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Volumn 47, Issue 12, 2012, Pages 1791-1798

The stability and thermodynamic parameters of a very thermostable and calcium-independent α-amylase from a newly isolated bacterium, Anoxybacillus beppuensis TSSC-1

Author keywords

Calcium independent amylase; Chemical denaturation; pH stability; Production optimization; Thermodynamics; Thermostability

Indexed keywords

ALKALINE PH; CHEMICAL DENATURATION; COMPACT STRUCTURES; ENZYMATIC CATALYSIS; ENZYME-SUBSTRATE COMPLEXES; EXTREME TEMPERATURES; GENBANK; ION DEPENDENCY; PH STABILITY; PRODUCTION OPTIMIZATION; SINGLE-STEP PURIFICATION; SOLUBLE STARCH; SPECIFIC ACTIVITY; STRUCTURAL STABILITIES; THERMODYNAMIC PARAMETER; THERMOPHILIC BACTERIA; THERMOSTABILITY;

EID: 84870845185     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2012.06.005     Document Type: Article
Times cited : (60)

References (45)
  • 1
    • 0002587086 scopus 로고
    • Introduction: An overview of the thermophiles
    • T. Brock, John Wiley and Sons New York
    • T. Brock Introduction: an overview of the thermophiles T. Brock, Thermophiles: general, molecular and applied microbiology 1986 John Wiley and Sons New York 2 15
    • (1986) Thermophiles: General, Molecular and Applied Microbiology , pp. 2-15
    • Brock, T.1
  • 2
    • 3242721835 scopus 로고    scopus 로고
    • second revised ed. Vikas Publishing House Private Limited New Delhi p. 40-8
    • H.D. Kumar, and S. Swati Modern concepts of microbiology second revised ed. 2001 Vikas Publishing House Private Limited New Delhi p. 40-8
    • (2001) Modern Concepts of Microbiology
    • Kumar, H.D.1    Swati, S.2
  • 3
    • 0037411739 scopus 로고    scopus 로고
    • Developments in industrially important thermostable enzymes
    • G.D. Haki, and S.K. Rakshit Developments in industrially important thermostable enzymes Bioresource Technol 89 2003 17 34
    • (2003) Bioresource Technol , vol.89 , pp. 17-34
    • Haki, G.D.1    Rakshit, S.K.2
  • 8
    • 29644437685 scopus 로고    scopus 로고
    • Amylases and their applications
    • P.V. Aiyer Amylases and their applications Afr J Biotechnol 4 2005 1525 1529
    • (2005) Afr J Biotechnol , vol.4 , pp. 1525-1529
    • Aiyer, P.V.1
  • 9
    • 33750157980 scopus 로고    scopus 로고
    • A thermostable α-amylase from a moderately thermophilic Bacillus subtilis strain for starch processing
    • M. Asgher, M.J. Asad, S.U. Rahman, and R.L. Legge A thermostable α-amylase from a moderately thermophilic Bacillus subtilis strain for starch processing J Food Eng 79 2007 950 955
    • (2007) J Food Eng , vol.79 , pp. 950-955
    • Asgher, M.1    Asad, M.J.2    Rahman, S.U.3    Legge, R.L.4
  • 10
    • 77949300269 scopus 로고    scopus 로고
    • Optimization of growth medium and enzyme assay conditions for crude cellulase produced by a novel thermophilic and cellulolytic bacterium, Anoxybacillus sp. 527
    • Y. Liang, J. Yesuf, and J.W. Blackburn Optimization of growth medium and enzyme assay conditions for crude cellulase produced by a novel thermophilic and cellulolytic bacterium, Anoxybacillus sp. 527 Appl Biochem Biotechnol 160 6 2010 1841 1852
    • (2010) Appl Biochem Biotechnol , vol.160 , Issue.6 , pp. 1841-1852
    • Liang, Y.1    Yesuf, J.2    Blackburn, J.W.3
  • 11
    • 79953267462 scopus 로고    scopus 로고
    • Single step purification and characterization of a thermostable and calcium independent α-amylase from Bacillus amyloliquifaciens TSWK1-1 isolated from Tulsi Shyam Hot spring Reservoir, Gujarat (India)
    • B.A. Kikani, and S.P. Singh Single step purification and characterization of a thermostable and calcium independent α-amylase from Bacillus amyloliquifaciens TSWK1-1 isolated from Tulsi Shyam Hot spring Reservoir, Gujarat (India) Int J Biol Macromol 48 4 2011 676 681
    • (2011) Int J Biol Macromol , vol.48 , Issue.4 , pp. 676-681
    • Kikani, B.A.1    Singh, S.P.2
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 77954985806 scopus 로고    scopus 로고
    • Biochemical and thermal stabilization parameters of polygalacturonase from Erwinia carotovora subsp. carotorova BR1
    • V.B. Maisuria, V.A. Patel, and A.S. Nerurkar Biochemical and thermal stabilization parameters of polygalacturonase from Erwinia carotovora subsp. carotorova BR1 J Microbiol Biotechnol 20 2010 1077 1085
    • (2010) J Microbiol Biotechnol , vol.20 , pp. 1077-1085
    • Maisuria, V.B.1    Patel, V.A.2    Nerurkar, A.S.3
  • 14
    • 0000346442 scopus 로고
    • The application of the theory of absolute reaction rates to protein
    • H. Eyring, and A.E. Stearn The application of the theory of absolute reaction rates to protein Chem Rev 24 1939 253 270
    • (1939) Chem Rev , vol.24 , pp. 253-270
    • Eyring, H.1    Stearn, A.E.2
  • 15
    • 0031000325 scopus 로고    scopus 로고
    • PH and thermal stability studies of chitinase from Trichoderma harzianum: A thermodynamic consideration
    • A. Kapat, and T. Panda pH and thermal stability studies of chitinase from Trichoderma harzianum: a thermodynamic consideration Bioprocess Biosyst Eng 16 1997 269 272
    • (1997) Bioprocess Biosyst Eng , vol.16 , pp. 269-272
    • Kapat, A.1    Panda, T.2
  • 16
    • 77954987613 scopus 로고    scopus 로고
    • Thermal stabilization of chitinolytic enzymes of Pantoea dispersa
    • V. Gohel, and D.C. Naseby Thermal stabilization of chitinolytic enzymes of Pantoea dispersa Biochem Eng J 16 2007 57 67
    • (2007) Biochem Eng J , vol.16 , pp. 57-67
    • Gohel, V.1    Naseby, D.C.2
  • 17
    • 23744474187 scopus 로고    scopus 로고
    • Culture conditions for the production of thermostable amylase by Bacillus sp.
    • C.E.D. Teodoro, and M.L.L. Martins Culture conditions for the production of thermostable amylase by Bacillus sp. Braz J Microbiol 31 2000 298 302
    • (2000) Braz J Microbiol , vol.31 , pp. 298-302
    • Teodoro, C.E.D.1    Martins, M.L.L.2
  • 18
    • 0000156273 scopus 로고
    • Purification and properties of heat stable α-amylase from Bacillus brevis
    • V.T. Tsvetkov, and E.I. Emanuilova Purification and properties of heat stable α-amylase from Bacillus brevis Appl Microbiol Biotechnol 31 1989 246 248
    • (1989) Appl Microbiol Biotechnol , vol.31 , pp. 246-248
    • Tsvetkov, V.T.1    Emanuilova, E.I.2
  • 19
    • 0033748784 scopus 로고    scopus 로고
    • Production and partial characterization of thermostable and calcium-independent α-amylase of an extreme thermophile Bacillus thermooleovorans NP 54
    • R. Malhotra, S.M. Noorwez, and T. Satyanarayana Production and partial characterization of thermostable and calcium-independent α-amylase of an extreme thermophile Bacillus thermooleovorans NP 54 Lett Appl Microbiol 31 2000 378 384
    • (2000) Lett Appl Microbiol , vol.31 , pp. 378-384
    • Malhotra, R.1    Noorwez, S.M.2    Satyanarayana, T.3
  • 20
    • 70449126099 scopus 로고    scopus 로고
    • Thermostable α-amylase producing natural variant of Bacillus sp. isolated from Soil in Iran
    • S.D.A. Rasooli, H. Astaneh, K.A. Borna, and A. Barchini Thermostable α-amylase producing natural variant of Bacillus sp. isolated from Soil in Iran Am J Agric Biol Sci 3 2008 591 596
    • (2008) Am J Agric Biol Sci , vol.3 , pp. 591-596
    • Rasooli, S.D.A.1    Astaneh, H.2    Borna, K.A.3    Barchini, A.4
  • 21
    • 0030064025 scopus 로고    scopus 로고
    • The glucose effect and regulation of α-amylase synthesis in the hyperthermophilic archaeon Sulfolobus solfataricus
    • C. Haseltine, M. Rolfsmeier, and P. Blum The glucose effect and regulation of α-amylase synthesis in the hyperthermophilic archaeon Sulfolobus solfataricus J Bacteriol 178 1996 945 950
    • (1996) J Bacteriol , vol.178 , pp. 945-950
    • Haseltine, C.1    Rolfsmeier, M.2    Blum, P.3
  • 22
    • 78649966240 scopus 로고    scopus 로고
    • Production and properties of the highly efficient raw starch digesting α-amylase from a Bacillus licheniformis ATCC 9945
    • N. Bozic, J. Ruiz, J. Lopez-Santin, and Z. Vujcic Production and properties of the highly efficient raw starch digesting α-amylase from a Bacillus licheniformis ATCC 9945 Biochem Eng J 53 2011 203 209
    • (2011) Biochem Eng J , vol.53 , pp. 203-209
    • Bozic, N.1    Ruiz, J.2    Lopez-Santin, J.3    Vujcic, Z.4
  • 23
    • 58149242518 scopus 로고    scopus 로고
    • Production, purification and characterization of two extremely halotolerant, thermostable and alkali-stable α-amylases from Chromohalobacter sp. TVSP 101
    • B. Prakash, M. Vidyasagar, M.S. Madhukumar, G. Murlikrishna, and K. Sreeramulu Production, purification and characterization of two extremely halotolerant, thermostable and alkali-stable α-amylases from Chromohalobacter sp. TVSP 101 Process Biochem 44 2009 210 215
    • (2009) Process Biochem , vol.44 , pp. 210-215
    • Prakash, B.1    Vidyasagar, M.2    Madhukumar, M.S.3    Murlikrishna, G.4    Sreeramulu, K.5
  • 24
    • 79951674162 scopus 로고    scopus 로고
    • Purification and characterization of an organic solvent-tolerant halophilic α-amylase from the moderately halophilic Nesterenkonia sp. Strain F
    • M. Shafieim, A.A. Ziaee, and M.A. Amoozegar Purification and characterization of an organic solvent-tolerant halophilic α-amylase from the moderately halophilic Nesterenkonia sp. Strain F J Ind Microbiol Biotechnol 38 2011 275 281
    • (2011) J Ind Microbiol Biotechnol , vol.38 , pp. 275-281
    • Shafieim, M.1    Ziaee, A.A.2    Amoozegar, M.A.3
  • 25
    • 37249087867 scopus 로고    scopus 로고
    • A thermostable extracellular α-amylase from Bacillus licheniformis isolated from Cassava streep water
    • M.M. Adeyanju, F.K. Agboola, B.O. Omfuvbe, O.H. Oyefuga, and O.O. Adebavo A thermostable extracellular α-amylase from Bacillus licheniformis isolated from Cassava streep water Biotechnology 6 2007 473 480
    • (2007) Biotechnology , vol.6 , pp. 473-480
    • Adeyanju, M.M.1    Agboola, F.K.2    Omfuvbe, B.O.3    Oyefuga, O.H.4    Adebavo, O.O.5
  • 26
    • 70449122354 scopus 로고    scopus 로고
    • Characteristics of a novel highly thermostable and extremely thermophilic alkalitolerant amylase from hyperthermophilic Bacillus strain HUTBS71
    • F. Al-Quadan, H. Akel, and R. Natshi Characteristics of a novel highly thermostable and extremely thermophilic alkalitolerant amylase from hyperthermophilic Bacillus strain HUTBS71 J Biol Sci 9 2009 67 74
    • (2009) J Biol Sci , vol.9 , pp. 67-74
    • Al-Quadan, F.1    Akel, H.2    Natshi, R.3
  • 27
    • 77649180416 scopus 로고    scopus 로고
    • A novel thermostable, acidophilic α-amylase from a new thermophilic Bacillus sp. Ferdowsicous isolated from Ferdows hot mineral spring in Iran: Purification and biochemical characterization
    • A. Assodeh, J. Chamani, and M. Lagzian A novel thermostable, acidophilic α-amylase from a new thermophilic Bacillus sp. Ferdowsicous isolated from Ferdows hot mineral spring in Iran: purification and biochemical characterization Int J Biol Macromol 46 2010 289 297
    • (2010) Int J Biol Macromol , vol.46 , pp. 289-297
    • Assodeh, A.1    Chamani, J.2    Lagzian, M.3
  • 28
    • 71849095928 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable phytate resistant α-amylase from Geobacillus sp. LH8
    • N. Mollania, K. Khajeh, S. Hosseinkhani, and B. Dabirmanesh Purification and characterization of a thermostable phytate resistant α-amylase from Geobacillus sp. LH8 Int J Biol Macromol 46 2010 27 36
    • (2010) Int J Biol Macromol , vol.46 , pp. 27-36
    • Mollania, N.1    Khajeh, K.2    Hosseinkhani, S.3    Dabirmanesh, B.4
  • 29
    • 77956222611 scopus 로고    scopus 로고
    • Purification and characterization of highly thermostable α-amylase from thermophilic Alicyclobacillus acidocaldarius
    • G. Satheeshkumar, M.S. Chandra, K.V. Mallaiah, P. Srinivasulu, and Y.L. Choi Purification and characterization of highly thermostable α-amylase from thermophilic Alicyclobacillus acidocaldarius Biotechnol Bioprocess Eng 15 2010 435 440
    • (2010) Biotechnol Bioprocess Eng , vol.15 , pp. 435-440
    • Satheeshkumar, G.1    Chandra, M.S.2    Mallaiah, K.V.3    Srinivasulu, P.4    Choi, Y.L.5
  • 32
    • 14644411142 scopus 로고    scopus 로고
    • Enzymatic properties of an alkaline chelator-resistant α-amylase from an alkaliphilic Bacillus sp. isolate L1711
    • E.C.M. Bernhardsdotter, D.N. Joseph, and O.K. Garriott Enzymatic properties of an alkaline chelator-resistant α-amylase from an alkaliphilic Bacillus sp. isolate L1711 Process Biochem 40 7 2005 2401 2402
    • (2005) Process Biochem , vol.40 , Issue.7 , pp. 2401-2402
    • Bernhardsdotter, E.C.M.1    Joseph, D.N.2    Garriott, O.K.3
  • 33
    • 78649327448 scopus 로고    scopus 로고
    • Characterization and stability studies on surfactant, detergent and oxidant stable α-amylase from marine haloalkaliphilic Saccharopolyspora species A9
    • S. Chakraborty, A. Khopade, R. Biao, W. Jian, X.Y. Liu, and K. Mahadik Characterization and stability studies on surfactant, detergent and oxidant stable α-amylase from marine haloalkaliphilic Saccharopolyspora species A9 J Mol Catal B 68 2011 52 58
    • (2011) J Mol Catal B , vol.68 , pp. 52-58
    • Chakraborty, S.1    Khopade, A.2    Biao, R.3    Jian, W.4    Liu, X.Y.5    Mahadik, K.6
  • 36
    • 67349109119 scopus 로고    scopus 로고
    • 2+ independent α-amylase of an extreme thermophile Geobacillus thermoleovorans
    • 2+ independent α-amylase of an extreme thermophile Geobacillus thermoleovorans Appl Biochem Biotechnol 150 2008 205 219
    • (2008) Appl Biochem Biotechnol , vol.150 , pp. 205-219
    • Rao, J.U.M.1    Satyanarayana, T.2
  • 37
    • 38849110860 scopus 로고    scopus 로고
    • Highly thermostable, thermophilic, alkaline, SDS and chelator resistant amylase from a thermophilic Bacillus sp. isolate A3-15
    • B. Arikan Highly thermostable, thermophilic, alkaline, SDS and chelator resistant amylase from a thermophilic Bacillus sp. isolate A3-15 Bioresource Technol 99 2008 3071 3076
    • (2008) Bioresource Technol , vol.99 , pp. 3071-3076
    • Arikan, B.1
  • 38
    • 34250718072 scopus 로고    scopus 로고
    • Two-step purification of a highly thermostable alkaline protease from salt-tolerant alkaliphilic Streptomyces clavuligerus strain Mit-1
    • J. Thumar, and S.P. Singh Two-step purification of a highly thermostable alkaline protease from salt-tolerant alkaliphilic Streptomyces clavuligerus strain Mit-1 J Chromatogr B 854 2007 198 203
    • (2007) J Chromatogr B , vol.854 , pp. 198-203
    • Thumar, J.1    Singh, S.P.2
  • 39
    • 43849095922 scopus 로고    scopus 로고
    • Salt dependent resistance against chemical denaturation of alkaline protease from a newly isolated haloalkaliphilic Bacillus sp.
    • M.S. Dodia, H.G. Bhimani, C.M. Rawal, R.H. Joshi, and S.P. Singh Salt dependent resistance against chemical denaturation of alkaline protease from a newly isolated haloalkaliphilic Bacillus sp. Bioresource Technol 99 2008 6223 6227
    • (2008) Bioresource Technol , vol.99 , pp. 6223-6227
    • Dodia, M.S.1    Bhimani, H.G.2    Rawal, C.M.3    Joshi, R.H.4    Singh, S.P.5
  • 40
    • 38049068849 scopus 로고    scopus 로고
    • Purification and stability characteristics of an alkaline serine protease from a newly isolated haloalkaliphilic bacterium species AH-6
    • M.S. Dodia, C.M. Rawal, H.G. Bhimani, R.H. Joshi, S.K. Khare, and S.P. Singh Purification and stability characteristics of an alkaline serine protease from a newly isolated haloalkaliphilic bacterium species AH-6 J Ind Microbiol Biotechnol 35 2008 121 132
    • (2008) J Ind Microbiol Biotechnol , vol.35 , pp. 121-132
    • Dodia, M.S.1    Rawal, C.M.2    Bhimani, H.G.3    Joshi, R.H.4    Khare, S.K.5    Singh, S.P.6
  • 41
    • 79956105295 scopus 로고    scopus 로고
    • Comparative analysis of enzymatic stability and amino acids sequences of thermostable alkaline proteases from two haloalkaliphilic bacteria isolated from coastal region of Gujarat, India
    • M.K. Purohit, and S.P. Singh Comparative analysis of enzymatic stability and amino acids sequences of thermostable alkaline proteases from two haloalkaliphilic bacteria isolated from coastal region of Gujarat, India Int J Biol Macromol 49 1 2011 103 112
    • (2011) Int J Biol Macromol , vol.49 , Issue.1 , pp. 103-112
    • Purohit, M.K.1    Singh, S.P.2
  • 42
    • 80053950927 scopus 로고    scopus 로고
    • Purification and characterization of alkaline-stable β-amylase in malted African finger millet (Eleusine coracana) seed
    • A.O. Kolawole, J.O. Ajele, and R. Sirdeshmukh Purification and characterization of alkaline-stable β-amylase in malted African finger millet (Eleusine coracana) seed Process Biochem 46 2011 2178 2186
    • (2011) Process Biochem , vol.46 , pp. 2178-2186
    • Kolawole, A.O.1    Ajele, J.O.2    Sirdeshmukh, R.3
  • 44
    • 0037424370 scopus 로고    scopus 로고
    • Activity-stability relationships in extremophilic enzymes
    • S. D'Amico, J.C. Marx, C. Gerday, and G. Feller Activity-stability relationships in extremophilic enzymes J Biol Chem 278 2003 7891 7896
    • (2003) J Biol Chem , vol.278 , pp. 7891-7896
    • D'Amico, S.1    Marx, J.C.2    Gerday, C.3    Feller, G.4
  • 45
    • 0037900194 scopus 로고    scopus 로고
    • Hyperthermostabilization of Bacillus licheniformis amylase and modulation of its stability over a 50 °c temperature range
    • N. Declerck, M. Machius, P. Joyet, G. Wiegand, R. Huber, and C. Gaillardin Hyperthermostabilization of Bacillus licheniformis amylase and modulation of its stability over a 50 °C temperature range Protein Eng 16 2003 287 293
    • (2003) Protein Eng , vol.16 , pp. 287-293
    • Declerck, N.1    MacHius, M.2    Joyet, P.3    Wiegand, G.4    Huber, R.5    Gaillardin, C.6


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