메뉴 건너뛰기




Volumn 31, Issue 5, 2008, Pages 509-517

An efficient immobilizing technique of penicillin acylase with combining mesocellular silica foams support and p-benzoquinone cross linker

Author keywords

Covalent immobilization; Macromolecular crowding; Mesocellular silica foams; Nanopore; Penicillin acylase

Indexed keywords

DEPOSITS; ENZYME ACTIVITY; ENZYMES; FOOD ADDITIVES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; FOURIER TRANSFORMS; INFRARED SPECTROSCOPY; POWER AMPLIFIERS; SILICA; SILICATE MINERALS; SILICON COMPOUNDS; SPECTROSCOPIC ANALYSIS; SULFIDE MINERALS;

EID: 47349112456     PISSN: 16157591     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00449-007-0189-x     Document Type: Article
Times cited : (37)

References (34)
  • 1
    • 20544476972 scopus 로고    scopus 로고
    • Immobilization of Penicillin G Acylase: The Key to Optimum Performance
    • AI Kallenberg FV Rantwijk RA Sheldon 2005 Immobilization of Penicillin G Acylase: The Key to Optimum Performance Adv Synth Catal 347 905 926
    • (2005) Adv Synth Catal , vol.347 , pp. 905-926
    • Kallenberg, A.I.1    Rantwijk, F.V.2    Sheldon, R.A.3
  • 2
    • 3543148392 scopus 로고    scopus 로고
    • Improved β-lactam acylases and their use as industrial biocatalysts
    • CF Sio WJ Quax 2004 Improved β-lactam acylases and their use as industrial biocatalysts Curr Opin Biotechnol 15 349 355
    • (2004) Curr Opin Biotechnol , vol.15 , pp. 349-355
    • Sio, C.F.1    Quax, W.J.2
  • 3
    • 33745966261 scopus 로고    scopus 로고
    • Polyelectrolyte complex formation mediated immobilization of chitosan-invertase neoglycoconjugate on pectin-coated chitin
    • L Gómez HL Ramírez A Neira-Carrillo R Villalonga 2006 Polyelectrolyte complex formation mediated immobilization of chitosan-invertase neoglycoconjugate on pectin-coated chitin Bioprocess Biosyst Eng 28 387 395
    • (2006) Bioprocess Biosyst Eng , vol.28 , pp. 387-395
    • Gómez, L.1    Ramírez, H.L.2    Neira-Carrillo, A.3    Villalonga, R.4
  • 5
    • 33847166926 scopus 로고    scopus 로고
    • A new method for immobilization of acetylcholinesterase
    • H Tümtürk F Sahin G Demirel 2007 A new method for immobilization of acetylcholinesterase Bioprocess Biosyst Eng 30 141 145
    • (2007) Bioprocess Biosyst Eng , vol.30 , pp. 141-145
    • Tümtürk, H.1    Sahin, F.2    Demirel, G.3
  • 6
    • 0034274420 scopus 로고    scopus 로고
    • Eupergit C, a carrier for immobilization of enzymes of industrial potential
    • E Katchalski-Katzir DM Kraemer 2000 Eupergit C, a carrier for immobilization of enzymes of industrial potential J Mol Catal B: Enzym 10 157 176
    • (2000) J Mol Catal B: Enzym , vol.10 , pp. 157-176
    • Katchalski-Katzir, E.1    Kraemer, D.M.2
  • 7
    • 7744226759 scopus 로고    scopus 로고
    • Enhanced catalytic activity of hemoglobin in organic solvents by layered titanate immobilization
    • Q Wang Q Gao J Shi 2004 Enhanced catalytic activity of hemoglobin in organic solvents by layered titanate immobilization J Am Chem Soc 126 14346 14347
    • (2004) J Am Chem Soc , vol.126 , pp. 14346-14347
    • Wang, Q.1    Gao, Q.2    Shi, J.3
  • 8
    • 4344649335 scopus 로고    scopus 로고
    • Design of large-pore mesoporous materials for immobilization of penicillin G acylase biocatalyst
    • AS Maria Chong XS Zhao 2004 Design of large-pore mesoporous materials for immobilization of penicillin G acylase biocatalyst Catal Today 93-95 293 299
    • (2004) Catal Today , vol.93-95 , pp. 293-299
    • Maria Chong, A.S.1    Zhao, X.S.2
  • 9
    • 0038306713 scopus 로고    scopus 로고
    • Organically modified xerogels as novel tailor-made supports for covalent immobilization of enzymes (penicillin G acylase)
    • A Basso L De Martin C Ebert 2003 Organically modified xerogels as novel tailor-made supports for covalent immobilization of enzymes (penicillin G acylase) Tetrahedron Lett 44 5889 5891
    • (2003) Tetrahedron Lett , vol.44 , pp. 5889-5891
    • Basso, A.1    De Martin, L.2    Ebert, C.3
  • 10
    • 34547209337 scopus 로고    scopus 로고
    • Enzyme immobilization: The quest for optimum performance
    • RA Sheldon 2007 Enzyme immobilization: the quest for optimum performance Adv Synth Catal 349 1289 1307
    • (2007) Adv Synth Catal , vol.349 , pp. 1289-1307
    • Sheldon, R.A.1
  • 11
    • 0035949430 scopus 로고    scopus 로고
    • Stabilization of proteins in confined spaces
    • HX Zhou KA Dill 2001 Stabilization of proteins in confined spaces Biochemistry 40 11289 11293
    • (2001) Biochemistry , vol.40 , pp. 11289-11293
    • Zhou, H.X.1    Dill, K.A.2
  • 12
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • AP Minton 2001 The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media J Biol Chem 276 10577 10580
    • (2001) J Biol Chem , vol.276 , pp. 10577-10580
    • Minton, A.P.1
  • 13
    • 33846044706 scopus 로고    scopus 로고
    • Characterization of functionalized nanoporous supports for protein confinement
    • C Lei Y Shin JK Magnuson G Fryxell 2006 Characterization of functionalized nanoporous supports for protein confinement Nanotechnology 17 5531 5538
    • (2006) Nanotechnology , vol.17 , pp. 5531-5538
    • Lei, C.1    Shin, Y.2    Magnuson, J.K.3    Fryxell, G.4
  • 14
    • 33749845982 scopus 로고    scopus 로고
    • Complex biocatalyst assembled by enzyme and inorganic/ metal nanoparticles
    • J Zong YW Chen SB Shen 2006 Complex biocatalyst assembled by enzyme and inorganic/ metal nanoparticles J Chem Ind Eng (China) 57 1777 1781
    • (2006) J Chem Ind Eng (China) , vol.57 , pp. 1777-1781
    • Zong, J.1    Chen, Y.W.2    Shen, S.B.3
  • 15
    • 33644676244 scopus 로고    scopus 로고
    • Poly (GMA/MA/MBAA) copolymer beads: A highly efficient support immobilizing penicillin G acylase
    • P Xue GZ Lu WY Liu 2006 Poly (GMA/MA/MBAA) copolymer beads: a highly efficient support immobilizing penicillin G acylase Chin Chem Lett 17 129 132
    • (2006) Chin Chem Lett , vol.17 , pp. 129-132
    • Xue, P.1    Lu, G.Z.2    Liu, W.Y.3
  • 16
    • 33344476423 scopus 로고    scopus 로고
    • Nanopore-protein interactions dramatically alter stability and yield of the native state in restricted spaces
    • MS Cheung D Thirumalai 2006 Nanopore-protein interactions dramatically alter stability and yield of the native state in restricted spaces J Mol Biol 357 632 643
    • (2006) J Mol Biol , vol.357 , pp. 632-643
    • Cheung, M.S.1    Thirumalai, D.2
  • 17
    • 16344389134 scopus 로고    scopus 로고
    • Molecular crowding enhances native state stability and refolding rates of globular proteins
    • MS Cheung D Klimov D Thirumalai 2005 Molecular crowding enhances native state stability and refolding rates of globular proteins Proc Natl Acad Sci USA 102 4753 4758
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 4753-4758
    • Cheung, M.S.1    Klimov, D.2    Thirumalai, D.3
  • 18
    • 0033550516 scopus 로고    scopus 로고
    • Mesocellular siliceous foams with uniformly sized cells and windows
    • P Schmidt-Winkel WW Lukens D Zhao 1999 Mesocellular siliceous foams with uniformly sized cells and windows J Am Chem Soc 121 254 255
    • (1999) J Am Chem Soc , vol.121 , pp. 254-255
    • Schmidt-Winkel, P.1    Lukens, W.W.2    Zhao, D.3
  • 19
    • 0037161884 scopus 로고    scopus 로고
    • Microwave assisted template removal of siliceous porous materials
    • B Tian X Liu C Yu 2002 Microwave assisted template removal of siliceous porous materials Chem Commun (Camb) 7 1186 1187
    • (2002) Chem Commun (Camb) , vol.7 , pp. 1186-1187
    • Tian, B.1    Liu, X.2    Yu, C.3
  • 20
    • 20444406055 scopus 로고
    • Controlled growth of monodisperse silica spheres in the micron size range
    • W Stöber A Fink E Bohn 1968 Controlled growth of monodisperse silica spheres in the micron size range J Colloid Interface Sci 26 62 69
    • (1968) J Colloid Interface Sci , vol.26 , pp. 62-69
    • Stöber, W.1    Fink, A.2    Bohn, E.3
  • 21
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • MMA Bradford 1976 Rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding Anal Biochem 72 248 250
    • (1976) Anal Biochem , vol.72 , pp. 248-250
    • Bradford, M.M.A.1
  • 22
    • 0002083389 scopus 로고
    • Evaluation of determination of 6-aminopenicillanic acid by p-dimethylaminobenzaldehyde
    • JG Shewale KK Kumar GR Ambekar 1987 Evaluation of determination of 6-aminopenicillanic acid by p-dimethylaminobenzaldehyde Biotechnol Tech 1 69 72
    • (1987) Biotechnol Tech , vol.1 , pp. 69-72
    • Shewale, J.G.1    Kumar, K.K.2    Ambekar, G.R.3
  • 23
    • 0037142781 scopus 로고    scopus 로고
    • Active site titration as a tool for the evaluation of immobilization procedures of penicillin acylase
    • LM Van Langen MHA Janssen NHP Oosthoek 2002 Active site titration as a tool for the evaluation of immobilization procedures of penicillin acylase Biotech Bioeng 79 223 227
    • (2002) Biotech Bioeng , vol.79 , pp. 223-227
    • Van Langen, L.M.1    Janssen, M.H.A.2    Oosthoek, N.H.P.3
  • 24
    • 33645301003 scopus 로고    scopus 로고
    • A new method for spectrophotometric assay of activity of cross-linked penicillin acylase aggregates
    • NA Pchelintsev MI Youshko VK Ŝvedas 2006 A new method for spectrophotometric assay of activity of cross-linked penicillin acylase aggregates Biochemistry (Mosc) 71 315 319
    • (2006) Biochemistry (Mosc) , vol.71 , pp. 315-319
    • Pchelintsev, N.A.1    Youshko, M.I.2    Ŝvedas, V.K.3
  • 25
    • 0028847040 scopus 로고
    • Lyophilization-Induced Reversible Changes in the Secondary Structure of Proteins
    • K Griebenow AM Klibanov 1995 Lyophilization-Induced Reversible Changes in the Secondary Structure of Proteins Proc Natl Acad Sci USA 92 10969 10976
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10969-10976
    • Griebenow, K.1    Klibanov, A.M.2
  • 28
    • 33847205076 scopus 로고    scopus 로고
    • Effects of macroporous resin size on Candida antarctica lipase B adsorption, fraction of active molecules, and catalytic activity for polyester synthesis
    • B Chen EM Miller RA Gross 2007 Effects of macroporous resin size on Candida antarctica lipase B adsorption, fraction of active molecules, and catalytic activity for polyester synthesis Langmuir 23 1381 1387
    • (2007) Langmuir , vol.23 , pp. 1381-1387
    • Chen, B.1    Miller, E.M.2    Gross, R.A.3
  • 30
    • 0030773072 scopus 로고    scopus 로고
    • Stabilization of Escherichia coli penicillin G acylase against thermal inactivation by cross-linking with dextran dialdehyde polymers
    • D Kazan H Ertan A Erarslan 1997 Stabilization of Escherichia coli penicillin G acylase against thermal inactivation by cross-linking with dextran dialdehyde polymers Appl Microbiol Biotechnol 48 191 197
    • (1997) Appl Microbiol Biotechnol , vol.48 , pp. 191-197
    • Kazan, D.1    Ertan, H.2    Erarslan, A.3
  • 32
    • 0025357111 scopus 로고
    • Proteins secondary structures in water from second-derivative amide-I infrared spectra
    • AC Dong P Huang WS Caughey 1990 Proteins secondary structures in water from second-derivative amide-I infrared spectra Biochemistry 29 3303 3308
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.C.1    Huang, P.2    Caughey, W.S.3
  • 34
    • 0033004064 scopus 로고    scopus 로고
    • How does a protein unfold on a reversed phase liquid chromatography surface
    • JL Mcnay EJ Fernandez 1999 How does a protein unfold on a reversed phase liquid chromatography surface J Chromatogr A 849 135 148
    • (1999) J Chromatogr a , vol.849 , pp. 135-148
    • McNay, J.L.1    Fernandez, E.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.