메뉴 건너뛰기




Volumn 5, Issue 3, 2006, Pages 337-345

Production of a high maltose-forming, hyperthermostable and Ca 2+-independent amylopullulanase by an extreme thermophile Geobacillus thermoleovorans in submerged fermentation

Author keywords

Amylopullulanase; Geobacillus thermoleovorans; Starch hydrolysis; Submerged fermentation

Indexed keywords

AMMONIUM SULFATE; AMYLOPULLULANASE; CALCIUM ION; DETERGENT; DIPOTASSIUM HYDROGEN PHOSPHATE; MAGNESIUM SULFATE; MALTOSE; MALTOTRIOSE; PULLULANASE; SODIUM CHLORIDE; STARCH; SURFACTANT; TRACE ELEMENT; UNCLASSIFIED DRUG;

EID: 33748447483     PISSN: 09725849     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (17)

References (38)
  • 1
    • 0031925343 scopus 로고    scopus 로고
    • Glycosyl hydrolases from hyperthermophilic microorganisms
    • Bauer M W, Driskill L E & Kelly R M, Glycosyl hydrolases from hyperthermophilic microorganisms, Curr Opin Biotechnol, 9 (1998) 141-145.
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 141-145
    • Bauer, M.W.1    Driskill, L.E.2    Kelly, R.M.3
  • 2
    • 0002831485 scopus 로고
    • Biotechnology of thermophilic bacteria-Growth, products, and application
    • Sonnleitner B, Biotechnology of thermophilic bacteria-Growth, products, and application, Adv Biochem Eng Biotechnol, 28 (1983) 69-138.
    • (1983) Adv Biochem Eng Biotechnol , vol.28 , pp. 69-138
    • Sonnleitner, B.1
  • 4
    • 0001484876 scopus 로고
    • Pullulanase-amylase complex enzyme from Bacillus subtilis
    • Takasaki Y, Pullulanase-amylase complex enzyme from Bacillus subtilis, Agric Biol Chem, 51 (1987) 9-16.
    • (1987) Agric Biol Chem , vol.51 , pp. 9-16
    • Takasaki, Y.1
  • 5
    • 0024722550 scopus 로고
    • Novel highly thermostable pullulanase from thermophiles
    • Saha B C & Zeikus J G, Novel highly thermostable pullulanase from thermophiles, Trends Biotechnol, 7 (1989) 234-238.
    • (1989) Trends Biotechnol , vol.7 , pp. 234-238
    • Saha, B.C.1    Zeikus, J.G.2
  • 6
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses and molecular mechanisms for thermostability
    • Vieille C & Zeikus G J, Hyperthermophilic enzymes: Sources, uses and molecular mechanisms for thermostability, Microbiol Mol Biol Rev, 65 (2001) 1-43.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 7
    • 33748442051 scopus 로고    scopus 로고
    • Modified enzyme system to inhibit bread firming method for preparing same and use of same in bread and other bakery products, US Pat 4299848, 10 November, 1981; http://www.uspto.gov/patft/index.html
    • De Stefanis V A & Turner E W, Modified enzyme system to inhibit bread firming method for preparing same and use of same in bread and other bakery products, US Pat 4299848, 10 November, 1981; http://www.uspto.gov/patft/index. html.
    • De Stefanis, V.A.1    Turner, E.W.2
  • 8
    • 0343907736 scopus 로고    scopus 로고
    • Effects of enzyme preparations for baking, mixing time and resting time on bread quality and bread staling
    • Sahlstrom S & Brathen E, Effects of enzyme preparations for baking, mixing time and resting time on bread quality and bread staling, Food Chem, 58 (1997) 175-180.
    • (1997) Food Chem , vol.58 , pp. 175-180
    • Sahlstrom, S.1    Brathen, E.2
  • 11
    • 0025300853 scopus 로고
    • Physiology and enzymology of thermophilic anaerobic bacteria degrading starch
    • Antranikian G, Physiology and enzymology of thermophilic anaerobic bacteria degrading starch, FEMS Microbiol Rev, 75 (1990) 201-218.
    • (1990) FEMS Microbiol Rev , vol.75 , pp. 201-218
    • Antranikian, G.1
  • 12
    • 0036525719 scopus 로고    scopus 로고
    • Starch-hydrolyzing enzymes from thermophilic archaea and bacteria
    • Bertoldo C & Antranikian G, Starch-hydrolyzing enzymes from thermophilic archaea and bacteria, Curr Opin Chem Biol, 6 (2002) 151-160.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 151-160
    • Bertoldo, C.1    Antranikian, G.2
  • 13
    • 2342584768 scopus 로고    scopus 로고
    • Development of an ideal starch saccharification process using amylolytic enzymes from thermophiles
    • Satyanarayana T, Noorwez S M, Kumar S, Rao J L U M, Ezhilvannan M et al, Development of an ideal starch saccharification process using amylolytic enzymes from thermophiles, Biochem Soc Trans, 32 (2004) 276-278.
    • (2004) Biochem Soc Trans , vol.32 , pp. 276-278
    • Satyanarayana, T.1    Noorwez, S.M.2    Kumar, S.3    Rao, J.L.U.M.4    Ezhilvannan, M.5
  • 14
    • 0033748784 scopus 로고    scopus 로고
    • Production and partial characterization of thermostable and calcium-independent α-amylase of an extreme thermophile, Bacillus thermoleovorans NP54
    • Malhotra R, Noorwez S M & Satyanarayana T, Production and partial characterization of thermostable and calcium-independent α-amylase of an extreme thermophile, Bacillus thermoleovorans NP54, 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
  • 15
    • 33748037939 scopus 로고
    • Amylases, α and β
    • Bernfeld P, Amylases, α and β, Methods Enzymol, 1 (1955) 149-158.
    • (1955) Methods Enzymol , vol.1 , pp. 149-158
    • Bernfeld, P.1
  • 16
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic reagent for determination of reducing sugars
    • Miller G L, Use of dinitrosalicylic reagent for determination of reducing sugars, Anal Chem, 31 (1959) 426-428.
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 17
    • 0038119653 scopus 로고    scopus 로고
    • Purification and kinetics of a raw starch-hydrolyzing, thermostable, and neutral glucoamylase of the thermophilic mold Thermomucor indicae-seudaticae
    • Kumar S & Satyanarayana T, Purification and kinetics of a raw starch-hydrolyzing, thermostable, and neutral glucoamylase of the thermophilic mold Thermomucor indicae-seudaticae, Biotechnol Prog, 19 (2003) 936-944.
    • (2003) Biotechnol Prog , vol.19 , pp. 936-944
    • Kumar, S.1    Satyanarayana, T.2
  • 18
    • 0014766893 scopus 로고
    • Substrate specificity of pullulanase
    • Abdullah M & French D, Substrate specificity of pullulanase, Arch Biochem Biophys, 137 (1970) 483-493.
    • (1970) Arch Biochem Biophys , vol.137 , pp. 483-493
    • Abdullah, M.1    French, D.2
  • 20
    • 0028052068 scopus 로고
    • General characteristics of thermostable amylopullulanases and amylases from the alkalophilic Bacillus sp. TS-23
    • Lin L-L, Tsau M-R & Chu W-S, General characteristics of thermostable amylopullulanases and amylases from the alkalophilic Bacillus sp. TS-23, Appl Microbiol Biotechnol, 42 (1994) 51-56.
    • (1994) Appl Microbiol Biotechnol , vol.42 , pp. 51-56
    • Lin, L.-L.1    Tsau, M.-R.2    Chu, W.-S.3
  • 21
    • 0025104602 scopus 로고
    • Physiological and enzymatic characterization of a novel pullulan-degrading thermophilic Bacillus strain 3183
    • Shen G-J, Srivastava K C, Saha B C & Zeikus J G, Physiological and enzymatic characterization of a novel pullulan-degrading thermophilic Bacillus strain 3183, Appl Environ Microbiol, 33 (1990) 340-344.
    • (1990) Appl Environ Microbiol , vol.33 , pp. 340-344
    • Shen, G.-J.1    Srivastava, K.C.2    Saha, B.C.3    Zeikus, J.G.4
  • 22
    • 0025268429 scopus 로고
    • Production of novel pullulanases at high concentrations by two newly isolated thermophilic Clostridia
    • Klingeberg M, Hippe H & Antranikian G, Production of novel pullulanases at high concentrations by two newly isolated thermophilic Clostridia, FEMS Microbiol Lett, 69 (1990) 145-152.
    • (1990) FEMS Microbiol Lett , vol.69 , pp. 145-152
    • Klingeberg, M.1    Hippe, H.2    Antranikian, G.3
  • 23
    • 0027179678 scopus 로고
    • Characterization of amylolytic enzymes, having both α-1,4 and α-1,6 hydrolytic activity, from the thermophilic archaea, Pyrococcus furiosus and Thermococcus littoralis
    • Brown S H & Kelly R M, Characterization of amylolytic enzymes, having both α-1,4 and α-1,6 hydrolytic activity, from the thermophilic archaea, Pyrococcus furiosus and Thermococcus littoralis, Appl Environ Microbiol, 59 (1993) 2614-2621.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 2614-2621
    • Brown, S.H.1    Kelly, R.M.2
  • 24
    • 84987246396 scopus 로고
    • Purification and characterization of a maltotriogenic α-amylase I and a maltogenic α-amylase II capable of cleaving α-1,6-bonds in amylopectin
    • Suzuki Y, Nagayama T, Nakano H & Oishi K, Purification and characterization of a maltotriogenic α-amylase I and a maltogenic α-amylase II capable of cleaving α-1,6-bonds in amylopectin, Starch/Stärke, 39 (1987) 211-214.
    • (1987) Starch/Stärke , vol.39 , pp. 211-214
    • Suzuki, Y.1    Nagayama, T.2    Nakano, H.3    Oishi, K.4
  • 25
    • 0031991241 scopus 로고    scopus 로고
    • Purification and properties of an amylopullulanase, a glucoamylase and an α-glucosidase in the amylolytic enzyme system of Thermoanaerobacterium thermosacchamlyticum
    • Ganghofner D, Kellermann J, Staudenbauer W L & Bronnenmeier K, Purification and properties of an amylopullulanase, a glucoamylase and an α-glucosidase in the amylolytic enzyme system of Thermoanaerobacterium thermosacchamlyticum, Biosci Biotechnol Biochem, 62 (1998) 302-308.
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 302-308
    • Ganghofner, D.1    Kellermann, J.2    Staudenbauer, W.L.3    Bronnenmeier, K.4
  • 27
    • 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 et al, 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 (1995) 315-324.
    • (1995) Biochim Biophys Acta , vol.1243 , pp. 315-324
    • Ara, K.1    Saeki, K.2    Igarashi, K.3    Takaiwa, M.4    Uemura, T.5
  • 28
    • 3543006264 scopus 로고
    • Cultural conditions for protein production by Bacillus brevis No. 47
    • Shaku M, Koike S & Udaka S, Cultural conditions for protein production by Bacillus brevis No. 47, Agric Biol Chem, 44 (1980) 99-103.
    • (1980) Agric Biol Chem , vol.44 , pp. 99-103
    • Shaku, M.1    Koike, S.2    Udaka, S.3
  • 29
    • 0000533474 scopus 로고
    • Influence of environment on the control of enzyme synthesis
    • Demain A C R, Influence of environment on the control of enzyme synthesis, J Appl Chem Biotechnol, 22 (1972) 245-259.
    • (1972) J Appl Chem Biotechnol , vol.22 , pp. 245-259
    • Demain, A.C.R.1
  • 30
    • 0027217955 scopus 로고
    • Improved purification and biochemical characterization of extracellular amylopullulanase from Thermoanaerobacter ethanolicus 39E
    • Mathupala S P & Zeikus J G, Improved purification and biochemical characterization of extracellular amylopullulanase from Thermoanaerobacter ethanolicus 39E, Appl Microbiol Biotechnol. 39 (1993) 487-493.
    • (1993) Appl Microbiol Biotechnol , vol.39 , pp. 487-493
    • Mathupala, S.P.1    Zeikus, J.G.2
  • 31
    • 0028859745 scopus 로고
    • Isolation and characterization of a heat-stable pullulanase from the hyperthermophilic archaeon Pyrococcus woesei after cloning and expression of its gene in Escherichia coli
    • Rudiger A, Jorgensen P L & Antranikian G. Isolation and characterization of a heat-stable pullulanase from the hyperthermophilic archaeon Pyrococcus woesei after cloning and expression of its gene in Escherichia coli, Appl Environ Microbiol, 61 (1995) 567-575.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 567-575
    • Rudiger, A.1    Jorgensen, P.L.2    Antranikian, G.3
  • 32
    • 0022468191 scopus 로고
    • Culture conditions for production of thermostable amylase by Bacillus stearothermophilus
    • Srivastava R A R & Baruah J N, Culture conditions for production of thermostable amylase by Bacillus stearothermophilus, Appl Environ Microbiol, 52 (1986) 179-184.
    • (1986) Appl Environ Microbiol , vol.52 , pp. 179-184
    • Srivastava, R.A.R.1    Baruah, J.N.2
  • 33
    • 0017652017 scopus 로고
    • Extracellular enzyme synthesis in the Genus Bacillus
    • Priest F G, Extracellular enzyme synthesis in the Genus Bacillus, Bacteriol Rev, 41 (1977) 711-753.
    • (1977) Bacteriol Rev , vol.41 , pp. 711-753
    • Priest, F.G.1
  • 34
    • 0022388164 scopus 로고
    • Regulation and genetic enhancement of glucoamylase and pullulanase production in Clostridium thermohydrosulfuricum
    • Hyun H H & Zeikus J G, Regulation and genetic enhancement of glucoamylase and pullulanase production in Clostridium thermohydrosulfuricum, J Bacteriol, 164 (1985) 1146-1152.
    • (1985) J Bacteriol , vol.164 , pp. 1146-1152
    • Hyun, H.H.1    Zeikus, J.G.2
  • 35
    • 0008380429 scopus 로고
    • Induction of α-amylase of Bacillus stearothermophilus by maltodextrins
    • Welker N E & Campbell L L, Induction of α-amylase of Bacillus stearothermophilus by maltodextrins, J Bacteriol, 86 (1963) 687-691.
    • (1963) J Bacteriol , vol.86 , pp. 687-691
    • Welker, N.E.1    Campbell, L.L.2
  • 36
    • 0016635708 scopus 로고
    • Regulating factors affecting α-amylase production in Bacillus licheniformis
    • Saito N & Yamamoto K, Regulating factors affecting α-amylase production in Bacillus licheniformis, J Bacteriol, 121 (1975) 850-856.
    • (1975) J Bacteriol , vol.121 , pp. 850-856
    • Saito, N.1    Yamamoto, K.2
  • 37
    • 0031885663 scopus 로고    scopus 로고
    • Shake flask to fermerter: What have we learnt?
    • Humphrey A, Shake flask to fermerter: What have we learnt?, Biotechnol Prog, 14 (1998) 3-7.
    • (1998) Biotechnol Prog , vol.14 , pp. 3-7
    • Humphrey, A.1
  • 38
    • 0031027749 scopus 로고    scopus 로고
    • Purification and properties of a thermostable pullulanase from a newly isolated anaerobic bacterium Fervidobacterium pennavorans Ven5
    • Koch R, Canganella F, Hippe H, Jhanke K D & Antranikian G, Purification and properties of a thermostable pullulanase from a newly isolated anaerobic bacterium Fervidobacterium pennavorans Ven5, Appl Environ Microbiol, 63 (1997) 1088-1094.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 1088-1094
    • Koch, R.1    Canganella, F.2    Hippe, H.3    Jhanke, K.D.4    Antranikian, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.