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Volumn 10, Issue 12, 2007, Pages 2039-2047

Production and immobilization of α-amylase from Bacillus subtilis

Author keywords

Bacillus subtilis; Immobilization; Production; amylase

Indexed keywords

BACILLUS SUBTILIS;

EID: 34447298613     PISSN: 10288880     EISSN: 18125735     Source Type: Journal    
DOI: 10.3923/pjbs.2007.2039.2047     Document Type: Article
Times cited : (16)

References (49)
  • 1
    • 0027345141 scopus 로고
    • Immobilization of Aspergillus niger NRC 107 xylanase and xylosidase and properties of the immobilized enzymes
    • Abdel-Naby, M.A., 1993. Immobilization of Aspergillus niger NRC 107 xylanase and xylosidase and properties of the immobilized enzymes. Applied Biochem. Biotechnol., 38: 69-81.
    • (1993) Applied Biochem. Biotechnol , vol.38 , pp. 69-81
    • Abdel-Naby, M.A.1
  • 2
    • 15444365823 scopus 로고    scopus 로고
    • Effect of C:N ratio on alpha-amylase production by Bacillus licheniformis SPT 27
    • Aiyer, P.V.D., 2004. Effect of C:N ratio on alpha-amylase production by Bacillus licheniformis SPT 27. Afr. J. Biotechnol., 3: 519-522.
    • (2004) Afr. J. Biotechnol , vol.3 , pp. 519-522
    • Aiyer, P.V.D.1
  • 3
    • 0025300853 scopus 로고
    • Physiology and enzymology of thermophilic anaerobic bacteria degrading starch
    • Antranikian, G., 1990. Physiology and enzymology of thermophilic anaerobic bacteria degrading starch. FEMS Microbiol. Rev., 75: 201-218.
    • (1990) FEMS Microbiol. Rev , vol.75 , pp. 201-218
    • Antranikian, G.1
  • 4
    • 21144476269 scopus 로고
    • The effect and removal of starch in the sugar refining industry
    • Anyangwa, E.M., C. Mapsev, P. Musanage and M. Elemva, 1993. The effect and removal of starch in the sugar refining industry. J. Int. Sugar, 95: 210-213.
    • (1993) J. Int. Sugar , vol.95 , pp. 210-213
    • Anyangwa, E.M.1    Mapsev, C.2    Musanage, P.3    Elemva, M.4
  • 5
    • 0006044160 scopus 로고
    • Extracellular calcium in habited α-amylase production in batch and fell batch cultures of Bacillus subtilis
    • Babu, K.R. and T. Satyanarayana, 1995. Extracellular calcium in habited α-amylase production in batch and fell batch cultures of Bacillus subtilis. Folia Microbiol., 29: 359-364.
    • (1995) Folia Microbiol , vol.29 , pp. 359-364
    • Babu, K.R.1    Satyanarayana, T.2
  • 6
    • 0024961629 scopus 로고    scopus 로고
    • Bajpai, P. and P. Bajpai, 1989. High temperature alkaline α-amylase from Bacillus licheniformis TCRFC-BI3. Biotechnol. Bioeng., 33: 72-78.
    • Bajpai, P. and P. Bajpai, 1989. High temperature alkaline α-amylase from Bacillus licheniformis TCRFC-BI3. Biotechnol. Bioeng., 33: 72-78.
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M., 1976. A rapid and sensitive method for the quantitation 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.M.1
  • 8
    • 0002736063 scopus 로고
    • Production of extracellular thermostable-amylase by Bacillus licheniformis
    • Chandra, A.K., S. Medda and A.K. Bhadra, 1980. Production of extracellular thermostable-amylase by Bacillus licheniformis. J. Ferment. Technol., 58: 1-10.
    • (1980) J. Ferment. Technol , vol.58 , pp. 1-10
    • Chandra, A.K.1    Medda, S.2    Bhadra, A.K.3
  • 9
    • 0025335873 scopus 로고
    • Energy transduction and amino acid transport in thermophilic aerobic and fermentative bacteria
    • De Vrij, W., G. Speelmans and R.I.R. Heyne, 1990. Energy transduction and amino acid transport in thermophilic aerobic and fermentative bacteria. FEMS Microbiol. Rev., 75: 183-200.
    • (1990) FEMS Microbiol. Rev , vol.75 , pp. 183-200
    • De Vrij, W.1    Speelmans, G.2    Heyne, R.I.R.3
  • 10
    • 29244470172 scopus 로고    scopus 로고
    • Immobilization of α-amylase produced by Bacillus circulans GRS 313
    • Dey, G., B. Singh and R. Banerjee, 2003. Immobilization of α-amylase produced by Bacillus circulans GRS 313. Brazilian Arch. Biol. Technol., 46: 167-176.
    • (2003) Brazilian Arch. Biol. Technol , vol.46 , pp. 167-176
    • Dey, G.1    Singh, B.2    Banerjee, R.3
  • 11
    • 0028907616 scopus 로고    scopus 로고
    • The S-layer from Bacillus stearothermophilus DSM 2358 functions as an adhesion site for a high-molecular-weight amylase
    • Egelseer, E., I. Schocher and M. Sara, 1996a. The S-layer from Bacillus stearothermophilus DSM 2358 functions as an adhesion site for a high-molecular-weight amylase. J. Bacteriol., 177: 1444-1451.
    • (1996) J. Bacteriol , vol.177 , pp. 1444-1451
    • Egelseer, E.1    Schocher, I.2    Sara, M.3
  • 12
    • 0029819431 scopus 로고    scopus 로고
    • Evidence that an N-terminal S-layer protein fragment triggers the release of a cell-associated high-molecular-weight amylase in Bacillus stearothermophilus ATCC 12980
    • Egelseer, E., I. Schocher and U. Sleytr, 1996b. Evidence that an N-terminal S-layer protein fragment triggers the release of a cell-associated high-molecular-weight amylase in Bacillus stearothermophilus ATCC 12980. J. Bacteriol., 178: 5602-5609.
    • (1996) J. Bacteriol , vol.178 , pp. 5602-5609
    • Egelseer, E.1    Schocher, I.2    Sleytr, U.3
  • 13
    • 77957121083 scopus 로고
    • Effects of environment on bacterial wall content and composition
    • Ellwood, L.L. and D.W. Tempest, 1972a. Effects of environment on bacterial wall content and composition. Adv. Microb. Physiol., 7: 83-117.
    • (1972) Adv. Microb. Physiol , vol.7 , pp. 83-117
    • Ellwood, L.L.1    Tempest, D.W.2
  • 14
    • 0015427096 scopus 로고
    • Influence of culture pH on the content and composition of teichoic acid in the walls of Bacillus subtilis
    • Ellwood, L.L. and D.W. Tempest, 1972b. Influence of culture pH on the content and composition of teichoic acid in the walls of Bacillus subtilis. J. Gen. Microbiol., 73: 395-397.
    • (1972) J. Gen. Microbiol , vol.73 , pp. 395-397
    • Ellwood, L.L.1    Tempest, D.W.2
  • 15
    • 0025082190 scopus 로고
    • Effects on the hydrolysis of native starch and glycogen by a thermostable α-amylase after immobilization on solid supports
    • Emne'us, J. and L. Gordon, 1990. Effects on the hydrolysis of native starch and glycogen by a thermostable α-amylase after immobilization on solid supports. Anal. Chim. Acta, 234: 97-106.
    • (1990) Anal. Chim. Acta , vol.234 , pp. 97-106
    • Emne'us, J.1    Gordon, L.2
  • 17
    • 0020824186 scopus 로고
    • Prodcution and purification of maltose-producing amylase from Bacillus subtilis IMD 198
    • Fogarty, M.M. and E.J. Bourke, 1983. Prodcution and purification of maltose-producing amylase from Bacillus subtilis IMD 198. J. Chem. Technol. Biotechnol., 33B: 145-154.
    • (1983) J. Chem. Technol. Biotechnol , vol.33 B , pp. 145-154
    • Fogarty, M.M.1    Bourke, E.J.2
  • 18
    • 0032927640 scopus 로고    scopus 로고
    • Purification and properties of the raw starch degrading α-amylase of Bacillus sp. IMD 434
    • Hamitton, L.M., C.T. Kelly and W.M. Fogarty, 1999. Purification and properties of the raw starch degrading α-amylase of Bacillus sp. IMD 434. Biotechol. Lett., 21: 111-5.
    • (1999) Biotechol. Lett , vol.21 , pp. 111-115
    • Hamitton, L.M.1    Kelly, C.T.2    Fogarty, W.M.3
  • 20
    • 0000066939 scopus 로고
    • Starch
    • 3rd Edn. Aspinall, G.O, Ed, New York: Academic Press, pp
    • Guilbot, A. and C. Mercier, 1985. Starch. In: The Polysaccharides, 3rd Edn. Aspinall, G.O. (Ed.), New York: Academic Press, pp: 209-282
    • (1985) The Polysaccharides , pp. 209-282
    • Guilbot, A.1    Mercier, C.2
  • 21
    • 0030808957 scopus 로고    scopus 로고
    • B1-phasic production of α-amylase of Bacillus flavor thermus in batch fermentation
    • Kelly, C.T., D.J. Botton and W.M. Forgaty, 1997. B1-phasic production of α-amylase of Bacillus flavor thermus in batch fermentation. Biotechnol. Lett., 19: 675-677.
    • (1997) Biotechnol. Lett , vol.19 , pp. 675-677
    • Kelly, C.T.1    Botton, D.J.2    Forgaty, W.M.3
  • 22
    • 34447296892 scopus 로고    scopus 로고
    • Kennedy, J.F., 1987. Enzyme technology. In: Biotechnol. Kenda, J.F. and D.M.S Cabral (Eds.), 7A. Weinhuin, Germany, VCH publisher-verlagsgeslls Chaft Mbt1, pp: 398-399.
    • Kennedy, J.F., 1987. Enzyme technology. In: Biotechnol. Kenda, J.F. and D.M.S Cabral (Eds.), Vol. 7A. Weinhuin, Germany, VCH publisher-verlagsgeslls Chaft Mbt1, pp: 398-399.
  • 24
    • 0033500785 scopus 로고    scopus 로고
    • Entrap-immobilization of urease on composite gel fiber of cellulose acetate and Zirconia
    • Koji, N., T. Koji, S. Fumio and K. Youichi, 1999. Entrap-immobilization of urease on composite gel fiber of cellulose acetate and Zirconia. J. Soc. Fiber Sci. Technol., 55: 563-568.
    • (1999) J. Soc. Fiber Sci. Technol , vol.55 , pp. 563-568
    • Koji, N.1    Koji, T.2    Fumio, S.3    Youichi, K.4
  • 25
    • 0031335464 scopus 로고    scopus 로고
    • Adsorption of α-amylase on dextrin immobilized on kieselguhr or chitin
    • Kurakake, M., M. Ueki, S. Hashimoto and T. Komaki, 1997. Adsorption of α-amylase on dextrin immobilized on kieselguhr or chitin. Carbohyd. Polym., 34: 54-59.
    • (1997) Carbohyd. Polym , vol.34 , pp. 54-59
    • Kurakake, M.1    Ueki, M.2    Hashimoto, S.3    Komaki, T.4
  • 26
  • 27
    • 0031849201 scopus 로고    scopus 로고
    • Production and properties of a raw starch degrading amylase from the thermophilic and alkaliphilic Bacillus sp. TS- 23
    • Lin, L.L., C.C. Chyau and W.H. Hsu, 1998. Production and properties of a raw starch degrading amylase from the thermophilic and alkaliphilic Bacillus sp. TS- 23. Biotechnol. Applied Biochem., 28: 61-68.
    • (1998) Biotechnol. Applied Biochem , vol.28 , pp. 61-68
    • Lin, L.L.1    Chyau, C.C.2    Hsu, W.H.3
  • 28
    • 0032803951 scopus 로고    scopus 로고
    • Effect of cultivation conditions on growth and amylase production by a thermophilic Bacillus sp
    • Mamo, G. and A. Gessesse, 1999. Effect of cultivation conditions on growth and amylase production by a thermophilic Bacillus sp. Lett. Applied Microbiol., 29: 61-65.
    • (1999) Lett. Applied Microbiol , vol.29 , pp. 61-65
    • Mamo, G.1    Gessesse, A.2
  • 29
    • 0000108523 scopus 로고
    • The regulation of α-amylase production in Bacillus licheniformis
    • Meers, J.L., 1972. The regulation of α-amylase production in Bacillus licheniformis. Antonie Van Leeuwenhok, 38: 585-590.
    • (1972) Antonie Van Leeuwenhok , vol.38 , pp. 585-590
    • Meers, J.L.1
  • 30
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller, G.L., 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem., 31: 426-428.
    • (1959) Anal. Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 31
    • 0027213394 scopus 로고
    • Effect of temperature on fatty acid composition of a white Thermus strain
    • Nordstrom, K.M., 1993. Effect of temperature on fatty acid composition of a white Thermus strain. Applied Environm. Microbiol., 59: 1975-1976.
    • (1993) Applied Environm. Microbiol , vol.59 , pp. 1975-1976
    • Nordstrom, K.M.1
  • 33
    • 34249053727 scopus 로고    scopus 로고
    • Characterization of amylase by Bacillus subtilis
    • Riaz, N., I. Ul-Haq and M.A. Qadeer, 2003. Characterization of amylase by Bacillus subtilis. Int. J. Agric. Biol., 5: 249-252.
    • (2003) Int. J. Agric. Biol , vol.5 , pp. 249-252
    • Riaz, N.1    Ul-Haq, I.2    Qadeer, M.A.3
  • 34
    • 0034237335 scopus 로고    scopus 로고
    • Exploiting unusual affinity of usual poly-saccharides for separation of enzymes on fluidized beds
    • Roy, I., M. Sardar and M.N. Gupta, 2000. Exploiting unusual affinity of usual poly-saccharides for separation of enzymes on fluidized beds. Enzyme Microb. Technol., 27: 53-65.
    • (2000) Enzyme Microb. Technol , vol.27 , pp. 53-65
    • Roy, I.1    Sardar, M.2    Gupta, M.N.3
  • 35
    • 33747360729 scopus 로고    scopus 로고
    • Screening and identification of starch-, amylopectin-and pullulan-degrading activities in Bifidobacterial strains
    • Ryan, S.M., G.F. Fitzerald and D. Sinderen, 2006. Screening and identification of starch-, amylopectin-and pullulan-degrading activities in Bifidobacterial strains. Applied Environ. Microbiol., 72: 5289-5296.
    • (2006) Applied Environ. Microbiol , vol.72 , pp. 5289-5296
    • Ryan, S.M.1    Fitzerald, G.F.2    Sinderen, D.3
  • 36
    • 0027657081 scopus 로고
    • Immobilization of α-amylase from Myceliophthora thermophila D-14 (ATCC48104)
    • Sadhukhan, R., S.K. Roy and S.L. Chakrabarty, 1993. Immobilization of α-amylase from Myceliophthora thermophila D-14 (ATCC48104). Enzyme Microbiol. Technol., 15: 801-804.
    • (1993) Enzyme Microbiol. Technol , vol.15 , pp. 801-804
    • Sadhukhan, R.1    Roy, S.K.2    Chakrabarty, S.L.3
  • 37
    • 0015606538 scopus 로고
    • Thermophilic extracellular α-amylase from Bacillus licheniformis
    • Saito, N., 1973. Thermophilic extracellular α-amylase from Bacillus licheniformis. Arch. Biochem. Biophys., 15: 290-298.
    • (1973) Arch. Biochem. Biophys , vol.15 , pp. 290-298
    • Saito, N.1
  • 38
    • 0016635708 scopus 로고
    • Regulatory factors affecting α-amylase production in Bacillus licheniformis
    • Saito, N. and K. Yamamoto, 1975. Regulatory factors affecting α-amylase production in Bacillus licheniformis. J. Bacteriol., 121: 848-856.
    • (1975) J. Bacteriol , vol.121 , pp. 848-856
    • Saito, N.1    Yamamoto, K.2
  • 39
    • 34447315452 scopus 로고
    • Studies on the α-amylase from the germinated rice seeds
    • Shaw, J.F. and L.Y. Chuang, 1982. Studies on the α-amylase from the germinated rice seeds. Bot. Bull. Acad. Sin., 23: 45-61.
    • (1982) Bot. Bull. Acad. Sin , vol.23 , pp. 45-61
    • Shaw, J.F.1    Chuang, L.Y.2
  • 40
    • 33646496532 scopus 로고
    • Simultaneous purification of α-and β-amylase from germinated rice seeds and some factors affecting activities of the purified enzymes
    • Shaw, J.F. and T.M. Ou-Lee, 1989. Simultaneous purification of α-and β-amylase from germinated rice seeds and some factors affecting activities of the purified enzymes. Bot. Bull. Acad. Sin., 25: 197-204.
    • (1989) Bot. Bull. Acad. Sin , vol.25 , pp. 197-204
    • Shaw, J.F.1    Ou-Lee, T.M.2
  • 41
    • 0028853064 scopus 로고
    • Purification and properties of an extracellular α-amylase from Thermus sp
    • Shaw, J.F., F.P. Lin, S.C. Chen and H.C. Chen, 1995. Purification and properties of an extracellular α-amylase from Thermus sp. Bot. Bull. Acad. Sin., 36: 195-200.
    • (1995) Bot. Bull. Acad. Sin , vol.36 , pp. 195-200
    • Shaw, J.F.1    Lin, F.P.2    Chen, S.C.3    Chen, H.C.4
  • 42
    • 0029103506 scopus 로고
    • Corallina officinalis bromoperoxidase immobilized on agarose
    • Sheffield, D.J., T.R. Harry, A.J. Smith and L.J. Rogers, 1995. Corallina officinalis bromoperoxidase immobilized on agarose. Phytochemistry, 38: 1103-1107.
    • (1995) Phytochemistry , vol.38 , pp. 1103-1107
    • Sheffield, D.J.1    Harry, T.R.2    Smith, A.J.3    Rogers, L.J.4
  • 43
    • 0000738385 scopus 로고
    • Endospore-forming Gram-positive rods and cocci
    • Holt, J.G, N.R. Krieg, P.H.A. Sneath, J.T. Staley and S.T. Williams Eds, Williams and Wilkins, Baltimore, Section 13
    • Sneath, P.H.A., 1986. Endospore-forming Gram-positive rods and cocci. In: Bergey's Manual of Systematic Bacteriology. Holt, J.G., N.R. Krieg, P.H.A. Sneath, J.T. Staley and S.T. Williams (Eds.), Williams and Wilkins, Baltimore, Vol: 2, Section 13.
    • (1986) Bergey's Manual of Systematic Bacteriology , vol.2
    • Sneath, P.H.A.1
  • 44
    • 0032479216 scopus 로고    scopus 로고
    • The influence of protein folding on late stages of the secretion of α-amylase from Bacillus subtilis
    • Stephenson, K., N. Mo. Carter, C.R. Harwood, M.F. Petitglatron and R. Chambert, 1998. The influence of protein folding on late stages of the secretion of α-amylase from Bacillus subtilis. FEBS Lett., 430: 385-389.
    • (1998) FEBS Lett , vol.430 , pp. 385-389
    • Stephenson, K.1    Carter, N.M.2    Harwood, C.R.3    Petitglatron, M.F.4    Chambert, R.5
  • 45
    • 0033229723 scopus 로고    scopus 로고
    • Immobilization of α-amylase on a zirconium dynamic membrane
    • Tien, C.J. and B.H. Chiang, 1999. Immobilization of α-amylase on a zirconium dynamic membrane. Proc. Biochem., 35: 377-383.
    • (1999) Proc. Biochem , vol.35 , pp. 377-383
    • Tien, C.J.1    Chiang, B.H.2
  • 46
    • 0001025180 scopus 로고
    • Thermostable α-amylase from depressed Bacillus licheniformis produced in high yields from glucose
    • Tonkova, A., R. Monolov and E. Dobreva, 1993. Thermostable α-amylase from depressed Bacillus licheniformis produced in high yields from glucose. Process. Biochem., 28: 539-542.
    • (1993) Process. Biochem , vol.28 , pp. 539-542
    • Tonkova, A.1    Monolov, R.2    Dobreva, E.3
  • 48
    • 0028332440 scopus 로고
    • Characterization of a new Bacillus stearothermophilus isolate: A highly thermostable α-amylase producing strain
    • Wind, R.D., R.M. Buitelaar and G. Eggink, 1994. Characterization of a new Bacillus stearothermophilus isolate: A highly thermostable α-amylase producing strain. Applied Microbiol. Biotechnol., 41: 155-162.
    • (1994) Applied Microbiol. Biotechnol , vol.41 , pp. 155-162
    • Wind, R.D.1    Buitelaar, R.M.2    Eggink, G.3
  • 49
    • 0000534915 scopus 로고
    • Continuous production of maltose using a dual immobilized enzyme system enzyme
    • Yoshida, M., K. Oishi, T. Kimura, M. Ogata and I. Nakakuki, 1989. Continuous production of maltose using a dual immobilized enzyme system enzyme System. Agric. Biol. Chem., 35: 3139-3142.
    • (1989) System. Agric. Biol. Chem , vol.35 , pp. 3139-3142
    • Yoshida, M.1    Oishi, K.2    Kimura, T.3    Ogata, M.4    Nakakuki, I.5


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