메뉴 건너뛰기




Volumn 44, Issue 2, 2006, Pages 275-282

Enhanced production of thermostable pullulanase type 1 using bacillus cereus fdta 13 and its mutant

Author keywords

Bacillus cereus; Mutation; Optimization; Orthogonal array; Polymethylsulphonate fluoride; Thermostable pullulanase

Indexed keywords

CARBON SOURCE; CHEMICAL MUTATION; FERMENTATION CONDITIONS; MUTATION; ORTHOGONAL ARRAY; POLYMETHYLSULPHONATE FLUORIDE; PULLULANASE; YEAST EXTRACTS;

EID: 33745823891     PISSN: 13309862     EISSN: 13309862     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (26)

References (33)
  • 1
    • 17344380706 scopus 로고    scopus 로고
    • Pullulan degrading enzymes of bacterial origin
    • M. Doman-Pytka, J. Bardowski, Pullulan degrading enzymes of bacterial origin, Crit. Rev. Microbiol. 30 (2004) 107-121.
    • (2004) Crit. Rev. Microbiol. , vol.30 , pp. 107-121
    • Doman-Pytka, M.1    Bardowski, J.2
  • 2
    • 0001832594 scopus 로고
    • Microbial degradation of starch
    • G. Winkelman (Ed.), Verlag Chemie, New York, USA
    • G. Antranikian: Microbial Degradation of Starch. In: Microbial Degradation of Natural Products, G. Winkelman (Ed.), Verlag Chemie, New York, USA (1992) pp. 27-56.
    • (1992) Microbial Degradation of Natural Products , pp. 27-56
    • Antranikian, G.1
  • 3
    • 0001588290 scopus 로고
    • Pullulanase (an amylopectin and glycogen debranching enzyme) from Aerobacter aerogenes
    • H. Bender, K. Wallenfels, Pullulanase (an amylopectin and glycogen debranching enzyme) from Aerobacter aerogenes, Methods Enzymol. 8 (1966) 555-559.
    • (1966) Methods Enzymol. , vol.8 , pp. 555-559
    • Bender, H.1    Wallenfels, K.2
  • 4
    • 0002629783 scopus 로고
    • The application of polysaccharide degrading enzymes in starch industry
    • R. Berkley, G.W. Gooday, D.C. Ellwood (Eds.), Academic Press, New York, USA
    • B.E. Norman: The Application of Polysaccharide Degrading Enzymes in Starch Industry. In: Microbial Polysaccharides, R. Berkley, G.W. Gooday, D.C. Ellwood (Eds.), Academic Press, New York, USA (1979) pp. 339-376.
    • (1979) Microbial Polysaccharides , pp. 339-376
    • Norman, B.E.1
  • 5
    • 84987193611 scopus 로고
    • A novel debranching enzymes for application in the glucose syrup industry
    • B.E. Norman, A novel debranching enzymes for application in the glucose syrup industry, Starch/Stärke, 34 (1982) 340-346.
    • (1982) Starch/Stärke , vol.34 , pp. 340-346
    • Norman, B.E.1
  • 6
    • 0032923123 scopus 로고    scopus 로고
    • A new pullulanase from a hyperthermophilic archaeon for starch hydrolysis
    • H. Gantelet, F. Duchiron, A new pullulanase from a hyperthermophilic archaeon for starch hydrolysis, Biotechnol. Lett. 21 (1999) 71-75.
    • (1999) Biotechnol. Lett. , vol.21 , pp. 71-75
    • Gantelet, H.1    Duchiron, F.2
  • 7
    • 0001015742 scopus 로고
    • Bacillus acidopullulyticus pullulanase - Application and regulatory aspects for use in the food industry
    • B.F. Jensen, B.E. Norman, Bacillus acidopullulyticus pullulanase - Application and regulatory aspects for use in the food industry. Process Biochem. 19 (1984) 129-134.
    • (1984) Process Biochem. , vol.19 , pp. 129-134
    • Jensen, B.F.1    Norman, B.E.2
  • 8
    • 0024722550 scopus 로고
    • Novel highly thermostable pullulanase from thermophiles
    • B.C. Saha, J.G. Zeikus, Novel highly thermostable pullulanase from thermophiles, TIBTECH, 7 (1989) 234-239.
    • (1989) TIBTECH , vol.7 , pp. 234-239
    • Saha, B.C.1    Zeikus, J.G.2
  • 9
    • 0020538551 scopus 로고
    • Production of extracellular thermostable pullulanase by an amylolytic obligately thermophilic soil bacterium. Bacillus stearothermophilus KP-1064
    • Y. Suzuki, M. Chishiro, Production of extracellular thermostable pullulanase by an amylolytic obligately thermophilic soil bacterium. Bacillus stearothermophilus KP-1064, Eur. J. Appl. Microbiol. Biotechnol. 17 (1983) 24-29.
    • (1983) Eur. J. Appl. Microbiol. Biotechnol. , vol.17 , pp. 24-29
    • Suzuki, Y.1    Chishiro, M.2
  • 10
    • 0033151659 scopus 로고    scopus 로고
    • Commodity scale production of sugars from starches
    • W.D. Crabb, J.K. Shetty, Commodity scale production of sugars from starches, Curr. Opin. Microbiol. 2 (1999) 252-256.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 252-256
    • Crabb, W.D.1    Shetty, J.K.2
  • 11
    • 0032829805 scopus 로고    scopus 로고
    • Co-expression of saccharifying alkaline amylase and pullulanase in Micrococcus halobius OR-1 isolated from tapioca cultivar soil
    • K.P.R. Devi, G. Yogeeswaran, Co-expression of saccharifying alkaline amylase and pullulanase in Micrococcus halobius OR-1 isolated from tapioca cultivar soil, World J. Microb. Biotechnol. 15 (1999) 223-229.
    • (1999) World J. Microb. Biotechnol. , vol.15 , pp. 223-229
    • Devi, K.P.R.1    Yogeeswaran, G.2
  • 12
    • 0017186924 scopus 로고
    • Production and utilizations of β-amylase and pullulanase from Bacillus cereus var. mycoide
    • Y. Takasaki, Production and utilizations of β-amylase and pullulanase from Bacillus cereus var. mycoide, Agr. Biol. Chem. 40 (1976) 1515-1522.
    • (1976) Agr. Biol. Chem. , vol.40 , pp. 1515-1522
    • Takasaki, Y.1
  • 13
    • 0014296814 scopus 로고
    • Metabolism of the reserve polysaccharide of Streptococcus mitis. Some properties of a pullulanase
    • G.J. Walker, Metabolism of the reserve polysaccharide of Streptococcus mitis. Some properties of a pullulanase, Biochem. J. 108 (1968) 33-40.
    • (1968) Biochem. J. , vol.108 , pp. 33-40
    • Walker, G.J.1
  • 15
    • 0000302658 scopus 로고
    • Production of thermostable α-amylase, pullulanase, and α-glucosidase in continuous culture by a new Clostridium isolate
    • G. Antranikian, C. Herzberg, G. Gottschalk, Production of thermostable α-amylase, pullulanase, and α-glucosidase in continuous culture by a new Clostridium isolate, Appl. Environ. Microbiol. 53 (1987) 1668-1673.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 1668-1673
    • Antranikian, G.1    Herzberg, C.2    Gottschalk, G.3
  • 16
    • 0023655676 scopus 로고
    • Characterization of α-amylase and pullulanase activities of Clostridium thermohydrosulfuricum - Evidence for a novel thermostable amylase
    • H. Melasniemi, Characterization of α-amylase and pullulanase activities of Clostridium thermohydrosulfuricum - Evidence for a novel thermostable amylase, Biochem. J. 246 (1987) 193-197.
    • (1987) Biochem. J. , vol.246 , pp. 193-197
    • Melasniemi, H.1
  • 17
    • 0026028264 scopus 로고
    • Hyperthermostable pullulanase produced by an extreme thermophile, Bacillus flavocaldarius KP 1228, and evidence for the proline theory of increasing protein thermostability
    • Y. Suzuki, K. Hatagaki, H.A. Oda, Hyperthermostable pullulanase produced by an extreme thermophile, Bacillus flavocaldarius KP 1228, and evidence for the proline theory of increasing protein thermostability, Appl. Microbiol. Biotechnol. 34 (1991) 707-714
    • (1991) Appl. Microbiol. Biotechnol. , vol.34 , pp. 707-714
    • Suzuki, Y.1    Hatagaki, K.2    Oda, H.A.3
  • 18
    • 0030715627 scopus 로고    scopus 로고
    • Cloning and sequence of a type i pullulanase from an extremely thermophilic anaerobic bacterium, Caldicellulosiruptor saccharolyticus
    • G.D. Albertson, R.H. Mchale, M.D. Gibbs, P.L. Bergquist, Cloning and sequence of a type I pullulanase from an extremely thermophilic anaerobic bacterium, Caldicellulosiruptor saccharolyticus, BBA-Gene Struct. Expr. 1354 (1997) 35-39.
    • (1997) BBA-Gene Struct. Expr. , vol.1354 , pp. 35-39
    • Albertson, G.D.1    Mchale, R.H.2    Gibbs, M.D.3    Bergquist, P.L.4
  • 19
    • 0031027749 scopus 로고    scopus 로고
    • Purification and properties of a thermostable pullulanase from a newly isolated thermophilic anaerobic bacterium, Fervidobacterium pennavorans Ven5
    • R. Koch, F. Canganella, H. Hippe, K.D. Jahnke, G. Antranikian, Purification and properties of a thermostable pullulanase from a newly isolated thermophilic 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    Jahnke, K.D.4    Antranikian, G.5
  • 20
    • 0031917122 scopus 로고    scopus 로고
    • Production of thermostable amylolytic enzymes by Thermococcus hydrothermalis
    • E. Legin, A. Copinet, F. Duchiron, Production of thermostable amylolytic enzymes by Thermococcus hydrothermalis, Biotechnol. Lett. 20 (1998) 363-367.
    • (1998) Biotechnol. Lett. , vol.20 , pp. 363-367
    • Legin, E.1    Copinet, A.2    Duchiron, F.3
  • 21
    • 0036525719 scopus 로고    scopus 로고
    • Starch-hydrolyzing enzymes from thermophilic archaea and bacteria
    • C. Bertoldo, G. Antranikian, Starch-hydrolyzing enzymes from thermophilic archaea and bacteria, Curr. Opin. Microbiol. 6 (2002) 151-160.
    • (2002) Curr. Opin. Microbiol. , vol.6 , pp. 151-160
    • Bertoldo, C.1    Antranikian, G.2
  • 22
    • 0026705174 scopus 로고
    • Thermostable pullulanase from a mesophilic Bacillus cereus isolate and its mutant UV 7.4
    • A. Bakshi, P.R. Patnaik, J.K. Gupta, Thermostable pullulanase from a mesophilic Bacillus cereus isolate and its mutant UV 7.4, Biotechnol. Lett. 4 (1992) 689-694.
    • (1992) Biotechnol. Lett. , vol.4 , pp. 689-694
    • Bakshi, A.1    Patnaik, P.R.2    Gupta, J.K.3
  • 23
    • 1942538348 scopus 로고    scopus 로고
    • Developments in the use of Bacillus species for industrial production
    • M. Schallmey, A. Singh, O.P. Ward, Developments in the use of Bacillus species for industrial production, Can. J. Microbiol. 50 (2004) 1-17.
    • (2004) Can. J. Microbiol. , vol.50 , pp. 1-17
    • Schallmey, M.1    Singh, A.2    Ward, O.P.3
  • 24
    • 0038696156 scopus 로고    scopus 로고
    • Optimisation of submerged culture conditions for mycelial growth and exo-biopolymer production by Paecilomyces tenuipes C240
    • C. Xu, S. Kim, H. Hwang, J. Choi, J. Yun, Optimisation of submerged culture conditions for mycelial growth and exo-biopolymer production by Paecilomyces tenuipes C240, Process Biochem. 38 (2003) 1025-1030.
    • (2003) Process Biochem. , vol.38 , pp. 1025-1030
    • Xu, C.1    Kim, S.2    Hwang, H.3    Choi, J.4    Yun, J.5
  • 25
    • 0027418073 scopus 로고
    • Effect of mutation of an amino-acid residue near the catalytic site on the activity of Bacillus stearothermophilus alpha-amylase
    • K. Takase, Effect of mutation of an amino-acid residue near the catalytic site on the activity of Bacillus stearothermophilus alpha-amylase, Eur. J. Biochem. 211 (1993) 899-902.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 899-902
    • Takase, K.1
  • 26
    • 0022388164 scopus 로고
    • Regulation and genetic enhancement of glucoamylase and pullulanase production in Clostridium thermohydrosulfuricum
    • H.H. Hyun, J.G. Zeikus, 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
  • 27
    • 0002262344 scopus 로고
    • A plate culture method for simultaneous detection of bacteria producing pullulan and or starch-hydrolyzing enzymes
    • M. Kanno, E. Tomimura, A plate culture method for simultaneous detection of bacteria producing pullulan and or starch-hydrolyzing enzymes, Agr. Biol. Chem. 49 (1985) 1529-1530.
    • (1985) Agr. Biol. Chem. , vol.49 , pp. 1529-1530
    • Kanno, M.1    Tomimura, E.2
  • 28
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugars
    • G.L. Miller, Use of dinitrosalicylic acid reagent for determination of reducing sugars. Anal. Chem. 31 (1959) 426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 29
    • 24044449637 scopus 로고    scopus 로고
    • Nutritional requirements of mycelial growth of Cordyceps sinensis in submerged culture
    • C.H. Dong, Y.J. Yao, Nutritional requirements of mycelial growth of Cordyceps sinensis in submerged culture, J. Appl. Microbiol. 99 (2005) 483-492.
    • (2005) J. Appl. Microbiol. , vol.99 , pp. 483-492
    • Dong, C.H.1    Yao, Y.J.2
  • 30
    • 0000738385 scopus 로고
    • Genus bacillus cohn 1872
    • P.H.A. Sneath, N.S. Mair, M.E. Sharpe, J.G. Holt (Eds.), Williams and Wilkins, Baltimore, USA
    • D. Claus, R.C.W. Berkeley: Genus Bacillus Cohn 1872. In: Bergeys Manual of Systematic Bacteriology, P.H.A. Sneath, N.S. Mair, M.E. Sharpe, J.G. Holt (Eds.), Williams and Wilkins, Baltimore, USA (1986) pp. 1105-1139.
    • (1986) Bergeys Manual of Systematic Bacteriology , pp. 1105-1139
    • Claus, D.1    Berkeley, R.C.W.2
  • 31
    • 0025300853 scopus 로고
    • Physiology and enzymology of thermophilic anaerobic bacteria degrading starch
    • G. Antranikian, 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
  • 32
    • 0031667894 scopus 로고    scopus 로고
    • Characteristics of pullulanases from extremely thermophilic archaea isolated from deep-sea hydrothermal vents
    • H. Gantelet, C. Ladrat, A. Godfroy, G. Barbier, F. Duchiron, Characteristics of pullulanases from extremely thermophilic archaea isolated from deep-sea hydrothermal vents, Biotechnol. Lett. 20 (1998) 819-823.
    • (1998) Biotechnol. Lett. , vol.20 , pp. 819-823
    • Gantelet, H.1    Ladrat, C.2    Godfroy, A.3    Barbier, G.4    Duchiron, F.5
  • 33
    • 34250091040 scopus 로고
    • Purification and characterization of a thermostable pullulanase from Thermoactinomyces thalpophilus
    • F.J.C. Odibo, S.K.C. Obi, Purification and characterization of a thermostable pullulanase from Thermoactinomyces thalpophilus, J. Ind. Microbiol. 3 (1988) 343-350.
    • (1988) J. Ind. Microbiol. , vol.3 , pp. 343-350
    • Odibo, F.J.C.1    Obi, S.K.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.