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Volumn 46, Issue 3, 2009, Pages 306-312

Purification of CBS 819.72 α-amylase by aqueous two-phase systems: Modelling using Response Surface Methodology

Author keywords

Amylase; Aqueous two phase system; Aspergillus oryzae; Modelling; PEG citrate; Purification; Response Surface Methodology

Indexed keywords

AQUEOUS TWO-PHASE SYSTEM; ASPERGILLUS ORYZAE; MODELLING; PEG/CITRATE; RESPONSE SURFACE METHODOLOGY;

EID: 67749143575     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2009.06.003     Document Type: Article
Times cited : (50)

References (49)
  • 1
    • 8344232634 scopus 로고    scopus 로고
    • Biomanufacturing, from bust to boom...to bubble
    • Thiel K.A. Biomanufacturing, from bust to boom...to bubble. Nat. Biotechnol. 22 (2004) 1365-1372
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1365-1372
    • Thiel, K.A.1
  • 2
    • 2942722679 scopus 로고    scopus 로고
    • Antibodies and genetically engineered related molecules: production and purification
    • Roque A.C.A., Lowe C.R., and Taipa M.A. Antibodies and genetically engineered related molecules: production and purification. Biotechnol. Prog. 20 (2004) 639-654
    • (2004) Biotechnol. Prog. , vol.20 , pp. 639-654
    • Roque, A.C.A.1    Lowe, C.R.2    Taipa, M.A.3
  • 3
    • 34250879050 scopus 로고    scopus 로고
    • Purification of recombinant phenylalanine dehydrogenase by partitioning in aqueous two-phase systems
    • Mohamadi H.S., and Omidinia E. Purification of recombinant phenylalanine dehydrogenase by partitioning in aqueous two-phase systems. J. Chromatogr. B 854 (2007) 273-278
    • (2007) J. Chromatogr. B , vol.854 , pp. 273-278
    • Mohamadi, H.S.1    Omidinia, E.2
  • 5
    • 12944276863 scopus 로고    scopus 로고
    • Partial purification of α-amylase from culture supernatant of Bacillus subtilis in aqueous two-phase systems
    • Zhi W., Song J., Bi J., and Ouyang F. Partial purification of α-amylase from culture supernatant of Bacillus subtilis in aqueous two-phase systems. Bioprocess Biosyst. Eng. 27 (2004) 3-7
    • (2004) Bioprocess Biosyst. Eng. , vol.27 , pp. 3-7
    • Zhi, W.1    Song, J.2    Bi, J.3    Ouyang, F.4
  • 6
    • 33846011124 scopus 로고    scopus 로고
    • Application of central composite design to the optimisation of aqueous two-phase extraction of human antibodies
    • Rosa P.A.J., Azevedo A.M., and Aires-Barros M.R. Application of central composite design to the optimisation of aqueous two-phase extraction of human antibodies. J. Chromatogr. A 1141 (2007) 50-60
    • (2007) J. Chromatogr. A , vol.1141 , pp. 50-60
    • Rosa, P.A.J.1    Azevedo, A.M.2    Aires-Barros, M.R.3
  • 7
    • 34948903826 scopus 로고    scopus 로고
    • Continuous extraction of α- and β-amylases from Zea mays malt in a PEG4000/CaCl2 ATPS
    • Biazus J.P.M., Santana J.C.C., Souza R.R., Jord E., and Tambourgi E.B. Continuous extraction of α- and β-amylases from Zea mays malt in a PEG4000/CaCl2 ATPS. J. Chromatogr. B 858 (2007) 227-233
    • (2007) J. Chromatogr. B , vol.858 , pp. 227-233
    • Biazus, J.P.M.1    Santana, J.C.C.2    Souza, R.R.3    Jord, E.4    Tambourgi, E.B.5
  • 8
    • 0035814330 scopus 로고    scopus 로고
    • Typespecific separation of animal cells in aqueous two-phase systems using antibody conjugates with temperature-sensitive polymers
    • Kumar A., Kamihira M., Galaev I.Y., Mattiasson B., and Iijima S. Typespecific separation of animal cells in aqueous two-phase systems using antibody conjugates with temperature-sensitive polymers. Biotechnol. Bioeng. 75 (2001) 570-580
    • (2001) Biotechnol. Bioeng. , vol.75 , pp. 570-580
    • Kumar, A.1    Kamihira, M.2    Galaev, I.Y.3    Mattiasson, B.4    Iijima, S.5
  • 9
    • 2642553792 scopus 로고    scopus 로고
    • Separation and purification of methoxypoly(ethylene glycol) grafted red blood cells via two-phase partitioning
    • Bradley A.J., and Scott M.D. Separation and purification of methoxypoly(ethylene glycol) grafted red blood cells via two-phase partitioning. J. Chromatogr. B: Analyt. Technol. Biomed. Life Sci. 807 1 (2004) 163-168
    • (2004) J. Chromatogr. B: Analyt. Technol. Biomed. Life Sci. , vol.807 , Issue.1 , pp. 163-168
    • Bradley, A.J.1    Scott, M.D.2
  • 11
    • 0028923769 scopus 로고
    • Two rapid microscale procedures for isolation of total RNA from leaves rich in polyphenols and polysaccharides: application for sensitive detection of grapevine viroids
    • Staub U., Polivka H., and Gross H.J. Two rapid microscale procedures for isolation of total RNA from leaves rich in polyphenols and polysaccharides: application for sensitive detection of grapevine viroids. J. Virol. Methods 52 (1995) 209-218
    • (1995) J. Virol. Methods , vol.52 , pp. 209-218
    • Staub, U.1    Polivka, H.2    Gross, H.J.3
  • 12
    • 0348110469 scopus 로고    scopus 로고
    • Extraction of plasmid DNA from Escherichia coli cell lysate in a thermoseparating aqueous two-phase system
    • Kepka C., Rhodin J., Lemmens R., Tjerneld F., and Gustavsson P.E. Extraction of plasmid DNA from Escherichia coli cell lysate in a thermoseparating aqueous two-phase system. J. Chromatogr. A 1024 (2004) 95-104
    • (2004) J. Chromatogr. A , vol.1024 , pp. 95-104
    • Kepka, C.1    Rhodin, J.2    Lemmens, R.3    Tjerneld, F.4    Gustavsson, P.E.5
  • 13
    • 20544442647 scopus 로고    scopus 로고
    • Purification of plasmid DNA vectors by aqueous two-phase extraction and hydrophobic interaction chromatography
    • Trindade I.P., Diogo M.M., Prazeres D.M., and Marcos J.C. Purification of plasmid DNA vectors by aqueous two-phase extraction and hydrophobic interaction chromatography. J. Chromatogr. A 1082 2 (2005) 176-184
    • (2005) J. Chromatogr. A , vol.1082 , Issue.2 , pp. 176-184
    • Trindade, I.P.1    Diogo, M.M.2    Prazeres, D.M.3    Marcos, J.C.4
  • 15
    • 0037213311 scopus 로고    scopus 로고
    • An overview on fermentation, downstream processing and properties of microbial alkaline proteases
    • Gupta R., Beg Q.K., Khan S., and Chauhan B. An overview on fermentation, downstream processing and properties of microbial alkaline proteases. Appl. Microbiol. Biotechnol. 60 4 (2002) 381-395
    • (2002) Appl. Microbiol. Biotechnol. , vol.60 , Issue.4 , pp. 381-395
    • Gupta, R.1    Beg, Q.K.2    Khan, S.3    Chauhan, B.4
  • 16
    • 2642572488 scopus 로고    scopus 로고
    • Purification of hyperthermophilic archaeal amylolytic enzyme (MJA1) using thermoseparating aqueous two-phase systems
    • Li M., and Peeples T.L. Purification of hyperthermophilic archaeal amylolytic enzyme (MJA1) using thermoseparating aqueous two-phase systems. J. Chromatogr. B 807 (2004) 69-74
    • (2004) J. Chromatogr. B , vol.807 , pp. 69-74
    • Li, M.1    Peeples, T.L.2
  • 17
    • 21244500953 scopus 로고    scopus 로고
    • Application of response surface methodology to the modeling of α-amylase purification by aqueous two-phase systems
    • Zhi W., Song J., Ouyang F., and Bi J. Application of response surface methodology to the modeling of α-amylase purification by aqueous two-phase systems. J. Biotechnol. 118 (2005) 157-165
    • (2005) J. Biotechnol. , vol.118 , pp. 157-165
    • Zhi, W.1    Song, J.2    Ouyang, F.3    Bi, J.4
  • 18
    • 33646129677 scopus 로고    scopus 로고
    • Partitioning of β-glucosidase from Trichoderma reesei in poly(ethylene glycol) and potassium phosphate aqueous two-phase systems: influence of pH and temperature
    • Gautam S., and Simon L. Partitioning of β-glucosidase from Trichoderma reesei in poly(ethylene glycol) and potassium phosphate aqueous two-phase systems: influence of pH and temperature. Biochem. Eng. J. 30 (2006) 104-108
    • (2006) Biochem. Eng. J. , vol.30 , pp. 104-108
    • Gautam, S.1    Simon, L.2
  • 19
    • 33645999646 scopus 로고    scopus 로고
    • Thermostable d-carbamoylase from Sinorhizobium morelens S-5: purification, characterization and gene expression in Escherichia coli
    • Wu S., Liu Y., Zhao G., Wang J., and Sun W. Thermostable d-carbamoylase from Sinorhizobium morelens S-5: purification, characterization and gene expression in Escherichia coli. Biochimie 88 3-4 (2006) 237-244
    • (2006) Biochimie , vol.88 , Issue.3-4 , pp. 237-244
    • Wu, S.1    Liu, Y.2    Zhao, G.3    Wang, J.4    Sun, W.5
  • 20
    • 31944444062 scopus 로고    scopus 로고
    • Purification of potato polyphenol oxidase (PPO) by partitioning in aqueous two-phase system
    • Vaidya B.K., Suthar H.K., Kasture S., and Nene S. Purification of potato polyphenol oxidase (PPO) by partitioning in aqueous two-phase system. Biochem. Eng. J. 28 (2006) 161-166
    • (2006) Biochem. Eng. J. , vol.28 , pp. 161-166
    • Vaidya, B.K.1    Suthar, H.K.2    Kasture, S.3    Nene, S.4
  • 21
    • 33344459675 scopus 로고    scopus 로고
    • Optimization of reversed micellar extraction of chitosanases produced by Bacillus cereus
    • Chen Y.L., Su C.K., and Chiang B.H. Optimization of reversed micellar extraction of chitosanases produced by Bacillus cereus. Process Biochem. 41 (2006) 752-758
    • (2006) Process Biochem. , vol.41 , pp. 752-758
    • Chen, Y.L.1    Su, C.K.2    Chiang, B.H.3
  • 22
    • 2642513866 scopus 로고    scopus 로고
    • Mass transfer in aqueous two-phases system packed column
    • Igarashi L., Kieckbuschn T.G., and Franco T.T. Mass transfer in aqueous two-phases system packed column. J. Chromatogr. B 807 (2004) 75-80
    • (2004) J. Chromatogr. B , vol.807 , pp. 75-80
    • Igarashi, L.1    Kieckbuschn, T.G.2    Franco, T.T.3
  • 23
    • 28944446897 scopus 로고    scopus 로고
    • Aqueous two-phase partitioning of xylanase produced by solid-state cultivation of Polyporus squamosus
    • Antov M.G., Peričin D.M., and Dašić M.G. Aqueous two-phase partitioning of xylanase produced by solid-state cultivation of Polyporus squamosus. Process Biochem. 41 (2006) 232-235
    • (2006) Process Biochem. , vol.41 , pp. 232-235
    • Antov, M.G.1    Peričin, D.M.2    Dašić, M.G.3
  • 24
    • 33745073083 scopus 로고    scopus 로고
    • Direct comparison between ion-exchange chromatography and aqueous two-phase processes for the partial purification of penicillin acylase produced by E. coli
    • Aguilar O., Albiter V., Serrano-Carréon L., and Rito-Palomares M. Direct comparison between ion-exchange chromatography and aqueous two-phase processes for the partial purification of penicillin acylase produced by E. coli. J. Chromatogr. B 835 (2006) 77-83
    • (2006) J. Chromatogr. B , vol.835 , pp. 77-83
    • Aguilar, O.1    Albiter, V.2    Serrano-Carréon, L.3    Rito-Palomares, M.4
  • 25
    • 0347063915 scopus 로고    scopus 로고
    • Purification of phospholipase D by two-phase affinity extraction
    • Teotia S., and Gupta M.N. Purification of phospholipase D by two-phase affinity extraction. J. Chromatogr. A 1025 2 (2004) 297-301
    • (2004) J. Chromatogr. A , vol.1025 , Issue.2 , pp. 297-301
    • Teotia, S.1    Gupta, M.N.2
  • 26
    • 2342451294 scopus 로고    scopus 로고
    • Purification of xylose reductase from Candida mogii in aqueous two-phase systems
    • Mayerhoff Z.D.V.L., Roberto I.C., and Franco T.T. Purification of xylose reductase from Candida mogii in aqueous two-phase systems. Biochem. Eng. J. 18 (2004) 217-223
    • (2004) Biochem. Eng. J. , vol.18 , pp. 217-223
    • Mayerhoff, Z.D.V.L.1    Roberto, I.C.2    Franco, T.T.3
  • 27
    • 2642531799 scopus 로고    scopus 로고
    • Practical application of aqueous two-phase partition to process development for the recovery of biological products
    • Rito-Palomares M. Practical application of aqueous two-phase partition to process development for the recovery of biological products. J. Chromatogr. B 807 (2002) 3-11
    • (2002) J. Chromatogr. B , vol.807 , pp. 3-11
    • Rito-Palomares, M.1
  • 30
    • 0034468230 scopus 로고    scopus 로고
    • Scale-up of recombinant cutinase recovery by whole broth extraction with PEG-phosphate aqueous two-phase
    • Costa M.J.L., Cunha M.T., Cabral J.M.S., and Aires-Barros M.R. Scale-up of recombinant cutinase recovery by whole broth extraction with PEG-phosphate aqueous two-phase. Bioseparation 9 4 (2000) 231-238
    • (2000) Bioseparation , vol.9 , Issue.4 , pp. 231-238
    • Costa, M.J.L.1    Cunha, M.T.2    Cabral, J.M.S.3    Aires-Barros, M.R.4
  • 31
    • 0034705668 scopus 로고    scopus 로고
    • Investigation of aqueous biphasic systems for the separation of lignins from cellulose in the paper pulping process
    • Willauer H.D., Huddleston J.G., Li M., and Rogers R.D. Investigation of aqueous biphasic systems for the separation of lignins from cellulose in the paper pulping process. J. Chromatogr. B 743 (2000) 127-135
    • (2000) J. Chromatogr. B , vol.743 , pp. 127-135
    • Willauer, H.D.1    Huddleston, J.G.2    Li, M.3    Rogers, R.D.4
  • 32
    • 37449027774 scopus 로고    scopus 로고
    • Protein partitioning in poly(ethylene glycol)/sodium polyacrylate aqueous two-phase systems
    • Johansson H.O., Magaldi F.M., Feitosa Jr. E., and Adalberto Pessoa A. Protein partitioning in poly(ethylene glycol)/sodium polyacrylate aqueous two-phase systems. J. Chromatogr. A 1178 (2008) 145-153
    • (2008) J. Chromatogr. A , vol.1178 , pp. 145-153
    • Johansson, H.O.1    Magaldi, F.M.2    Feitosa Jr., E.3    Adalberto Pessoa, A.4
  • 33
    • 0034705688 scopus 로고    scopus 로고
    • Bioaffinity extraction of glucoamylase in aqueous two-phase systems using starch as free bioligand
    • De Gouveia T., and Kilikian B.V. Bioaffinity extraction of glucoamylase in aqueous two-phase systems using starch as free bioligand. J. Chromatogr. B: Biomed. Sci. Appl. 743 1-2 (2000) 241-246
    • (2000) J. Chromatogr. B: Biomed. Sci. Appl. , vol.743 , Issue.1-2 , pp. 241-246
    • De Gouveia, T.1    Kilikian, B.V.2
  • 34
    • 43049162197 scopus 로고    scopus 로고
    • Application of a statistical design to the optimization of parameters and culture medium for alpha-amylase production by Aspergillus oryzae CBS 819.72 grown on gruel (wheat grinding by-product)
    • Kammoun R., Naili B., and Bejar S. Application of a statistical design to the optimization of parameters and culture medium for alpha-amylase production by Aspergillus oryzae CBS 819.72 grown on gruel (wheat grinding by-product). Bioresour. Technol. 99 13 (2008) 5602-5609
    • (2008) Bioresour. Technol. , vol.99 , Issue.13 , pp. 5602-5609
    • Kammoun, R.1    Naili, B.2    Bejar, S.3
  • 36
    • 36849083174 scopus 로고    scopus 로고
    • Recombinant human proinsulin from transgenic corn endosperm: solvent screening and extraction studies
    • Farinas C.S., Leite A., and Miranda E.A. Recombinant human proinsulin from transgenic corn endosperm: solvent screening and extraction studies. Braz. J. Chem. Eng. 24 03 (2007) 315-323
    • (2007) Braz. J. Chem. Eng. , vol.24 , Issue.3 , pp. 315-323
    • Farinas, C.S.1    Leite, A.2    Miranda, E.A.3
  • 37
    • 40749106458 scopus 로고    scopus 로고
    • Process optimization studies on solvent extraction with naphthalene-2-boronic acid ion-pairing with trioctylmethylammonium chloride in sugar purification using design of experiments
    • Abdul Aziz H., Kamaruddin A.H., and Abu Bakar M.Z. Process optimization studies on solvent extraction with naphthalene-2-boronic acid ion-pairing with trioctylmethylammonium chloride in sugar purification using design of experiments. Sep. Purif. Technol. 60 2 (2008) 190-197
    • (2008) Sep. Purif. Technol. , vol.60 , Issue.2 , pp. 190-197
    • Abdul Aziz, H.1    Kamaruddin, A.H.2    Abu Bakar, M.Z.3
  • 38
    • 78651031122 scopus 로고
    • Enzymes of starch degradation and synthesis
    • Bernfeld P. Enzymes of starch degradation and synthesis. Adv. Enzymol. 12 (1951) 397-427
    • (1951) Adv. Enzymol. , vol.12 , pp. 397-427
    • Bernfeld, P.1
  • 39
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 40
    • 0001131698 scopus 로고
    • The design of optimum multifactorial experiments
    • Plackett R.L., and Burman J.P. The design of optimum multifactorial experiments. Biometrika 33 (1946) 305-325
    • (1946) Biometrika , vol.33 , pp. 305-325
    • Plackett, R.L.1    Burman, J.P.2
  • 41
    • 23144461645 scopus 로고    scopus 로고
    • Experimental design for the formulation and optimization of novel cross-linked oilispheres developed for in vitro site-specific release of Mentha piperita oil
    • Article 18 (http://www.aapspharmscitech.org/)
    • Sibanda W., Pillay V., Danckwerts M.P., Viljoen A.M., Vuuren S.V., and Khan R.A. Experimental design for the formulation and optimization of novel cross-linked oilispheres developed for in vitro site-specific release of Mentha piperita oil. AAPS Pharm. Sci. Tech. 5 1 (2004). http://www.aapspharmscitech.org/ Article 18 (http://www.aapspharmscitech.org/)
    • (2004) AAPS Pharm. Sci. Tech. , vol.5 , Issue.1
    • Sibanda, W.1    Pillay, V.2    Danckwerts, M.P.3    Viljoen, A.M.4    Vuuren, S.V.5    Khan, R.A.6
  • 42
    • 67749127663 scopus 로고
    • Process for the production of solution stable alpha-amylase and liquid alpha-amylase produced thereby,
    • US Patent 4,724,208
    • J.W. Brewer, Y.K. Chong, J.M. Curtis, K.S. Jayarama, Process for the production of solution stable alpha-amylase and liquid alpha-amylase produced thereby, US Patent 4,724,208 (1988).
    • (1988)
    • Brewer, J.W.1    Chong, Y.K.2    Curtis, J.M.3    Jayarama, K.S.4
  • 43
    • 53049088555 scopus 로고    scopus 로고
    • Aqueous two-phase extraction (ATPE): an attractive and economically viable technology for downstream processing of Aspergillus oryzae α-galactosidase
    • Naganagouda K., and Mulimani V.H. Aqueous two-phase extraction (ATPE): an attractive and economically viable technology for downstream processing of Aspergillus oryzae α-galactosidase. Process Biochem. 43 (2008) 1293-1299
    • (2008) Process Biochem. , vol.43 , pp. 1293-1299
    • Naganagouda, K.1    Mulimani, V.H.2
  • 44
    • 33646129677 scopus 로고    scopus 로고
    • Partitioning of β-glucosidase from Trichoderma reesei in poly (ethylene glycol) and potassium phosphate aqueous two-phase systems: influence of pH and temperature
    • Gautam S., and Simon L. Partitioning of β-glucosidase from Trichoderma reesei in poly (ethylene glycol) and potassium phosphate aqueous two-phase systems: influence of pH and temperature. Biochem. Eng. J. 30 (2006) 104-108
    • (2006) Biochem. Eng. J. , vol.30 , pp. 104-108
    • Gautam, S.1    Simon, L.2
  • 45
    • 0028177532 scopus 로고
    • Partitioning and purification of α-amylase in aqueous two-phase systems
    • Schmid A.S., Ventom A.M., and Asenjo J.A. Partitioning and purification of α-amylase in aqueous two-phase systems. Enzyme Microb. Technol. 16 (1994) 131-142
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 131-142
    • Schmid, A.S.1    Ventom, A.M.2    Asenjo, J.A.3
  • 46
    • 0035185611 scopus 로고    scopus 로고
    • Partitioning and separation of α-lactalbumin and β-lactoglobulin in polyethylene glycol/ammonium sulphate aqueous two-phase systems
    • Rodrigues L.R., Venâncio A., and Teixeira J.A. Partitioning and separation of α-lactalbumin and β-lactoglobulin in polyethylene glycol/ammonium sulphate aqueous two-phase systems. Biotechnol. Lett. 23 (2001) 1893-1897
    • (2001) Biotechnol. Lett. , vol.23 , pp. 1893-1897
    • Rodrigues, L.R.1    Venâncio, A.2    Teixeira, J.A.3
  • 48
    • 67749110224 scopus 로고    scopus 로고
    • Downstream processing of antibodies: single-stage versus multi-stage aqueous two-phase extraction
    • doi:10.1016/j.chroma.2009.02.024
    • Rosa P.A.J., Azevedo A.M., Ferreira I.F., Sommerfeld S., Bäcker W., and Aires-Barros M.R. Downstream processing of antibodies: single-stage versus multi-stage aqueous two-phase extraction. J. Chromatogr. A (2009) doi:10.1016/j.chroma.2009.02.024
    • (2009) J. Chromatogr. A
    • Rosa, P.A.J.1    Azevedo, A.M.2    Ferreira, I.F.3    Sommerfeld, S.4    Bäcker, W.5    Aires-Barros, M.R.6


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