production and characterization of thermostable α-amylase from Nocardiopsis sp. endophyte of yam bean
    • 10.1016/S0960-8524(00)00089-4
    • T Stamford N Stamford L Coelho J Araujo 2001 Production and characterization of thermostable α-amylase from Nocardiopsis sp. endophyte of yam bean Bioresour Technol 76 137 141 10.1016/S0960-8524(00)00089-4
    • (2001) Bioresour Technol , vol.76 , pp. 137-141
    • Stamford, T.1    Stamford, N.2    Coelho, L.3    Araujo, J.4
  • 32
    • 0034283404 scopus 로고    scopus 로고
    • New type of starch-binding domain: The direct repeat motif in the C-terminal region of Bacillus sp. no. 195 α-amylase contributes to starch binding and raw starch degrading
    • 10.1042/0264-6021:3500477
    • J Sumitani T Tottori T Kawaguchi M Arai 2000 New type of starch-binding domain: the direct repeat motif in the C-terminal region of Bacillus sp. no. 195 α-amylase contributes to starch binding and raw starch degrading Biochem J 350 477 484 10.1042/0264-6021:3500477
    • (2000) Biochem J , vol.350 , pp. 477-484
    • Sumitani, J.1    Tottori, T.2    Kawaguchi, T.3    Arai, M.4
  • 33
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • JD Thompson DG Higgins TJ Gibson 1994 CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res 22 4673 4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 34
    • 0024989048 scopus 로고
    • Characterization of a thermostable Bacillus stearothermophilus α-amylase
    • M Vihinen P Mäntsälä 1990 Characterization of a thermostable Bacillus stearothermophilus α-amylase Biotechnol Appl Biochem 12 427 435
    • (1990) Biotechnol Appl Biochem , vol.12 , pp. 427-435
    • Vihinen, M.1    Mäntsälä, P.2
  • 35
    • 0027551706 scopus 로고
    • Towards modifying plants for altered starch content and composition
    • 10.1016/0167-7799(93) 90124-R
    • RGF Visser E Jacobson 1993 Towards modifying plants for altered starch content and composition Trends Biotechnol 11 63 68 10.1016/0167-7799(93) 90124-R
    • (1993) Trends Biotechnol , vol.11 , pp. 63-68
    • Visser, R.G.F.1    Jacobson, E.2
  • 36
    • 0028332440 scopus 로고
    • Characterization of a new Bacillus stearothermophilus isolate: A highly thermostable α-amylase producing strain
    • 10.1007/BF00186953
    • R Wind R Buitelaar G Egglink H Huizing L Dijkhuizen 1994 Characterization of a new Bacillus stearothermophilus isolate: a highly thermostable α-amylase producing strain Appl Microbiol Biotechnol 4 155 162 10.1007/BF00186953
    • (1994) Appl Microbiol Biotechnol , vol.4 , pp. 155-162
    • Wind, R.1    Buitelaar, R.2    Egglink, G.3    Huizing, H.4    Dijkhuizen, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.