메뉴 건너뛰기




Volumn 102, Issue 3, 2000, Pages 173-180

Rhizopus oryzae lipase-catalyzed stereospecific esterification of 2-monoradylglycerols - A comparison to corresponding triradylglycerol hydrolysis

Author keywords

Esterification; Hydrolysis; Molecular modeling; Rhizopus oryzae lipase; Water activity

Indexed keywords


EID: 0034340766     PISSN: 14387697     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1438-9312(200003)102:3<173::AID-EJLT173>3.0.CO;2-F     Document Type: Article
Times cited : (2)

References (27)
  • 1
    • 0000720480 scopus 로고
    • Selectivity is an important characteristic of lipases (acylglycerol hydrolases)
    • R. G. Jensen, D. R. Galluzzo, V. J. Bush: Selectivity is an important characteristic of lipases (acylglycerol hydrolases). Biocatalysis 3 (1990) 307-316.
    • (1990) Biocatalysis , vol.3 , pp. 307-316
    • Jensen, R.G.1    Galluzzo, D.R.2    Bush, V.J.3
  • 3
    • 51249166314 scopus 로고
    • Enzymatic esterification of glycerol. Lipase-catalyzed synthesis of regioisomerically pure 1, 3-sn-diacylglycerols
    • M. Berger, K. Laumen, M. P. Schneider: Enzymatic esterification of glycerol. Lipase-catalyzed synthesis of regioisomerically pure 1, 3-sn-diacylglycerols. J. Am. Oil Chem. Soc. 69 (1992) 955-960.
    • (1992) J. Am. Oil Chem. Soc. , vol.69 , pp. 955-960
    • Berger, M.1    Laumen, K.2    Schneider, M.P.3
  • 4
    • 0001218601 scopus 로고    scopus 로고
    • Lipases: Interfacial enzymes with attractive applications
    • R. D. Schmid, R. Verger: Lipases: interfacial enzymes with attractive applications. Angew. Chem. Int. Ed. 110 (1998) 1694-1720.
    • (1998) Angew. Chem. Int. Ed. , vol.110 , pp. 1694-1720
    • Schmid, R.D.1    Verger, R.2
  • 5
    • 0028889185 scopus 로고
    • Stereoselectivity of microbial lipases. The substitution at position sn-2 of triacylglycerol analogs influences the stereoselectivity of different microbial lipases
    • P. Stadler, A. Kovac, L. Haalck, F. Spener, F. Paltauf: Stereoselectivity of microbial lipases. The substitution at position sn-2 of triacylglycerol analogs influences the stereoselectivity of different microbial lipases. Eur. J. Biochem. 227 (1995) 335-343.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 335-343
    • Stadler, P.1    Kovac, A.2    Haalck, L.3    Spener, F.4    Paltauf, F.5
  • 6
    • 0342547002 scopus 로고    scopus 로고
    • Computer-aided modelling of stereoselective triglyceride hydrolysis catalyzed by Rhizopus oryzae lipase
    • H. C. Holzwarth, J. Pleiss, R. D. Schmid: Computer-aided modelling of stereoselective triglyceride hydrolysis catalyzed by Rhizopus oryzae lipase. J. Mol. Catal. 3 (1997) 73-82.
    • (1997) J. Mol. Catal. , vol.3 , pp. 73-82
    • Holzwarth, H.C.1    Pleiss, J.2    Schmid, R.D.3
  • 8
    • 0032957715 scopus 로고    scopus 로고
    • Stereoselectivity of Mucorales lipases toward triradylglycerols - A simple solution to a complex problem
    • H. Scheib, J. Pleiss, A. Kovac, F. Paltauf, R. D. Schmid: Stereoselectivity of Mucorales lipases toward triradylglycerols - A simple solution to a complex problem. Protein Sci. 8 (1999) 215-221.
    • (1999) Protein Sci. , vol.8 , pp. 215-221
    • Scheib, H.1    Pleiss, J.2    Kovac, A.3    Paltauf, F.4    Schmid, R.D.5
  • 9
    • 0030848588 scopus 로고    scopus 로고
    • Stereoselectivity of lipase from Rhizopus oryzae toward triacylglycerols and analogs: Computer-aided modeling and experimental validation
    • L. Haalck, F. Paltauf, J. Pleiss, R. D. Schmid, F. Spener, P. Stadler: Stereoselectivity of lipase from Rhizopus oryzae toward triacylglycerols and analogs: computer-aided modeling and experimental validation. Methods Enzymol. 284 (1997) 353-376.
    • (1997) Methods Enzymol. , vol.284 , pp. 353-376
    • Haalck, L.1    Paltauf, F.2    Pleiss, J.3    Schmid, R.D.4    Spener, F.5    Stadler, P.6
  • 12
    • 0001290876 scopus 로고
    • Synthesis of optically active polyunsaturated diacylglycerols
    • A. A. Duralski, P. J. R. Spooner, A. Watts: Synthesis of optically active polyunsaturated diacylglycerols. Tetrahedron Lett. 30 (1989) 3585-3588.
    • (1989) Tetrahedron Lett. , vol.30 , pp. 3585-3588
    • Duralski, A.A.1    Spooner, P.J.R.2    Watts, A.3
  • 13
    • 0028477764 scopus 로고
    • Carba analogues of triglycerides-isosteric mimics for natural lipids. Novel substrates for the determination of regio- and enantioselectivities displayed by lipases
    • M. Berger, B. Jakob, M. P. Schneider: Carba analogues of triglycerides-isosteric mimics for natural lipids. Novel substrates for the determination of regio- and enantioselectivities displayed by lipases. Bioorg. Med. Chem. 2/7 (1994) 573-588.
    • (1994) Bioorg. Med. Chem. , vol.2-7 , pp. 573-588
    • Berger, M.1    Jakob, B.2    Schneider, M.P.3
  • 14
    • 0029896744 scopus 로고    scopus 로고
    • Hydrolysis and esterification of acylglycerols and analogs in aqueous medium catalyzed by microbial lipases
    • A. Kovac, P. Stadler, L. Haalck, F. Spener, F. Paltauf: Hydrolysis and esterification of acylglycerols and analogs in aqueous medium catalyzed by microbial lipases. Biochim. Biophys. Acta 1301 (1996) 57-66.
    • (1996) Biochim. Biophys. Acta , vol.1301 , pp. 57-66
    • Kovac, A.1    Stadler, P.2    Haalck, L.3    Spener, F.4    Paltauf, F.5
  • 15
    • 0029744652 scopus 로고    scopus 로고
    • Analysis of the catalytic mechanism of a fungal lipase using computer-aided design and structural mutants
    • H. D. Beer, G. Wohlfahrt, J. E. G. McCarthy, D. Schomburg, R. D. Schmid: Analysis of the catalytic mechanism of a fungal lipase using computer-aided design and structural mutants. Protein Eng. 9 (1996) 507-517.
    • (1996) Protein Eng. , vol.9 , pp. 507-517
    • Beer, H.D.1    Wohlfahrt, G.2    McCarthy, J.E.G.3    Schomburg, D.4    Schmid, R.D.5
  • 16
    • 0026550733 scopus 로고
    • Catalysis at the interface: The anatomy of a conformational change in a triglyceride lipase
    • U. Derewenda, A. M. Brozowski, D. M. Lawson, Z. S. Derewenda: Catalysis at the interface: The anatomy of a conformational change in a triglyceride lipase. Biochemistry 31 (1992) 1532-1541.
    • (1992) Biochemistry , vol.31 , pp. 1532-1541
    • Derewenda, U.1    Brozowski, A.M.2    Lawson, D.M.3    Derewenda, Z.S.4
  • 17
    • 0343036190 scopus 로고    scopus 로고
    • Selection of salt hydrate pairs for use in water control in enzyme catalysis in organic solvents
    • E. Zacharis, I. C. Omar, J. Partridge, D. A. Robb, P. J. Halling: Selection of salt hydrate pairs for use in water control in enzyme catalysis in organic solvents. Biotechnol. Bioeng. 55 (1997) 367-374.
    • (1997) Biotechnol. Bioeng. , vol.55 , pp. 367-374
    • Zacharis, E.1    Omar, I.C.2    Partridge, J.3    Robb, D.A.4    Halling, P.J.5
  • 18
    • 0028302684 scopus 로고
    • The solvent dependence of enzyme specificity
    • C. R. Wescott, A. M. Klibanov: The solvent dependence of enzyme specificity. Biochim. Biophys. Acta 1206 (1994) 1-9.
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 1-9
    • Wescott, C.R.1    Klibanov, A.M.2
  • 20
    • 0011818012 scopus 로고
    • Effect of the solvent on enzyme enantioselectivity
    • Eds. Tramper, J., Vermue, M. H., Beeftink, H. H. von Stockar, U., Elsevier Sci. Publ., Amsterdam (The Netherlands)
    • L. Gubicza: Effect of the solvent on enzyme enantioselectivity. In: Biocatalysis in Non-Conventional Media. Eds. Tramper, J., Vermue, M. H., Beeftink, H. H. von Stockar, U., Elsevier Sci. Publ., Amsterdam (The Netherlands) 1992, pp. 497-503.
    • (1992) Biocatalysis in Non-Conventional Media , pp. 497-503
    • Gubicza, L.1
  • 21
    • 0032104493 scopus 로고    scopus 로고
    • The role of the reaction medium in lipase-catalyzed esterifications and transesterifications
    • E. Cernia, C. Palocci, S. Soro: The role of the reaction medium in lipase-catalyzed esterifications and transesterifications. Chem. Phys. Lipids 93 (1998) 157-168.
    • (1998) Chem. Phys. Lipids , vol.93 , pp. 157-168
    • Cernia, E.1    Palocci, C.2    Soro, S.3
  • 22
    • 0027527221 scopus 로고
    • Water activity influences enantioselectivity in a lipase-catalyzed resolution by esterification in an organic solvent
    • H. E. Högberg, H. Edlund, P. Berglund, E. Hedenström: Water activity influences enantioselectivity in a lipase-catalyzed resolution by esterification in an organic solvent. Tetrahedron Asymmetry 4 (1993) 2123-2126.
    • (1993) Tetrahedron Asymmetry , vol.4 , pp. 2123-2126
    • Högberg, H.E.1    Edlund, H.2    Berglund, P.3    Hedenström, E.4
  • 23
    • 0028396938 scopus 로고
    • Thermodynamic predictions for biocatalysis in nonconventional media: Theory, tests and recommendations for experimental design and analysis
    • P. J. Halling: Thermodynamic predictions for biocatalysis in nonconventional media: Theory, tests and recommendations for experimental design and analysis. Enzyme Microbiol. Technol. 16 (1994) 178-206.
    • (1994) Enzyme Microbiol. Technol. , vol.16 , pp. 178-206
    • Halling, P.J.1
  • 24
    • 0026592262 scopus 로고
    • Effects of medium and of reaction conditions on the enantioselectivity of lipases in organic solvents and possible rationales
    • F. Secundo, S. Riva, G. Carrea: Effects of medium and of reaction conditions on the enantioselectivity of lipases in organic solvents and possible rationales. Tetrahedron Asymmetry 3 (1992) 267-280.
    • (1992) Tetrahedron Asymmetry , vol.3 , pp. 267-280
    • Secundo, F.1    Riva, S.2    Carrea, G.3
  • 26
    • 0032968722 scopus 로고    scopus 로고
    • Crucial role of support and water activity on the lipase-catalyzed synthesis of structured triglycerides
    • M. M. Soumanou, U. T. Bornscheuer, U. Schmid, R. D. Schmid: Crucial role of support and water activity on the lipase-catalyzed synthesis of structured triglycerides. Biocatal. Biotransform. 16 (1999) 443-459.
    • (1999) Biocatal. Biotransform. , vol.16 , pp. 443-459
    • Soumanou, M.M.1    Bornscheuer, U.T.2    Schmid, U.3    Schmid, R.D.4
  • 27
    • 0024997533 scopus 로고
    • High affinity binding of water by proteins is similar in air and organic solvents
    • P. J. Halling: High affinity binding of water by proteins is similar in air and organic solvents. Biochim. Biophys. Acta 1040 (1990) 225-228.
    • (1990) Biochim. Biophys. Acta , vol.1040 , pp. 225-228
    • Halling, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.