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Volumn 5, Issue 2, 2012, Pages 729-737

Statistical Optimization of Pullulanase Production by Raoultella planticola DSMZ 4617 Using Sago Starch as Carbon and Peptone as Nitrogen Sources

Author keywords

Central composite design; Optimization; Pullulanase; Raoultella planticola DSMZ 4617; Response surface methodology; Sago starch

Indexed keywords

CENTRAL COMPOSITE DESIGNS; PULLULANASE; RAOULTELLA PLANTICOLA DSMZ 4617; RESPONSE SURFACE METHODOLOGY; SAGO STARCH;

EID: 84856574411     PISSN: 19355130     EISSN: 19355149     Source Type: Journal    
DOI: 10.1007/s11947-010-0368-7     Document Type: Article
Times cited : (28)

References (38)
  • 1
    • 0032751754 scopus 로고    scopus 로고
    • Osmoprotection of Escherichia coli by peptone is mediated by the uptake and accumulation of free praline but not of praline-containing peptides
    • Amezaga, A. R., & Booth, I. R. (1999). Osmoprotection of Escherichia coli by peptone is mediated by the uptake and accumulation of free praline but not of praline-containing peptides. Applied and Environmental Microbiology, 65, 5272-5278.
    • (1999) Applied and Environmental Microbiology , vol.65 , pp. 5272-5278
    • Amezaga, A.R.1    Booth, I.R.2
  • 2
    • 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., Hagihara, H., et al. (1995). Purification and characterization of an alkaline amylopullulanase with both α-1, 4 and α-1, 6 hydrolytic activity from alkalophilic Bacillus sp. KSM-1378. Biochimica et Biophysica Acta, 1243, 315-324.
    • (1995) Biochimica Et Biophysica Acta , vol.1243 , pp. 315-324
    • Ara, K.1    Saeki, K.2    Igarashi, K.3    Takaiwa, M.4    Uemura, T.5    Hagihara, H.6    Kawai, S.7    Ito, S.8
  • 4
    • 50349094345 scopus 로고    scopus 로고
    • Process optimisation studies of lead biosorption onto immobilized cells of Pycnoporus sanguineus using response surface methodology
    • Azila, Y. Y., Mashitah, M. D., & Bhatia, S. (2008). Process optimisation studies of lead biosorption onto immobilized cells of Pycnoporus sanguineus using response surface methodology. Bioresource Technology, 99, 8549-8552.
    • (2008) Bioresource Technology , vol.99 , pp. 8549-8552
    • Azila, Y.Y.1    Mashitah, M.D.2    Bhatia, S.3
  • 5
    • 0028171099 scopus 로고
    • Characterization of amylolytic and pullulytic enzymes from thermophilic archaea and from a new Fervidobacterium species
    • Canganella, F., Andrade, C. M., & Antranikian, G. (1994). Characterization of amylolytic and pullulytic enzymes from thermophilic archaea and from a new Fervidobacterium species. Applied Microbiology and Biotechnology, 42, 239-245.
    • (1994) Applied Microbiology and Biotechnology , vol.42 , pp. 239-245
    • Canganella, F.1    Andrade, C.M.2    Antranikian, G.3
  • 6
    • 47949120002 scopus 로고    scopus 로고
    • Optimization of media composition for Nattokinase production by Bacillus subtilis using response surface methodology
    • Deepak, V., Kalishwaralal, K., Ramkumarpandian, S., & Babu, S. V. (2008). Optimization of media composition for Nattokinase production by Bacillus subtilis using response surface methodology. Bioresource Technology, 99, 8170-8174.
    • (2008) Bioresource Technology , vol.99 , pp. 8170-8174
    • Deepak, V.1    Kalishwaralal, K.2    Ramkumarpandian, S.3    Babu, S.V.4
  • 7
    • 34547548919 scopus 로고    scopus 로고
    • Optimizing the production of cutinase by Fusarium oxysporum using response surface methodology
    • Fontes-Dio, T., & Alves-Macedo, G. (2007). Optimizing the production of cutinase by Fusarium oxysporum using response surface methodology. Enzyme and Microbial Technology, 41, 613-619.
    • (2007) Enzyme and Microbial Technology , vol.41 , pp. 613-619
    • Fontes-Dio, T.1    Alves-Macedo, G.2
  • 8
    • 0031809735 scopus 로고    scopus 로고
    • Purification and properties of a thermoactive and thermostable pullulanase from Thermococcus hydrothermalis, a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
    • Gantelet, H., & Duchiron, F. (1998). Purification and properties of a thermoactive and thermostable pullulanase from Thermococcus hydrothermalis, a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent. Applied Microbiology and Biotechnology, 49, 770-777.
    • (1998) Applied Microbiology and Biotechnology , vol.49 , pp. 770-777
    • Gantelet, H.1    Duchiron, F.2
  • 9
    • 0043170899 scopus 로고    scopus 로고
    • Highly thermostable amylase and pullulanase of the extreme thermophilic eubacterium Rhodothermus marinus: production and partial characterization
    • Gomes, I., Gomes, J., & Steiner, W. (2003). Highly thermostable amylase and pullulanase of the extreme thermophilic eubacterium Rhodothermus marinus: production and partial characterization. Bioresource Technolology, 90, 207-214.
    • (2003) Bioresource Technolology , vol.90 , pp. 207-214
    • Gomes, I.1    Gomes, J.2    Steiner, W.3
  • 11
    • 77953454588 scopus 로고    scopus 로고
    • Enhancement of extracellular pullulanase production by Raoultella planticola DSMZ 4617 using optimized medium based on sago starch
    • Hii, S. L., Ling, T. C., Rosfarizan, M., & Ariff, A. B. (2009b). Enhancement of extracellular pullulanase production by Raoultella planticola DSMZ 4617 using optimized medium based on sago starch. The Open Biotechnology Journal, 3, 1-8.
    • (2009) The Open Biotechnology Journal , vol.3 , pp. 1-8
    • Hii, S.L.1    Ling, T.C.2    Rosfarizan, M.3    Ariff, A.B.4
  • 12
    • 7444234893 scopus 로고    scopus 로고
    • Optimization of medium for the production of β-cyclodextrin glucanotransferase using Central Composite Design (CCD)
    • Ibrahim, H. M., Yusoff, W. W. M., Hamid, A. A., Illias, R. M., Hassan, O., & Omar, O. (2005). Optimization of medium for the production of β-cyclodextrin glucanotransferase using Central Composite Design (CCD). Process Biochemistry, 40, 753-758.
    • (2005) Process Biochemistry , vol.40 , pp. 753-758
    • Ibrahim, H.M.1    Yusoff, W.W.M.2    Hamid, A.A.3    Illias, R.M.4    Hassan, O.5    Omar, O.6
  • 13
    • 33748746493 scopus 로고    scopus 로고
    • Improved high thermal stability of pullulanase from a newly isolated thermophilic Bacillus sp. AN-7
    • Kunamneni, A., & Singh, S. (2006). Improved high thermal stability of pullulanase from a newly isolated thermophilic Bacillus sp. AN-7. Enzyme and Microbial Technology, 39, 1399-1404.
    • (2006) Enzyme and Microbial Technology , vol.39 , pp. 1399-1404
    • Kunamneni, A.1    Singh, S.2
  • 14
    • 15744373608 scopus 로고    scopus 로고
    • Immobilisation and stabilization of pullulanase from Klebsiella pneumoniae by a multipoint attachment method using activated agar gel supports
    • Kuroiwa, T., Shoda, H., Ichikawa, S., Sato, S., & Mukataka, S. (2005). Immobilisation and stabilization of pullulanase from Klebsiella pneumoniae by a multipoint attachment method using activated agar gel supports. Process Biochemistry, 40, 2637-2642.
    • (2005) Process Biochemistry , vol.40 , pp. 2637-2642
    • Kuroiwa, T.1    Shoda, H.2    Ichikawa, S.3    Sato, S.4    Mukataka, S.5
  • 15
    • 59249096043 scopus 로고    scopus 로고
    • Effect of pullulanase debranching and recrystallization on structure and digestibility of waxy maize starch
    • Miao, M., Jiang, B., & Zhang, T. (2009). Effect of pullulanase debranching and recrystallization on structure and digestibility of waxy maize starch. Carbohydrate Polymers, 76, 214-221.
    • (2009) Carbohydrate Polymers , vol.76 , pp. 214-221
    • Miao, M.1    Jiang, B.2    Zhang, T.3
  • 16
    • 0022365856 scopus 로고
    • Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae
    • Michaelis, S., Chapon, C., D'enfert, C., Pugsley, A. P., & Schwartz, M. (1985). Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae. Journal of Bacteriology, 164, 633-638.
    • (1985) Journal of Bacteriology , vol.164 , pp. 633-638
    • Michaelis, S.1    Chapon, C.2    D'Enfert, C.3    Pugsley, A.P.4    Schwartz, M.5
  • 17
    • 33747333106 scopus 로고
    • Use of dinitrosalycilic acid reagent for determination of reducing sugars
    • Miller, G. L. (1959). Use of dinitrosalycilic acid reagent for determination of reducing sugars. Analytical Chemistry, 31, 426-428.
    • (1959) Analytical Chemistry , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 19
    • 0024378491 scopus 로고
    • Biosynthesis and secretion of pullulanase, a lipoprotein from Klebsiella aerogenes
    • Murooka, Y., & Ikeda, R. (1989). Biosynthesis and secretion of pullulanase, a lipoprotein from Klebsiella aerogenes. The Journal of Biological Chemistry, 264, 17524-17531.
    • (1989) The Journal of Biological Chemistry , vol.264 , pp. 17524-17531
    • Murooka, Y.1    Ikeda, R.2
  • 20
    • 33745823891 scopus 로고    scopus 로고
    • Enhanced production of thermostable pullulanase type 1 using Bacillus cereus FDTA 13 and its mutant
    • Nair, S. U., Singhal, R. S., & Kamat, M. Y. (2006). Enhanced production of thermostable pullulanase type 1 using Bacillus cereus FDTA 13 and its mutant. Food Technology and Biotechnology, 44, 275-282.
    • (2006) Food Technology and Biotechnology , vol.44 , pp. 275-282
    • Nair, S.U.1    Singhal, R.S.2    Kamat, M.Y.3
  • 21
    • 33748523479 scopus 로고    scopus 로고
    • Induction of pullulanase production in Bacillus cereus FDTA-13
    • Nair, S. U., Singhal, R. S., & Kamat, M. Y. (2007). Induction of pullulanase production in Bacillus cereus FDTA-13. Bioresource Technology, 98, 856-859.
    • (2007) Bioresource Technology , vol.98 , pp. 856-859
    • Nair, S.U.1    Singhal, R.S.2    Kamat, M.Y.3
  • 22
    • 0002056409 scopus 로고    scopus 로고
    • Some properties of starch debranching enzymes and their possible role in amylopectin biosynthesis
    • Nakamura, Y. (1996). Some properties of starch debranching enzymes and their possible role in amylopectin biosynthesis. Plant Science, 121, 1-18.
    • (1996) Plant Science , vol.121 , pp. 1-18
    • Nakamura, Y.1
  • 23
    • 7444263568 scopus 로고    scopus 로고
    • Optimization of chitinase production using statistics based experimental designs
    • Nawani, N. N., & Kapadnis, B. P. (2005). Optimization of chitinase production using statistics based experimental designs. Process Biochemistry, 40, 651-660.
    • (2005) Process Biochemistry , vol.40 , pp. 651-660
    • Nawani, N.N.1    Kapadnis, B.P.2
  • 24
    • 0031005016 scopus 로고    scopus 로고
    • Energy requirement for pullulanase secretion by the main terminal branch of the general secretory pathway
    • Possot, O. M., Letellier, L., & Pugsley, A. P. (1997). Energy requirement for pullulanase secretion by the main terminal branch of the general secretory pathway. Molecular Microbiology, 24, 457-464.
    • (1997) Molecular Microbiology , vol.24 , pp. 457-464
    • Possot, O.M.1    Letellier, L.2    Pugsley, A.P.3
  • 25
    • 4344616504 scopus 로고    scopus 로고
    • Optimization of growth medium for the production of cyclodextrin glucanotransferase from Bacillus stearothermophilus HR 1 using response surface methodology
    • Rahman, R. A., Illias, R. M., Mohd Nawawi, M. G., Ismail, A. F., Hassan, O., & Kamaruddin, K. (2004). Optimization of growth medium for the production of cyclodextrin glucanotransferase from Bacillus stearothermophilus HR 1 using response surface methodology. Process Biochemistry, 39, 2053-2060.
    • (2004) Process Biochemistry , vol.39 , pp. 2053-2060
    • Rahman, R.A.1    Illias, R.M.2    Mohd Nawawi, M.G.3    Ismail, A.F.4    Hassan, O.5    Kamaruddin, K.6
  • 26
    • 0343279008 scopus 로고    scopus 로고
    • Effect of various flours on the production of thermostable β-amylase and pullulanase by Clostridium thermosulfurogenes SV 2
    • Ramesh, B., Reddy, P. R. M., Seenayya, G., & Reddy, G. (2001). Effect of various flours on the production of thermostable β-amylase and pullulanase by Clostridium thermosulfurogenes SV 2. Bioresource Technology, 76, 169-171.
    • (2001) Bioresource Technology , vol.76 , pp. 169-171
    • Ramesh, B.1    Reddy, P.R.M.2    Seenayya, G.3    Reddy, G.4
  • 27
    • 0032796296 scopus 로고    scopus 로고
    • Production of thermostable pullulanase by Clostridium thermosulfurogenes SV2 in solid-state fermentation: optimization of nutrients levels using response surface methodology
    • Reddy, P. R. M., Reddy, G., & Seenayya, G. (1999). Production of thermostable pullulanase by Clostridium thermosulfurogenes SV2 in solid-state fermentation: optimization of nutrients levels using response surface methodology. Bioprocess Engineering, 21, 497-503.
    • (1999) Bioprocess Engineering , vol.21 , pp. 497-503
    • Reddy, P.R.M.1    Reddy, G.2    Seenayya, G.3
  • 28
    • 0036381075 scopus 로고    scopus 로고
    • Important of carbon source feeding and pH control strategies for maximum kojic acid production from sago starch by A. flavus
    • Rosfarizan, M., Ariff, A. B., Hassan, M. A., Karim, M. I. A., Shimizu, H., & Shioya, S. (2002). Important of carbon source feeding and pH control strategies for maximum kojic acid production from sago starch by A. flavus. Journal of Bioscience and Bioengineering, 94, 99-105.
    • (2002) Journal of Bioscience and Bioengineering , vol.94 , pp. 99-105
    • Rosfarizan, M.1    Ariff, A.B.2    Hassan, M.A.3    Karim, M.I.A.4    Shimizu, H.5    Shioya, S.6
  • 29
    • 15244356424 scopus 로고    scopus 로고
    • Optimization of medium composition for alkali-stable xylanase production by Aspergillus fischeri Fxn 1 in solid-state fermentation using central composite rotary design
    • Senthilkumar, S. R., Ashokkumar, B., Chandra Raj, K., & Gunasekaran, P. (2005). Optimization of medium composition for alkali-stable xylanase production by Aspergillus fischeri Fxn 1 in solid-state fermentation using central composite rotary design. Bioresource Technology, 96, 1380-1386.
    • (2005) Bioresource Technology , vol.96 , pp. 1380-1386
    • Senthilkumar, S.R.1    Ashokkumar, B.2    Chandra Raj, K.3    Gunasekaran, P.4
  • 30
    • 77953913671 scopus 로고    scopus 로고
    • A case study on optimization of biomass flow during single-screw extrusion cooking using genetic algorithm (GA) and response surface method (RSM)
    • doi:10.1007/s 1 1947-008-0172-9
    • Shankar, T. J., Sokhansanj, S., Bandyopadhyay, S., & Bawa, A. S. (2010). A case study on optimization of biomass flow during single-screw extrusion cooking using genetic algorithm (GA) and response surface method (RSM). Food and Bioprocess Technology. doi: 10. 1007/s11947-008-0172-9.
    • (2010) Food and Bioprocess Technology
    • Shankar, T.J.1    Sokhansanj, S.2    Bandyopadhyay, S.3    Bawa, A.S.4
  • 31
    • 34548646609 scopus 로고    scopus 로고
    • Optimisation of culture medium for rifamycin SV production by Amycolatopsis mediterranei MM2 using statistical designs
    • Shin, H. J., Kim, C. J., & Kim, S. B. (2007). Optimisation of culture medium for rifamycin SV production by Amycolatopsis mediterranei MM2 using statistical designs. Biotechnology and Bioprocess Engineering, 12, 457-461.
    • (2007) Biotechnology and Bioprocess Engineering , vol.12 , pp. 457-461
    • Shin, H.J.1    Kim, C.J.2    Kim, S.B.3
  • 32
    • 54049122924 scopus 로고    scopus 로고
    • Rheological behaviour of pullulanase-treated guar galactomannan on co-gelation with xanthan
    • Shobha, M. S., & Tharanathan, R. N. (2009). Rheological behaviour of pullulanase-treated guar galactomannan on co-gelation with xanthan. Food Hydrocolloids, 23, 749-754.
    • (2009) Food Hydrocolloids , vol.23 , pp. 749-754
    • Shobha, M.S.1    Tharanathan, R.N.2
  • 33
    • 84921077258 scopus 로고
    • A photometric method for the determination of α-amylase in blood and urine with use of the starch-iodine colour
    • Smith, B. W., & Roe, J. H. (1948). A photometric method for the determination of α-amylase in blood and urine with use of the starch-iodine colour. The Journal of Biological Chemistry, 179, 53-57.
    • (1948) The Journal of Biological Chemistry , vol.179 , pp. 53-57
    • Smith, B.W.1    Roe, J.H.2
  • 34
    • 0029185778 scopus 로고    scopus 로고
    • Thermostable pullulanase and α-amylase activity from Clostridium thermosulfurogenes SV 9-optimization of culture conditions for enzyme production
    • Swamy, M. V., & Seenayya, G. (1996). Thermostable pullulanase and α-amylase activity from Clostridium thermosulfurogenes SV 9-optimization of culture conditions for enzyme production. Process Biochemistry, 31, 157-162.
    • (1996) Process Biochemistry , vol.31 , pp. 157-162
    • Swamy, M.V.1    Seenayya, G.2
  • 35
    • 0021964980 scopus 로고
    • Cloning of the pullulanase gene and overproduction of pullulanase in Escherichia coli and Klebsiella aerogenes
    • Takizawa, N., & Murooka, Y. (1985). Cloning of the pullulanase gene and overproduction of pullulanase in Escherichia coli and Klebsiella aerogenes. Applied and Environmental Microbiology, 49, 294-2988.
    • (1985) Applied and Environmental Microbiology , vol.49 , pp. 294-2988
    • Takizawa, N.1    Murooka, Y.2
  • 37
    • 28844470263 scopus 로고    scopus 로고
    • Amylopullulanase: A novel enzyme of L. amylophilus GV6 in direct fermentation of starch to L(+) lactic acid
    • Vishnu, C., Naveena, B. J., Altaf, M. D., Venkateshwar, M., & Reddy, G. (2006). Amylopullulanase: A novel enzyme of L. amylophilus GV6 in direct fermentation of starch to L(+) lactic acid. Enzyme and Microbial Technology, 38, 645-550.
    • (2006) Enzyme and Microbial Technology , vol.38 , pp. 550-645
    • Vishnu, C.1    Naveena, B.J.2    Altaf, M.D.3    Venkateshwar, M.4    Reddy, G.5
  • 38
    • 33745456900 scopus 로고    scopus 로고
    • Enzymatic production of linear long-chain dextrin from sago (Metroxylon sagu) starch
    • Wong, C. W., Muhammad, S. K. S., Dzulkifly, M. H., Saari, N., & Ghazali, H. M. (2007). Enzymatic production of linear long-chain dextrin from sago (Metroxylon sagu) starch. Food Chemistry, 100, 774-780.
    • (2007) Food Chemistry , vol.100 , pp. 774-780
    • Wong, C.W.1    Muhammad, S.K.S.2    Dzulkifly, M.H.3    Saari, N.4    Ghazali, H.M.5


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