메뉴 건너뛰기




Volumn 44, Issue 6, 2009, Pages 641-646

Reactivation of covalently immobilized lipase from Thermomyces lanuginosus

Author keywords

Enzyme inactivation; Enzyme reactivation; Immobilized enzymes; Operational stabilization; Unfolding refolding

Indexed keywords

ENZYME INACTIVATION; ENZYME REACTIVATION; IMMOBILIZED ENZYMES; OPERATIONAL STABILIZATION; UNFOLDING-REFOLDING;

EID: 64749098154     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2009.02.001     Document Type: Article
Times cited : (38)

References (43)
  • 2
    • 33751193431 scopus 로고    scopus 로고
    • Hydroxypropyl-β-cyclodextrin induced complexation for the biocatalytic resolution of a poorly soluble epoxide
    • Yeates C.A., Krieg H.M., and Breytenbach J.C. Hydroxypropyl-β-cyclodextrin induced complexation for the biocatalytic resolution of a poorly soluble epoxide. Enzyme Microb Technol 40 (2007) 228-235
    • (2007) Enzyme Microb Technol , vol.40 , pp. 228-235
    • Yeates, C.A.1    Krieg, H.M.2    Breytenbach, J.C.3
  • 3
    • 33847135275 scopus 로고    scopus 로고
    • Substrate supply for effective biocatalysis
    • Kim P.Y., Pollard D.J., and Woodley J.M. Substrate supply for effective biocatalysis. Biotechnol Prog 23 (2007) 74-82
    • (2007) Biotechnol Prog , vol.23 , pp. 74-82
    • Kim, P.Y.1    Pollard, D.J.2    Woodley, J.M.3
  • 4
    • 33846084325 scopus 로고    scopus 로고
    • Asymmetric reduction and oxidation of aromatic ketones and alcohols using W110A secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus
    • Musa M.M., Ziegelmann-Fjeld K.I., Vieille C., Zeikus J.G., and Phillips R.S. Asymmetric reduction and oxidation of aromatic ketones and alcohols using W110A secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus. J Org Chem 72 (2007) 30-34
    • (2007) J Org Chem , vol.72 , pp. 30-34
    • Musa, M.M.1    Ziegelmann-Fjeld, K.I.2    Vieille, C.3    Zeikus, J.G.4    Phillips, R.S.5
  • 6
    • 52949085077 scopus 로고    scopus 로고
    • Carrier-bound and carrier-free penicillin acylase biocatalysts for the thermodynamically controlled synthesis of β-lactam compounds in organic medium
    • Wilson L., Illanes A., Romero O., Vergara J., and Mateo C. Carrier-bound and carrier-free penicillin acylase biocatalysts for the thermodynamically controlled synthesis of β-lactam compounds in organic medium. Enzyme Microb Technol 43 (2008) 442-447
    • (2008) Enzyme Microb Technol , vol.43 , pp. 442-447
    • Wilson, L.1    Illanes, A.2    Romero, O.3    Vergara, J.4    Mateo, C.5
  • 7
    • 0032189174 scopus 로고    scopus 로고
    • The presence of methanol exerts a strong and complex modulation of the synthesis of different antibiotics by immobilized Penicillin G acylase
    • Fernández-Lafuente R., Rosell C.M., and Guisán J.M. The presence of methanol exerts a strong and complex modulation of the synthesis of different antibiotics by immobilized Penicillin G acylase. Enzyme Microb Technol 23 (1998) 305-310
    • (1998) Enzyme Microb Technol , vol.23 , pp. 305-310
    • Fernández-Lafuente, R.1    Rosell, C.M.2    Guisán, J.M.3
  • 8
    • 0034884338 scopus 로고    scopus 로고
    • Biotransformations catalyzed by multimeric enzymes: stabilization of tetrameric ampicillin acylase permits the optimization of ampicillin synthesis under dissociation conditions
    • Fernández-Lafuente R., Hernández-Jústiz O., Mateo C., Terreni M., Fernández-Lorente G., Moreno M.A., et al. Biotransformations catalyzed by multimeric enzymes: stabilization of tetrameric ampicillin acylase permits the optimization of ampicillin synthesis under dissociation conditions. Biomacromolecules 2 (2001) 95-104
    • (2001) Biomacromolecules , vol.2 , pp. 95-104
    • Fernández-Lafuente, R.1    Hernández-Jústiz, O.2    Mateo, C.3    Terreni, M.4    Fernández-Lorente, G.5    Moreno, M.A.6
  • 9
    • 34447313904 scopus 로고    scopus 로고
    • The stability of engineered thermostable neutral proteases from Bacillus stearothermophilus in organic solvents and detergents
    • Mansfeld J., and Ulbrich-Hofmann R. The stability of engineered thermostable neutral proteases from Bacillus stearothermophilus in organic solvents and detergents. Biotechnol Bioeng 97 (2007) 672-679
    • (2007) Biotechnol Bioeng , vol.97 , pp. 672-679
    • Mansfeld, J.1    Ulbrich-Hofmann, R.2
  • 10
    • 33846575689 scopus 로고    scopus 로고
    • Stabilization of phenylalanine ammonia lyase against organic solvent mediated deactivation
    • Shah R.M., and D'Mello A.P. Stabilization of phenylalanine ammonia lyase against organic solvent mediated deactivation. Int J Pharm 331 (2007) 107-115
    • (2007) Int J Pharm , vol.331 , pp. 107-115
    • Shah, R.M.1    D'Mello, A.P.2
  • 11
    • 50849139867 scopus 로고    scopus 로고
    • Enzyme stability and stabilization: aqueous and non-aqueous environment
    • Iyer P.V., and Ananthanarayan L. Enzyme stability and stabilization: aqueous and non-aqueous environment. Process Biochem 43 (2008) 1019-1032
    • (2008) Process Biochem , vol.43 , pp. 1019-1032
    • Iyer, P.V.1    Ananthanarayan, L.2
  • 13
    • 46849092215 scopus 로고    scopus 로고
    • Cold active microbial lipases: some hot issues and recent developments
    • Joseph B., Ramteke P.W., and Thomas G. Cold active microbial lipases: some hot issues and recent developments. Biotechnol Adv 26 (2008) 457-470
    • (2008) Biotechnol Adv , vol.26 , pp. 457-470
    • Joseph, B.1    Ramteke, P.W.2    Thomas, G.3
  • 14
    • 33846209146 scopus 로고    scopus 로고
    • Trends in lipase-catalyzed asymmetric access to enantiomerically pure/enriched compounds
    • Ghanem A. Trends in lipase-catalyzed asymmetric access to enantiomerically pure/enriched compounds. Tetrahedron 63 (2007) 1721-1754
    • (2007) Tetrahedron , vol.63 , pp. 1721-1754
    • Ghanem, A.1
  • 15
    • 33646565623 scopus 로고    scopus 로고
    • Biocatalysis as a profound tool in the preparation of highly enantiopure β-amino acids
    • Liljeblad A., and Kanerva L.T. Biocatalysis as a profound tool in the preparation of highly enantiopure β-amino acids. Tetrahedron 62 (2006) 5831-5854
    • (2006) Tetrahedron , vol.62 , pp. 5831-5854
    • Liljeblad, A.1    Kanerva, L.T.2
  • 17
    • 38049012808 scopus 로고    scopus 로고
    • X-ray structure of candida antarctica Lipase A shows a novel lid structure and a likely mode of interfacial activation
    • Ericsson D.J., Kasrayan A., Johansson P., Bergfors T., Sandstrom A.G., Backvall J.E., et al. X-ray structure of candida antarctica Lipase A shows a novel lid structure and a likely mode of interfacial activation. J Mol Biol 376 (2008) 109-119
    • (2008) J Mol Biol , vol.376 , pp. 109-119
    • Ericsson, D.J.1    Kasrayan, A.2    Johansson, P.3    Bergfors, T.4    Sandstrom, A.G.5    Backvall, J.E.6
  • 18
    • 0034642243 scopus 로고    scopus 로고
    • Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase
    • Brzozowski A.M., Savage H., Verma C.S., Turkenburg J.P., Lawson D.M., Svendsen A., et al. Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase. Biochemistry 39 (2000) 15071-15082
    • (2000) Biochemistry , vol.39 , pp. 15071-15082
    • Brzozowski, A.M.1    Savage, H.2    Verma, C.S.3    Turkenburg, J.P.4    Lawson, D.M.5    Svendsen, A.6
  • 19
    • 0032510716 scopus 로고    scopus 로고
    • Interfacial activation of triglyceride lipase from Thermomyces (Humicola) lanuginosa: kinetic parameters and a basis for control of the lid
    • Berg O.G., Cajal Y., Butterfoss G.L., Grey R.L., Alsina M.A., Yu B.Z., et al. Interfacial activation of triglyceride lipase from Thermomyces (Humicola) lanuginosa: kinetic parameters and a basis for control of the lid. Biochemistry 37 (1998) 6615-6627
    • (1998) Biochemistry , vol.37 , pp. 6615-6627
    • Berg, O.G.1    Cajal, Y.2    Butterfoss, G.L.3    Grey, R.L.4    Alsina, M.A.5    Yu, B.Z.6
  • 20
    • 0017114559 scopus 로고
    • Mechanism of pancreatic lipase action 1. Interfacial activation of pancreatic lipase
    • Chapus C., Sémériva M., Bovier-Lapierre C., and Desnuelle P. Mechanism of pancreatic lipase action 1. Interfacial activation of pancreatic lipase. Biochemistry 15 (1976) 4980-4987
    • (1976) Biochemistry , vol.15 , pp. 4980-4987
    • Chapus, C.1    Sémériva, M.2    Bovier-Lapierre, C.3    Desnuelle, P.4
  • 21
    • 0026418174 scopus 로고
    • A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex
    • Brzozowski A.M., Derewenda U., Derewenda Z.S., Dodson G.G., Lawson D.M., Turkenburg J.P., et al. A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature 351 (1991) 491-494
    • (1991) Nature , vol.351 , pp. 491-494
    • Brzozowski, A.M.1    Derewenda, U.2    Derewenda, Z.S.3    Dodson, G.G.4    Lawson, D.M.5    Turkenburg, J.P.6
  • 22
    • 0034927657 scopus 로고    scopus 로고
    • Kinetic studies of Rhizopus oryzae lipase using monomolecular film technique
    • Ben Salah A., Sayari A., Verger R., and Gargouri Y. Kinetic studies of Rhizopus oryzae lipase using monomolecular film technique. Biochimie 83 (2001) 463-469
    • (2001) Biochimie , vol.83 , pp. 463-469
    • Ben Salah, A.1    Sayari, A.2    Verger, R.3    Gargouri, Y.4
  • 24
    • 0032486523 scopus 로고    scopus 로고
    • A single step purification, immobilization, and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports
    • Bastida A., Sabuquillo P., Armisen P., Fernández-Lafuente R., Huguet J., and Guisán J.M. A single step purification, immobilization, and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports. Biotechnol Bioeng 58 (1998) 486-493
    • (1998) Biotechnol Bioeng , vol.58 , pp. 486-493
    • Bastida, A.1    Sabuquillo, P.2    Armisen, P.3    Fernández-Lafuente, R.4    Huguet, J.5    Guisán, J.M.6
  • 28
    • 0026648514 scopus 로고
    • Stability and reconstitution of d-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima
    • Rehaber V., and Jaenicke R. Stability and reconstitution of d-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima. J Biol Chem 267 (1992) 10999-11006
    • (1992) J Biol Chem , vol.267 , pp. 10999-11006
    • Rehaber, V.1    Jaenicke, R.2
  • 29
    • 0027062923 scopus 로고
    • Renaturation of citrate synthase: influence of denaturant and folding assistants
    • Zhi W., Landry S.J., Gierasch L.M., and Srere P.A. Renaturation of citrate synthase: influence of denaturant and folding assistants. Protein Sci 1 (1992) 522-529
    • (1992) Protein Sci , vol.1 , pp. 522-529
    • Zhi, W.1    Landry, S.J.2    Gierasch, L.M.3    Srere, P.A.4
  • 30
    • 35448937272 scopus 로고    scopus 로고
    • Effect of nonionic detergents on the activity of a thermostable lipase from Bacillus stearothermophilus MC7
    • Guncheva M., Zhiryakova D., Radchenkova N., and Kambourova M. Effect of nonionic detergents on the activity of a thermostable lipase from Bacillus stearothermophilus MC7. J Mol Catal B: Enzym 49 (2007) 88-91
    • (2007) J Mol Catal B: Enzym , vol.49 , pp. 88-91
    • Guncheva, M.1    Zhiryakova, D.2    Radchenkova, N.3    Kambourova, M.4
  • 31
    • 13444278724 scopus 로고    scopus 로고
    • Activation, inhibition, and destabilization of Thermomyces lanuginosus lipase by detergents
    • Mogensen J.E., Sehgal P., and Otzen D.E. Activation, inhibition, and destabilization of Thermomyces lanuginosus lipase by detergents. Biochemistry 44 (2005) 1719-1730
    • (2005) Biochemistry , vol.44 , pp. 1719-1730
    • Mogensen, J.E.1    Sehgal, P.2    Otzen, D.E.3
  • 32
    • 34249828658 scopus 로고    scopus 로고
    • Improved catalytic properties of immobilized lipases by the presence of very low concentrations of detergents in the reaction medium
    • Fernandez-Lorente G., Palomo J.M., Cabrera Z., Fernandez-Lafuente R., and Guisán J.M. Improved catalytic properties of immobilized lipases by the presence of very low concentrations of detergents in the reaction medium. Biotechnol Bioeng 97 (2007) 242-250
    • (2007) Biotechnol Bioeng , vol.97 , pp. 242-250
    • Fernandez-Lorente, G.1    Palomo, J.M.2    Cabrera, Z.3    Fernandez-Lafuente, R.4    Guisán, J.M.5
  • 33
    • 0028939393 scopus 로고
    • Interfacial activation-based molecular bioimprinting of lipolytic enzymes
    • Mingarro I., Abad C., and Braco L. Interfacial activation-based molecular bioimprinting of lipolytic enzymes. Proc Natl Acad Sci USA 92 (1995) 3308-3312
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3308-3312
    • Mingarro, I.1    Abad, C.2    Braco, L.3
  • 34
    • 33749545520 scopus 로고    scopus 로고
    • Glutaraldehyde cross-linking of lipases adsorbed on aminated supports in the presence of detergents leads to improved performance
    • Fernández-Lorente G., Palomo J.M., Mateo C., Munilla R., Ortiz C., Cabrera Z., et al. Glutaraldehyde cross-linking of lipases adsorbed on aminated supports in the presence of detergents leads to improved performance. Biomacromolecules 7 (2006) 2610-2615
    • (2006) Biomacromolecules , vol.7 , pp. 2610-2615
    • Fernández-Lorente, G.1    Palomo, J.M.2    Mateo, C.3    Munilla, R.4    Ortiz, C.5    Cabrera, Z.6
  • 35
    • 0023030976 scopus 로고
    • Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effect of lauryl maltoside
    • Tandon S., and Horowitz P. Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effect of lauryl maltoside. J Biol Chem 261 (1986) 15615-15618
    • (1986) J Biol Chem , vol.261 , pp. 15615-15618
    • Tandon, S.1    Horowitz, P.2
  • 36
    • 0023255917 scopus 로고
    • Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effects of the concentration and type of detergent
    • Tandon S., and Horowitz P.M. Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effects of the concentration and type of detergent. J Biol Chem 262 (1987) 4486-4491
    • (1987) J Biol Chem , vol.262 , pp. 4486-4491
    • Tandon, S.1    Horowitz, P.M.2
  • 37
    • 44649119963 scopus 로고    scopus 로고
    • Lipase-catalyzed ethanolysis of soybean oil in a solvent-free system using central composite design and response surface methodology
    • Rodrigues R.C., Volpato G., Ayub M.A.Z., and Wada K. Lipase-catalyzed ethanolysis of soybean oil in a solvent-free system using central composite design and response surface methodology. J Chem Technol Biotechnol 83 (2008) 849-854
    • (2008) J Chem Technol Biotechnol , vol.83 , pp. 849-854
    • Rodrigues, R.C.1    Volpato, G.2    Ayub, M.A.Z.3    Wada, K.4
  • 38
    • 33747157176 scopus 로고    scopus 로고
    • Effects of reaction parameters on the incorporation of caprylic acid into soybean oil for production of structured lipids
    • Turan S., Karabulut I., and Vural H. Effects of reaction parameters on the incorporation of caprylic acid into soybean oil for production of structured lipids. J Food Lipids 13 (2006) 306-317
    • (2006) J Food Lipids , vol.13 , pp. 306-317
    • Turan, S.1    Karabulut, I.2    Vural, H.3
  • 39
    • 30344463784 scopus 로고    scopus 로고
    • Continuous production of structured phospholipids in a packed bed reactor with lipase from Thermomyces lanuginosa
    • Vikbjerg A.F., Peng L., Mu H., and Xu X. Continuous production of structured phospholipids in a packed bed reactor with lipase from Thermomyces lanuginosa. J Am Oil Chem Soc 82 (2005) 237-242
    • (2005) J Am Oil Chem Soc , vol.82 , pp. 237-242
    • Vikbjerg, A.F.1    Peng, L.2    Mu, H.3    Xu, X.4
  • 40
    • 2342489872 scopus 로고    scopus 로고
    • Enzyme-catalysed optical resolution of mandelic acid via RS(-/+)-methyl mandelate in non-aqueous media
    • Yadav G.D., and Sivakumar P. Enzyme-catalysed optical resolution of mandelic acid via RS(-/+)-methyl mandelate in non-aqueous media. Biochem Eng J 19 (2004) 101-107
    • (2004) Biochem Eng J , vol.19 , pp. 101-107
    • Yadav, G.D.1    Sivakumar, P.2
  • 41
    • 0028173902 scopus 로고
    • Current progress in crystallographic studies of new lipases from filamentous fungi
    • Derewenda U., Swenson L., Green R., Wei Y., Yamaguchi S., Joerger R., et al. Current progress in crystallographic studies of new lipases from filamentous fungi. Protein Eng 7 (1994) 551-557
    • (1994) Protein Eng , vol.7 , pp. 551-557
    • Derewenda, U.1    Swenson, L.2    Green, R.3    Wei, Y.4    Yamaguchi, S.5    Joerger, R.6
  • 43
    • 33847650952 scopus 로고    scopus 로고
    • Partial and enantioselective hydrolysis of diethyl phenylmalonate by immobilized preparations of lipase from Thermomyces lanuginose
    • Cabrera Z., Palomo J.M., Fernandez-Lorente G., Fernandez-Lafuente R., and Guisan J.M. Partial and enantioselective hydrolysis of diethyl phenylmalonate by immobilized preparations of lipase from Thermomyces lanuginose. Enzyme Microb Technol 40 (2007) 1280-1285
    • (2007) Enzyme Microb Technol , vol.40 , pp. 1280-1285
    • Cabrera, Z.1    Palomo, J.M.2    Fernandez-Lorente, G.3    Fernandez-Lafuente, R.4    Guisan, J.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.