메뉴 건너뛰기




Volumn 9, Issue 2, 2013, Pages 113-136

Synthesis of enantiopure drugs and drug intermediates by immobilized lipase-catalysis

Author keywords

Asymmetric transformation; Carbohydrates; Chemical modification; Immobilization; Kinetic resolution; Lipases; Pharmaceuticals

Indexed keywords

1,3 PROPANEDIAMINE; ANTINEOPLASTIC AGENT; ANTIOBESITY AGENT; ANTIOXIDANT; ASPARTIC ACID; BARIUM SULFATE; CANCER ANTIBODY; CEPHALOSPORIN DERIVATIVE; ESZOPICLONE; ETHYLENEDIAMINE; FLUOXETINE; FLURBIPROFEN; GLUTAMIC ACID; IBUPROFEN; INDOPROFEN; LOBELINE; MANDELIC ACID; MONASTROL; MUCIN 5AC; NAPROXEN; NEUROPROTECTIVE AGENT; NORSERTRALINE; NUCLEOPHILE; OSELTAMIVIR; PAROXETINE; PHENETHYL ALCOHOL; PYRAZINE DERIVATIVE; TRIACYLGLYCEROL LIPASE; VINYL ACETATE; ZOPICLONE;

EID: 84888126756     PISSN: 15734072     EISSN: 18756646     Source Type: Journal    
DOI: 10.2174/22115528112019990009     Document Type: Article
Times cited : (13)

References (172)
  • 1
    • 36148934066 scopus 로고    scopus 로고
    • Enantioselective synthesis of (R) and (S) curcumene and curcuphenol: An efficient chemoenzymatic route
    • Kamal, A.; Malik, M.S.; Shaik, A.A.; Azeeza, S. Enantioselective synthesis of (R) and (S) curcumene and curcuphenol: an efficient chemoenzymatic route. Tetrahedron Asymmetry, 2007, 18(21), 2547-2553.
    • (2007) Tetrahedron Asymmetry , vol.18 , Issue.21 , pp. 2547-2553
    • Kamal, A.1    Malik, M.S.2    Shaik, A.A.3    Azeeza, S.4
  • 2
    • 34547933047 scopus 로고    scopus 로고
    • A chemo-enzymatic process for sequential kinetic resolution of (R,S)-2-octanol under microwave irradiation
    • Yu, D.; Chen, P.; Wang, L.; Gu, Q.; Li, Y.; Wang, Z.; Cao, S. A chemo-enzymatic process for sequential kinetic resolution of (R,S)-2-octanol under microwave irradiation. Process Biochem., 2007, 42(9), 1312-1318.
    • (2007) Process Biochem , vol.42 , Issue.9 , pp. 1312-1318
    • Yu, D.1    Chen, P.2    Wang, L.3    Gu, Q.4    Li, Y.5    Wang, Z.6    Cao, S.7
  • 3
    • 34249287914 scopus 로고    scopus 로고
    • Enzymatic kinetic resolution of racemic 4-tetrahydropyranols by Candida rugosa lipase
    • Yadav, J.S.; Reddy, B.V.S.; Padmavani, B.; Venugopal, Ch.; Rao, A.B. Enzymatic kinetic resolution of racemic 4-tetrahydropyranols by Candida rugosa lipase. Tetrahedron Lett, 2007, 48(26), 4631-4633.
    • (2007) Tetrahedron Lett , vol.48 , Issue.26 , pp. 4631-4633
    • Yadav, J.S.1    Reddy, B.V.S.2    Padmavani, B.3    Venugopal, C.4    Rao, A.B.5
  • 4
    • 34547537549 scopus 로고    scopus 로고
    • Specificity enhancement towards hydrophobic substrates by immobilization of lipases by interfacial activation on hydrophobic supports
    • Fernández-Lorente, G.; Palomo, J.M.; Cabrera, Z.; Guisán, J.M.; Fernández-Lafuente, R. Specificity enhancement towards hydrophobic substrates by immobilization of lipases by interfacial activation on hydrophobic supports. Enzyme Microb. Technol., 2007, 41(5), 565-569.
    • (2007) Enzyme Microb. Technol , vol.41 , Issue.5 , pp. 565-569
    • Fernández-Lorente, G.1    Palomo, J.M.2    Cabrera, Z.3    Guisán, J.M.4    Fernández-Lafuente, R.5
  • 5
    • 36849022069 scopus 로고    scopus 로고
    • Combination of stereo-specific dihydroxylation and enzyme catalyzed enantioselective resolution for synthesis of enantiopure vicinal diols
    • Moen, A.R.; Ruud, K.; Anthonsen, T. Combination of stereo-specific dihydroxylation and enzyme catalyzed enantioselective resolution for synthesis of enantiopure vicinal diols. J. Mol. Catal. B: Enzym, 2008, 50(2-4), 74-79.
    • (2008) J. Mol. Catal. B: Enzym , vol.50 , Issue.2-4 , pp. 74-79
    • Moen, A.R.1    Ruud, K.2    Anthonsen, T.3
  • 6
    • 34547190795 scopus 로고    scopus 로고
    • Enzymatic preparation of novel aminoalkylpyridines using lipases in organic solvents
    • Torre, O.; Busto, E.; Gotor-Fernández, V.; Gotor, V. Enzymatic preparation of novel aminoalkylpyridines using lipases in organic solvents. Adv. Synth. Catal, 2007, 349(8-9), 1481-1488.
    • (2007) Adv. Synth. Catal , vol.349 , Issue.8-9 , pp. 1481-1488
    • Torre, O.1    Busto, E.2    Gotor-Fernández, V.3    Gotor, V.4
  • 8
    • 36049039802 scopus 로고    scopus 로고
    • One-Pot Enzymatic Resolution and Separation of sec-alcohols based on ionic acylating agents
    • Lourenco, N.M.T.; Afonso, C.A.M. One-Pot Enzymatic Resolution and Separation of sec-alcohols based on ionic acylating agents. Angew. Chem. Int. Ed, 2007, 465(43), 8178-8181.
    • (2007) Angew. Chem. Int. Ed , vol.465 , Issue.43 , pp. 8178-8181
    • Lourenco, N.M.T.1    Afonso, C.A.M.2
  • 9
    • 33846191192 scopus 로고    scopus 로고
    • Spontaneous enzymati-cally mediated dynamic kinetic resolution of 8-amino-5,6,7,8-tetrahydroquinoline
    • Crawford, J.B.; Skerlj, R.T.; Bridger, G.J. Spontaneous enzymati-cally mediated dynamic kinetic resolution of 8-amino-5,6,7,8-tetrahydroquinoline. J. Org. Chem., 2007, 72(2), 669-671.
    • (2007) J. Org. Chem , vol.72 , Issue.2 , pp. 669-671
    • Crawford, J.B.1    Skerlj, R.T.2    Bridger, G.J.3
  • 10
    • 33846216023 scopus 로고    scopus 로고
    • Dynamic kinetic resolution of secondary alcohols combining enzyme-catalyzed transesterification and zeolite-catalyzed racemization
    • Zhu, Y.; Fow, K.-L.; Chuah, G.-K.; Jaenicke, S. Dynamic kinetic resolution of secondary alcohols combining enzyme-catalyzed transesterification and zeolite-catalyzed racemization. Chem. Eur. J., 2007, 13(2), 541-547.
    • (2007) Chem. Eur. J , vol.13 , Issue.2 , pp. 541-547
    • Zhu, Y.1    Fow, K.-L.2    Chuah, G.-K.3    Jaenicke, S.4
  • 11
    • 33749817766 scopus 로고    scopus 로고
    • Li- pase/aluminum-catalyzed dynamic kinetic resolution of secondary alcohols
    • Berkessel, A.; Sebastian-Ibarz, M.L.; Muller, T.N. Li- pase/aluminum-catalyzed dynamic kinetic resolution of secondary alcohols. Angew. Chem. Int. Ed., 2006, 45(39), 6567-6570.
    • (2006) Angew. Chem. Int. Ed , vol.45 , Issue.39 , pp. 6567-6570
    • Berkessel, A.1    Sebastian-Ibarz, M.L.2    Muller, T.N.3
  • 12
    • 19044384195 scopus 로고    scopus 로고
    • Efficient lipase-catalyzed kinetic resolution and dynamic kinetic resolution of p-hydroxy nitriles. Correction of absolute configuration and transformation to chiral (3-hydroxy acids and y-amino alcohols
    • Pamies, O.; Backvall, J.-E. Efficient lipase-catalyzed kinetic resolution and dynamic kinetic resolution of p-hydroxy nitriles. Correction of absolute configuration and transformation to chiral (3-hydroxy acids and y-amino alcohols. Adv. Synth. Catal, 2002, 344 (9), 947-952.
    • (2002) Adv. Synth. Catal , vol.344 , Issue.9 , pp. 947-952
    • Pamies, O.1    Backvall, J.-E.2
  • 13
    • 33746284293 scopus 로고    scopus 로고
    • A dynamic kinetic resolution of allyl alcohols by the combined use of lipases and [VO(OSiPh3)3]
    • Akai, S.; Tanimoto, K.; Kanao, Y.; Egi, M.; Yamamoto, T.; Kita, Y. A dynamic kinetic resolution of allyl alcohols by the combined use of lipases and [VO(OSiPh3)3]. Angew. Chem. Int. Ed., 2006, 45(16), 2592-2595.
    • (2006) Angew. Chem. Int. Ed , vol.45 , Issue.16 , pp. 2592-2595
    • Akai, S.1    Tanimoto, K.2    Kanao, Y.3    Egi, M.4    Yamamoto, T.5    Kita, Y.6
  • 14
    • 33947146141 scopus 로고    scopus 로고
    • Conjugate addition of 2- and 4-pyridylcuprates: An expeditious asymmetric synthesis of natural (-)-evoninic acid
    • Spivey, A.C.; Shukla, L.; Hayler, J.F. Conjugate addition of 2- and 4-pyridylcuprates: an expeditious asymmetric synthesis of natural (-)-evoninic acid. Org. Lett, 2007, 9(5), 891-894.
    • (2007) Org. Lett , vol.9 , Issue.5 , pp. 891-894
    • Spivey, A.C.1    Shukla, L.2    Hayler, J.F.3
  • 15
    • 32844456411 scopus 로고    scopus 로고
    • Enantio-complementary deracemization of (±)-2-hydroxy-4-phenylbutanoic acid and (±)-3-phenyllactic acid using lipase-catalyzed kinetic resolution combined with biocatalytic racemization
    • Larissegger-Schnell, B.; Glueck, S. M.; Kroutil, W.; Faber, K. Enantio-complementary deracemization of (±)-2-hydroxy-4-phenylbutanoic acid and (±)-3-phenyllactic acid using lipase-catalyzed kinetic resolution combined with biocatalytic racemization. Tetrahedron, 2006, 62(12), 2912-2916.
    • (2006) Tetrahedron , vol.62 , Issue.12 , pp. 2912-2916
    • Larissegger-Schnell, B.1    Glueck, S.M.2    Kroutil, W.3    Faber, K.4
  • 16
    • 82755197953 scopus 로고    scopus 로고
    • New opportunities for biocatalysis: Driving the synthesis of chiral chemicals
    • Zheng, G.-W.; Xu, J.-H. New opportunities for biocatalysis: driving the synthesis of chiral chemicals. Curr. Opin. Biotech., 2011, 22(6), 784-792.
    • (2011) Curr. Opin. Biotech , vol.22 , Issue.6 , pp. 784-792
    • Zheng, G.-W.1    Xu, J.-H.2
  • 17
    • 77954633208 scopus 로고    scopus 로고
    • Optimization of immobilization conditions of Candida antarctica lipase based on response surface methodology
    • Liu, J.H.; Zhang, Y.Y.; Xia, Y.M.; Su, F. Optimization of immobilization conditions of Candida antarctica lipase based on response surface methodology. Chem. Biochem. Eng. Q., 2010, 24(2) 203-209.
    • (2010) Chem. Biochem. Eng. Q , vol.24 , Issue.2 , pp. 203-209
    • Liu, J.H.1    Zhang, Y.Y.2    Xia, Y.M.3    Su, F.4
  • 18
    • 40849142018 scopus 로고    scopus 로고
    • Lipase enzyme immobilization on synthetic beaded macroporous copolymers for kinetic resolution of chiral drugs intermediates
    • Bhushan, I.; Parshad, R.; Qazi, G. N.; Ingavle, G.; Rajan, C.R.; Ponrathnam, S.; Gupta, V. K. Lipase enzyme immobilization on synthetic beaded macroporous copolymers for kinetic resolution of chiral drugs intermediates. Process Biochem., 2008, 43(4), 321-330.
    • (2008) Process Biochem , vol.43 , Issue.4 , pp. 321-330
    • Bhushan, I.1    Parshad, R.2    Qazi, G.N.3    Ingavle, G.4    Rajan, C.R.5    Ponrathnam, S.6    Gupta, V.K.7
  • 21
    • 0026786234 scopus 로고
    • The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 Å resolution
    • Derewenda, Z.S.; Derewenda, U.; Dodson, G.G. The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 Å resolution. J. Mol. Biol, 1992, 227(3), 818-839.
    • (1992) J. Mol. Biol , vol.227 , Issue.3 , pp. 818-839
    • Derewenda, Z.S.1    Derewenda, U.2    Dodson, G.G.3
  • 22
    • 0028773288 scopus 로고
    • The sequence, crystal structure determination and refinement of two crystal forms of lipase B from
    • Uppenberg, J.; Hansen, M. T.; Patkar, S.; Jones, T. A. The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Structure, 1994, 2(4), 293-308.
    • (1994) Candida Antarctica. Structure , vol.2 , Issue.4 , pp. 293-308
    • Uppenberg, J.1    Hansen, M.T.2    Patkar, S.3    Jones, T.A.4
  • 24
    • 0026550733 scopus 로고
    • Catalysis at the interface: The anatomy of a conformational change in a triglyceride lipase
    • Derewenda, U.; Brzozowski, A.M.; Lawson, D. M.; Derewenda, Z.S. Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase. Biochemistry, 1992, 31(5), 1532-1541.
    • (1992) Biochemistry , vol.31 , Issue.5 , pp. 1532-1541
    • Derewenda, U.1    Brzozowski, A.M.2    Lawson, D.M.3    Derewenda, Z.S.4
  • 25
    • 0001406913 scopus 로고
    • Actions of pancreatic lipase on esters in emulsions
    • Sarda, L.; Desnuelle, P. Actions of pancreatic lipase on esters in emulsions. Biochim. Biophys. Acta, 1958, 30(3), 513-521.
    • (1958) Biochim. Biophys. Acta , vol.30 , Issue.3 , pp. 513-521
    • Sarda, L.1    Desnuelle, P.2
  • 26
    • 0030928763 scopus 로고    scopus 로고
    • A critical reevaluation of the phenomenon of interfacial activation
    • Ferrato, F.; F. Carriere, R. Verger. A critical reevaluation of the phenomenon of interfacial activation. Methods Enzymol, 1997, 286, 327-347
    • (1997) Methods Enzymol , vol.286 , pp. 327-347
    • Ferrato, F.1    Carriere, F.2    Verger, R.3
  • 27
    • 0028939393 scopus 로고
    • Interfacial activation-based molecular bioimprinting of lipolytic enzymes
    • Mingarro, Y.; Abad, C; Braco, L. Interfacial activation-based molecular bioimprinting of lipolytic enzymes. Proc. Nat. Acad. Sci. U.S.A., 1995, 92(8), 3308-3312.
    • (1995) Proc. Nat. Acad. Sci. U.S.A , vol.92 , Issue.8 , pp. 3308-3312
    • Mingarro, Y.1    Abad, C.2    Braco, L.3
  • 30
    • 0037457503 scopus 로고    scopus 로고
    • Self-assembly of Pseudomonas fluorescens lipase into bimolecular aggregates dramatically affects functional properties
    • Fernández-Lorente, G.; Palomo, J.M.; Fuentes, M.; Mateo, C; Guisán, J.M, Fernández-Lafuente, R. Self-assembly of Pseudomonas fluorescens lipase into bimolecular aggregates dramatically affects functional properties. Biotechnol. Bioeng., 2003, 82(2), 232-237.
    • (2003) Biotechnol. Bioeng , vol.82 , Issue.2 , pp. 232-237
    • Fernández-Lorente, G.1    Palomo, J.M.2    Fuentes, M.3    Mateo, C.4    Guisán, J.M.5    Fernández-Lafuente, R.6
  • 31
    • 0037010728 scopus 로고    scopus 로고
    • Interfacial adsorption of lipases on very hydrophobic support (Octadecyl-Sepabeads): Immobilization, hyperactivation and stabilization of the open form of lipases
    • Palomo, J.M.; Muñoz, G.; Fernández-Lorente, G.; Mateo, C; Fernández-Lafuente, R.; Guisán, J.M. Interfacial adsorption of lipases on very hydrophobic support (Octadecyl-Sepabeads): Immobilization, hyperactivation and stabilization of the open form of lipases. J. Mol. Catal. B Enzym., 2002, 19-20, 279-286.
    • (2002) J. Mol. Catal. B Enzym , vol.19-20 , pp. 279-286
    • Palomo, J.M.1    Muñoz, G.2    Fernández-Lorente, G.3    Mateo, C.4    Fernández-Lafuente, R.5    Guisán, J.M.6
  • 32
    • 33846665869 scopus 로고    scopus 로고
    • Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface
    • Foresti, M.L.; Ferreira, M.L. Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface. Colloid Surf. A, 2007, 294(1-3), 147-155.
    • (2007) Colloid Surf. A , vol.294 , Issue.1-3 , pp. 147-155
    • Foresti, M.L.1    Ferreira, M.L.2
  • 33
    • 33745220781 scopus 로고    scopus 로고
    • Immobilization of lipase and penicillin acylase on hydrophobic acrylic carriers. Enzyme Microb
    • Bryjak, J.; Trochimczuk, A.W. Immobilization of lipase and penicillin acylase on hydrophobic acrylic carriers. Enzyme Microb. Technol, 2006, 39(4), 573-578.
    • (2006) Technol , vol.39 , Issue.4 , pp. 573-578
    • Bryjak, J.1    Trochimczuk, A.W.2
  • 35
    • 0037025268 scopus 로고    scopus 로고
    • Modulation of the enantiose-lectivity of Candida antarctica B lipase via conformational engineering: Kinetic resolution of (±)-a-hydroxyphenylacetic acid derivatives
    • Palomo, J.M.; Fernández-Lorente, G.; Mateo, C; Fuentes, M.; Fernández-Lafuente, R.; Guisán, J.M. Modulation of the enantiose-lectivity of Candida antarctica B lipase via conformational engineering: Kinetic resolution of (±)-a-hydroxyphenylacetic acid derivatives. Tetrahedron:Asymmetry, 2002, 13(12), 1337-1345.
    • (2002) Tetrahedron:Asymmetry , vol.13 , Issue.12 , pp. 1337-1345
    • Palomo, J.M.1    Fernández-Lorente, G.2    Mateo, C.3    Fuentes, M.4    Fernández-Lafuente, R.5    Guisán, J.M.6
  • 36
    • 0036843441 scopus 로고    scopus 로고
    • Modulation of the enantiose-lectivity of lipases via controlled immobilization and medium engineering: Hydrolytic resolution of mandelic acid esters
    • Palomo, J.M.; Fernández-Lorente, G.; Mateo, C; Ortiz, C; Fernández-Lafuente, R.; Guisan, J.M. Modulation of the enantiose-lectivity of lipases via controlled immobilization and medium engineering: Hydrolytic resolution of mandelic acid esters. Enzyme Microb. Technol., 2002, 31(6), 775-783.
    • (2002) Enzyme Microb. Technol , vol.31 , Issue.6 , pp. 775-783
    • Palomo, J.M.1    Fernández-Lorente, G.2    Mateo, C.3    Ortiz, C.4    Fernández-Lafuente, R.5    Guisan, J.M.6
  • 37
    • 33747799719 scopus 로고    scopus 로고
    • Enan-tioselectivity modulation through immobilization of Arthrobacter sp. lipase: Kinetic resolution of fluoxetine intermediate
    • Chaubey, A.; Parshad, R.; Koul, S.; Taneja, S.C.; Qazi, G.N. Enan-tioselectivity modulation through immobilization of Arthrobacter sp. lipase: Kinetic resolution of fluoxetine intermediate. J. Mol. Catal. B Enzym., 2006, 42(1-2), 39-44.
    • (2006) J. Mol. Catal. B Enzym , vol.42 , Issue.1-2 , pp. 39-44
    • Chaubey, A.1    Parshad, R.2    Koul, S.3    Taneja, S.C.4    Qazi, G.N.5
  • 40
    • 1842474522 scopus 로고    scopus 로고
    • Enzymatic resolution of (±)- glycidyl butyrate in aqueous media. Strong modulation of the properties of the lipase from Rhizopus oryzae via immobilization techniques
    • Palomo, J.M.; Segura, R.L.; Fernández-Lorente, G.; Guisán, Jose M.; Fernández-Lafuente, R. Enzymatic resolution of (±)- glycidyl butyrate in aqueous media. Strong modulation of the properties of the lipase from Rhizopus oryzae via immobilization techniques. Tetrahedron:Asymmetry, 2004, 15(7), 1157-1161.
    • (2004) Tetrahedron:Asymmetry , vol.15 , Issue.7 , pp. 1157-1161
    • Palomo, J.M.1    Segura, R.L.2    Fernández-Lorente, G.3    Guisán, J.M.4    Fernández-Lafuente, R.5
  • 41
    • 0037450167 scopus 로고    scopus 로고
    • Modulation of Mucor miehei lipase properties via directed immobilization on different hetero-functional epoxy resins: Hydrolytic resolution of (R,S)-2-butyroyl-2-phenylacetic acid
    • Palomo, J.M.; Muñoz, G.; Fernández-Lorente, G.; Mateo, C; Fuentes, M.; Guisán J.M.; Fernández-Lafuente, R. Modulation of Mucor miehei lipase properties via directed immobilization on different hetero-functional epoxy resins: Hydrolytic resolution of (R,S)-2-butyroyl-2-phenylacetic acid. J. Mol. Catal. B Enzym., 2003, 21(4), 201-210.
    • (2003) J. Mol. Catal. B Enzym , vol.21 , Issue.4 , pp. 201-210
    • Palomo, J.M.1    Muñoz, G.2    Fernández-Lorente, G.3    Mateo, C.4    Fuentes, M.5    Guisán, J.M.6    Fernández-Lafuente, R.7
  • 42
    • 33947301782 scopus 로고    scopus 로고
    • Immobilization of lipase with a special microstructure in composite hydrophilic CA/hydrophobic PTFE membrane for the chiral separation of ra-cemic ibuprofen
    • Wang, Y.; Hu, Y.; Xu, J.; Luo, G.; Dai, Y. Immobilization of lipase with a special microstructure in composite hydrophilic CA/hydrophobic PTFE membrane for the chiral separation of ra-cemic ibuprofen. J. Membr. Sci., 2007, 293(1-2), 133-141.
    • (2007) J. Membr. Sci , vol.293 , Issue.1-2 , pp. 133-141
    • Wang, Y.1    Hu, Y.2    Xu, J.3    Luo, G.4    Dai, Y.5
  • 44
    • 34249341153 scopus 로고    scopus 로고
    • The study on efficient hydrolases immobilization for the kinetic resolution of the a-acetoxyamides
    • Koszelewski, D.; Redzej, A.; Ostaszewski, R. The study on efficient hydrolases immobilization for the kinetic resolution of the a-acetoxyamides. J. Mol. Catal. B Enzym., 2007, 47(1-2), 51-57.
    • (2007) J. Mol. Catal. B Enzym , vol.47 , Issue.1-2 , pp. 51-57
    • Koszelewski, D.1    Redzej, A.2    Ostaszewski, R.3
  • 45
    • 0037206820 scopus 로고    scopus 로고
    • Enzymatic resolution of (±)-trans-4-(4́-fluorophenyl)-6-oxopiperidin-3-ethyl carboxilate, intermediate in synthesis of (-)-Paroxetine
    • Palomo, J.M.; Fernández-Lorente, G.; Mateo, C; Fernández-Lafuente, R.; Guisán, J.M. Enzymatic resolution of (±)-trans-4-(4́-fluorophenyl)-6-oxopiperidin-3-ethyl carboxilate, intermediate in synthesis of (-)-Paroxetine. Tetrahedron: Asymmetry, 2002, 13(21), 2375-2381.
    • (2002) Tetrahedron: Asymmetry , vol.13 , Issue.21 , pp. 2375-2381
    • Palomo, J.M.1    Fernández-Lorente, G.2    Mateo, C.3    Fernández-Lafuente, R.4    Guisán, J.M.5
  • 46
    • 0037049410 scopus 로고    scopus 로고
    • Enzymatic production of (3S,4R)-4-(4́-fluorophenyl)-6-oxo-piperidin-3- carboxylic acid using a commercial preparation of lipase A from Candida antarctica: The role of a contaminant esterase
    • Palomo, J.M.; Fernández-Lorente, G.; Mateo, C; Fuentes, M.; Guisán, J.M.; Fernández-Lafuente, R. Enzymatic production of (3S,4R)-4-(4́-fluorophenyl)-6-oxo-piperidin-3- carboxylic acid using a commercial preparation of lipase A from Candida antarctica: the role of a contaminant esterase. Tetrahedron: Asymmetry, 2002, 13(24), 2653-2659.
    • (2002) Tetrahedron: Asymmetry , vol.13 , Issue.24 , pp. 2653-2659
    • Palomo, J.M.1    Fernández-Lorente, G.2    Mateo, C.3    Fuentes, M.4    Guisán, J.M.5    Fernández-Lafuente, R.6
  • 47
    • 0442307779 scopus 로고    scopus 로고
    • Resolution of paroxetine precursor using different lipases. Influence of the reaction conditions on the enanti-oselectivity of lipases
    • Fernández-Lorente, G.; Palomo, J.M.; Mateo, C; Guisán, J.M.; Fernández-Lafuente, R. Resolution of paroxetine precursor using different lipases. Influence of the reaction conditions on the enanti-oselectivity of lipases. Enzyme Microb. Technol, 2004, 34(3), 264-269.
    • (2004) Enzyme Microb. Technol , vol.34 , Issue.3 , pp. 264-269
    • Fernández-Lorente, G.1    Palomo, J.M.2    Mateo, C.3    Guisán, J.M.4    Fernández-Lafuente, R.5
  • 48
    • 0037025268 scopus 로고    scopus 로고
    • Guisán, Modulation of the enantioselectiv-ity of Candida antarctica B lipase via conformational engineering: Kinetic resolution of (±)-alfa-hydroxy-phenylacetic acid derivatives
    • Palomo, J.M.; Fernández-Lorente, G.; Mateo, C; Fuentes, M.; Fernández-Lafuente, R.; Guisán, Modulation of the enantioselectiv-ity of Candida antarctica B lipase via conformational engineering: kinetic resolution of (±)-alfa-hydroxy-phenylacetic acid derivatives. Tetrahedron: Asymmetry., 2002, 13(12), 1337-1345.
    • (2002) Tetrahedron: Asymmetry , vol.13 , Issue.12 , pp. 1337-1345
    • Palomo, J.M.1    Fernández-Lorente, G.2    Mateo, C.3    Fuentes, M.4    Fernández-Lafuente, R.5
  • 49
    • 1842763651 scopus 로고    scopus 로고
    • Purification, immobilization and stabilization of a lipase from Bacillus thermocatenulatus by interfacial adsorption on hydrophobic supports
    • Palomo, J.M.; Segura, R. L.; Fernández-Lorente, G.; Pernas, M.; Rua, M.L.; Guisán, J.M.; Fernández-Lafuente, R. Purification, immobilization and stabilization of a lipase from Bacillus thermocatenulatus by interfacial adsorption on hydrophobic supports. Biotechnol. Prog., 2004, 20(2), 630-635.
    • (2004) Biotechnol. Prog , vol.20 , Issue.2 , pp. 630-635
    • Palomo, J.M.1    Segura, R.L.2    Fernández-Lorente, G.3    Pernas, M.4    Rua, M.L.5    Guisán, J.M.6    Fernández-Lafuente, R.7
  • 50
    • 28844483422 scopus 로고    scopus 로고
    • Purification of different lipases from Aspergillus niger using a highly selective adsorption on hydrophobic supports
    • Fernández-Lorente, G.; Ortiz, C; Segura, R.L.; Fernández-Lafuente, R.; Guisán, J.M.; Palomo, J.M. Purification of different lipases from Aspergillus niger using a highly selective adsorption on hydrophobic supports. Biotechnol. Bioeng., 2005, 92(6), 773-779.
    • (2005) Biotechnol. Bioeng , vol.92 , Issue.6 , pp. 773-779
    • Fernández-Lorente, G.1    Ortiz, C.2    Segura, R.L.3    Fernández-Lafuente, R.4    Guisán, J.M.5    Palomo, J.M.6
  • 51
    • 11144277399 scopus 로고    scopus 로고
    • Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis
    • Foresti, M.L.; Alimenti, G.A.; Ferreira, M.L. Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis. Enzyme Microb. Technol, 2005, 36(2-3), 338-349.
    • (2005) Enzyme Microb. Technol , vol.36 , Issue.2-3 , pp. 338-349
    • Foresti, M.L.1    Alimenti, G.A.2    Ferreira, M.L.3
  • 52
    • 33645222148 scopus 로고    scopus 로고
    • Improvement of functional properties of a thermostable lipase from Alcaligenes sp. via strong adsorption on hydrophobic supports
    • Wilson, L.; Palomo, J.M.; Fernández-Lorente, G.; Illanes, A.; Guisán, J.M.; Fernández-Lafuente, R. Improvement of functional properties of a thermostable lipase from Alcaligenes sp. via strong adsorption on hydrophobic supports. Enzyme Microb. Technol, 2006, 38(7), 975-980.
    • (2006) Enzyme Microb. Technol , vol.38 , Issue.7 , pp. 975-980
    • Wilson, L.1    Palomo, J.M.2    Fernández-Lorente, G.3    Illanes, A.4    Guisán, J.M.5    Fernández-Lafuente, R.6
  • 55
    • 8644245911 scopus 로고    scopus 로고
    • Polyethylenimine coated agarose supports, for the reversible immobilisation of (3-galactosidase from Aspergillus oryzae
    • Gonzalez, P.; Batista-Viera, F.; Brena, B.M. Polyethylenimine coated agarose supports, for the reversible immobilisation of (3-galactosidase from Aspergillus oryzae. Int. J. Biotechnol, 2004, 6(4), 338-345.
    • (2004) Int. J. Biotechnol , vol.6 , Issue.4 , pp. 338-345
    • Gonzalez, P.1    Batista-Viera, F.2    Brena, B.M.3
  • 56
    • 33847711403 scopus 로고    scopus 로고
    • Stem bromelain: An enzyme that naturally facilitates oriented immobilization
    • Khatoon, H.; Younus, H.; Saleemuddin, M. Stem bromelain: An enzyme that naturally facilitates oriented immobilization. Prot. Pep. Lett., 2007, 14(3), 233-236.
    • (2007) Prot. Pep. Lett , vol.14 , Issue.3 , pp. 233-236
    • Khatoon, H.1    Younus, H.2    Saleemuddin, M.3
  • 57
    • 37349035008 scopus 로고    scopus 로고
    • Immobilization of lipase enzyme in polyvinyl alcohol (PVA) nanofibrous membranes
    • Wang, Y.; Hsieh, Y.-L. Immobilization of lipase enzyme in polyvinyl alcohol (PVA) nanofibrous membranes. J. Membr. Sci., 2008, 309(1-2), 73-81.
    • (2008) J. Membr. Sci , vol.309 , Issue.1-2 , pp. 73-81
    • Wang, Y.1    Hsieh, Y.-L.2
  • 58
    • 33747453910 scopus 로고    scopus 로고
    • Characterization of Thermoanaerobacter cyclomaltodextrin glucanotransferase immobilized on glyoxyl-agarose
    • Tardioli, P.W.; Zanin, G.M.; de Moraes, F.F. Characterization of Thermoanaerobacter cyclomaltodextrin glucanotransferase immobilized on glyoxyl-agarose. Enzyme Microb. Technol, 2006, 39(6), 1270-1278.
    • (2006) Enzyme Microb. Technol , vol.39 , Issue.6 , pp. 1270-1278
    • Tardioli, P.W.1    Zanin, G.M.2    de Moraes, F.F.3
  • 59
    • 33746002604 scopus 로고    scopus 로고
    • Improvement of the stability of alcohol dehydrogenase by covalent immobilization on glyoxyl-agarose
    • Bolivar, J.M.; Wilson, L.; Ferrarotti, S.A.; Guisán, J.M.; Fernández-Lafuente, R.; Mateo, C. Improvement of the stability of alcohol dehydrogenase by covalent immobilization on glyoxyl-agarose. J. Biotechnol., 2006, 125(1), 85-94.
    • (2006) J. Biotechnol , vol.125 , Issue.1 , pp. 85-94
    • Bolivar, J.M.1    Wilson, L.2    Ferrarotti, S.A.3    Guisán, J.M.4    Fernández-Lafuente, R.5    Mateo, C.6
  • 63
    • 0034099693 scopus 로고    scopus 로고
    • Entrapment of lipases in hydrophobic sol-gel-materials: Efficient heterogeneous biocatalysts in aqueous medium
    • Reetz, M.T.; Wenkel, R.; Avnir, D. Entrapment of lipases in hydrophobic sol-gel-materials: Efficient heterogeneous biocatalysts in aqueous medium. Synthesis, 2000, 6(1-3), 781-783.
    • (2000) Synthesis , vol.6 , Issue.1-3 , pp. 781-783
    • Reetz, M.T.1    Wenkel, R.2    Avnir, D.3
  • 64
    • 0029134278 scopus 로고
    • Efficient heterogeneous biocatalysts by entrapment of lipases in hydrophobic Sol-Gel materials
    • Reetz, M.T.; Zonta, A.; Simpelkamp, J. Efficient heterogeneous biocatalysts by entrapment of lipases in hydrophobic Sol-Gel materials. Angew. Chem. Int. Ed, 1995, 34(3), 301-303.
    • (1995) Angew. Chem. Int. Ed , vol.34 , Issue.3 , pp. 301-303
    • Reetz, M.T.1    Zonta, A.2    Simpelkamp, J.3
  • 65
    • 0037025268 scopus 로고    scopus 로고
    • Modulation of the enantiose-lectivity of Candida antarctica B lipase via conformational engineering: Kinetic resolution of (±)-alfa-hydroxy-phenylacetic acid derivatives
    • Palomo, J.M.; Fernández-Lorente, G.; Mateo, C; Fuentes, M.; Fernández-Lafuente, R.; Guisán, J.M. Modulation of the enantiose-lectivity of Candida antarctica B lipase via conformational engineering: kinetic resolution of (±)-alfa-hydroxy-phenylacetic acid derivatives. Tetrahedron: Asymmetry, 2002, 13(12), 1337-1345.
    • (2002) Tetrahedron: Asymmetry , vol.13 , Issue.12 , pp. 1337-1345
    • Palomo, J.M.1    Fernández-Lorente, G.2    Mateo, C.3    Fuentes, M.4    Fernández-Lafuente, R.5    Guisán, J.M.6
  • 68
    • 83755195520 scopus 로고    scopus 로고
    • Enzyme surface glycosylation on the solid phase: Improve activity and selectivity of Candida antarctica lipase B
    • Gutarra, M.L, Romero, O.; Abian, O.; Torres, F.A.G.; Freire, D.M.G.; Castro, A.M.; Guisan, J.M.; Palomo, J.M. Enzyme surface glycosylation on the solid phase: improve activity and selectivity of Candida antarctica lipase B. ChemCatChem, 2011, 3(12), 1902-1910.
    • (2011) ChemCatChem , vol.3 , Issue.12 , pp. 1902-1910
    • Gutarra, M.L.1    Romero, O.2    Abian, O.3    Torres, F.A.G.4    Freire, D.M.G.5    Castro, A.M.6    Guisan, J.M.7    Palomo, J.M.8
  • 69
    • 79960342892 scopus 로고    scopus 로고
    • Trans,trans-2,4-Hexadiene incorporation on enzymes for site-specific immobilization and fluorescent labeling
    • Filice, M, Romero, O.; Guisan, J.M.; Palomo, J.M. Trans,trans-2,4-Hexadiene incorporation on enzymes for site-specific immobilization and fluorescent labeling. Org. Biomol. Chem., 2011, 9, 5535-5540
    • (2011) Org. Biomol. Chem , vol.9 , pp. 5535-5540
    • Filice, M.1    Romero, O.2    Guisan, J.M.3    Palomo, J.M.4
  • 70
    • 78649297620 scopus 로고    scopus 로고
    • Diels-alder cycloaddition in protein chemistry
    • Palomo, J.M. Diels-alder cycloaddition in protein chemistry. Eur. J. Org. Chem. 2010, 33, 6303-6314.
    • (2010) Eur. J. Org. Chem , vol.33 , pp. 6303-6314
    • Palomo, J.M.1
  • 71
    • 77649183732 scopus 로고    scopus 로고
    • Enhanced activity of an immobilized lipase promoted by site-directed chemical modification with polymers
    • Godoy, C. A.; Rivas, B.; Filice, M.; Fernández-Lorente, G.; Guisan J. M.; Palomo, J. M. Enhanced activity of an immobilized lipase promoted by site-directed chemical modification with polymers. Process Biochem., 2010, 45(4), 534-541.
    • (2010) Process Biochem , vol.45 , Issue.4 , pp. 534-541
    • Godoy, C.A.1    Rivas, B.2    Filice, M.3    Fernández-Lorente, G.4    Guisan, J.M.5    Palomo, J.M.6
  • 73
    • 54749090797 scopus 로고    scopus 로고
    • Lipases Enantioselectivity Alteration by Immobilization Techniques
    • Palomo, J.M. Lipases Enantioselectivity Alteration by Immobilization Techniques. Curr.Bio. Comp., 2008, 4, 126-138.
    • (2008) Curr.Bio. Comp , vol.4 , pp. 126-138
    • Palomo, J.M.1
  • 75
    • 0030575795 scopus 로고    scopus 로고
    • Easy access to an enantio-pure precursor of (+)-goniodiol
    • Surivet, J.P.; Volle, J.N.; Vatele, J.M. Easy access to an enantio-pure precursor of (+)-goniodiol. Tetrahedron:Asymmetry, 1996, 7(11), 3305-3308.
    • (1996) Tetrahedron:Asymmetry , vol.7 , Issue.11 , pp. 3305-3308
    • Surivet, J.P.1    Volle, J.N.2    Vatele, J.M.3
  • 76
    • 0034685738 scopus 로고    scopus 로고
    • Synthesis of 1-aza-cryptophycin 1, an unstable cryptophycin. An unusual skeletal rearrangement
    • Barrow, R.A.; Moore, R.E.; Li, L.H.; Tius, M.A. Synthesis of 1-aza-cryptophycin 1, an unstable cryptophycin. An unusual skeletal rearrangement. Tetrahedron, 2000, 56(21), 3339-3351.
    • (2000) Tetrahedron , vol.56 , Issue.21 , pp. 3339-3351
    • Barrow, R.A.1    Moore, R.E.2    Li, L.H.3    Tius, M.A.4
  • 77
    • 2342489872 scopus 로고    scopus 로고
    • Enzyme-catalysed optical resolution of mandelic acid via (RS)-(±)-methyl mandelate in non-aqueous media
    • Yadav, G.D.; Sivakumar, P. Enzyme-catalysed optical resolution of mandelic acid via (RS)-(±)-methyl mandelate in non-aqueous media. Biochem. Eng. J., 2004, 19(2), 101-107.
    • (2004) Biochem. Eng. J , vol.19 , Issue.2 , pp. 101-107
    • Yadav, G.D.1    Sivakumar, P.2
  • 78
    • 77954214536 scopus 로고    scopus 로고
    • Highly enan-tioselective biocatalysts by coating immobilized lipases with poly-ethyleneimine
    • Cabrera, Z.; Gutarra M.L, Guisan, J.M.; Palomo, J.M. Highly enan-tioselective biocatalysts by coating immobilized lipases with poly-ethyleneimine. Catal Commun., 2010, 11, 964-967.
    • (2010) Catal Commun , vol.11 , pp. 964-967
    • Cabrera, Z.1    Gutarra, M.L.2    Guisan, J.M.3    Palomo, J.M.4
  • 80
    • 74049101638 scopus 로고    scopus 로고
    • Lipase-mediated enantioselective kinetic resolution of racemic acidic drugs in non-standard organic solvents: Direct chiral liquid chromatography monitoring and accurate determination of the enantiomeric excesses
    • Ghanem, A.; Aboul-Enein, M. N.; El-Azzouny, A.; El-Behairy M. F. Lipase-mediated enantioselective kinetic resolution of racemic acidic drugs in non-standard organic solvents: Direct chiral liquid chromatography monitoring and accurate determination of the enantiomeric excesses. J. Chromatogr. A, 2010, 1217(7), 1063-1074.
    • (2010) J. Chromatogr. A , vol.1217 , Issue.7 , pp. 1063-1074
    • Ghanem, A.1    Aboul-Enein, M.N.2    El-Azzouny, A.3    El-Behairy, M.F.4
  • 81
    • 0036898158 scopus 로고    scopus 로고
    • Dynamic kinetic resolutions and asymmetric transformations by enzymes coupled with metal catalysis
    • Kim, M.J.; Ahn, Y.S.; Park, J.W. Dynamic kinetic resolutions and asymmetric transformations by enzymes coupled with metal catalysis. Curr. Opin. Biotechnol, 2002, 13(6), 578-587.
    • (2002) Curr. Opin. Biotechnol , vol.13 , Issue.6 , pp. 578-587
    • Kim, M.J.1    Ahn, Y.S.2    Park, J.W.3
  • 82
    • 0037458533 scopus 로고    scopus 로고
    • Chiral Resolution of (±)-5-substituted-6-(5-chloropyridin-2-yl)-7-oxo-5,6-dihydropyrrolo[3,4b]pyrazine derivatives-precursors of (S)-(+)-Zopiclone, catalyzed by immobilized Candida antarctica B lipase in aqueous media
    • Palomo, J.M.; Mateo, C; Fernández-Lorente, G.; Solares, L.F.; Diaz, M.; Sánchez, V.M.; Bayod, M.; Gotor, V.; Fernández-Lafuente, R.; Guisán, J.M. Chiral Resolution of (±)-5-substituted-6-(5-chloropyridin-2-yl)-7-oxo-5,6-dihydropyrrolo[3,4b]pyrazine derivatives-precursors of (S)-(+)-Zopiclone, catalyzed by immobilized Candida antarctica B lipase in aqueous media. Tetrahedron:Asymmetry, 2003, 14(4), 429-438.
    • (2003) Tetrahedron:Asymmetry , vol.14 , Issue.4 , pp. 429-438
    • Palomo, J.M.1    Mateo, C.2    Fernández-Lorente, G.3    Solares, L.F.4    Diaz, M.5    Sánchez, V.M.6    Bayod, M.7    Gotor, V.8    Fernández-Lafuente, R.9    Guisán, J.M.10
  • 83
    • 40849142018 scopus 로고    scopus 로고
    • Lipase enzyme immobilization on synthetic beaded macroporous copolymers for kinetic resolution of chiral drugs intermediates
    • Bhushan, I.; Parshad, R, Qazi, G. N.; Ingavle, G.; Rajan, C.R.; Ponrathnam, S.; Gupta, V. K. Lipase enzyme immobilization on synthetic beaded macroporous copolymers for kinetic resolution of chiral drugs intermediates. Process Biochem., 2008, 43(4), 321-330.
    • (2008) Process Biochem , vol.43 , Issue.4 , pp. 321-330
    • Bhushan, I.1    Parshad, R.2    Qazi, G.N.3    Ingavle, G.4    Rajan, C.R.5    Ponrathnam, S.6    Gupta, V.K.7
  • 84
    • 38349039911 scopus 로고    scopus 로고
    • Large-scale rutheniumand enzyme-catalyzed dynamic kinetic resolution of (rac)- 1-phenylethanol
    • Bogár, K.; Martín-Matute, B.; Bäckvall, Beilstein, J.E. Large-scale rutheniumand enzyme-catalyzed dynamic kinetic resolution of (rac)- 1-phenylethanol. Beil. J. Org. Chem., 2007, 3(50), 1-3.
    • (2007) Beil. J. Org. Chem , vol.3 , Issue.50 , pp. 1-3
    • Bogár, K.1    Martín-Matute, B.2    Bäckvall Beilstein, J.E.3
  • 85
    • 81155134084 scopus 로고    scopus 로고
    • Lipase mediated sequential resolution of aromatic (3-hydroxy esters using fatty acid derivatives
    • Brem, J.; Naghi, M.; Toa, M.; Boros, Z.; Poppe, L.; Irimie, F.; Paizs, C. Lipase mediated sequential resolution of aromatic (3-hydroxy esters using fatty acid derivatives. Tetrahedron: Asymmetry, 2011, 22(16-17), 1672-1679.
    • (2011) Tetrahedron: Asymmetry , vol.22 , Issue.16-17 , pp. 1672-1679
    • Brem, J.1    Naghi, M.2    Toa, M.3    Boros, Z.4    Poppe, L.5    Irimie, F.6    Paizs, C.7
  • 86
    • 47549112707 scopus 로고    scopus 로고
    • E factors, green chemistry and catalysis: An odyssey
    • Sheldon, R.A. E factors, green chemistry and catalysis: an odyssey. Chem. Commun., 2008, 29, 3352-3365.
    • (2008) Chem. Commun , vol.29 , pp. 3352-3365
    • Sheldon, R.A.1
  • 87
    • 66449086922 scopus 로고    scopus 로고
    • First dynamic kinetic resolution of selenium-containing chiral amines catalyzed by palladium (Pd/BaSO4) and Candida antartica lipase (CAL-B)
    • Andrade, L.H.; Silva, A.V.; Pedrozo, E.C. First dynamic kinetic resolution of selenium-containing chiral amines catalyzed by palladium (Pd/BaSO4) and Candida antartica lipase (CAL-B). Tetrahe-dron Lett, 2009, 50(30), 4331-4334.
    • (2009) Tetrahe-dron Lett , vol.50 , Issue.30 , pp. 4331-4334
    • Andrade, L.H.1    Silva, A.V.2    Pedrozo, E.C.3
  • 88
    • 63749090004 scopus 로고    scopus 로고
    • A chemoenzymatic approach to enantiomerically pure amines using dynamic kinetic resolution: Application to the synthesis of norsertraline
    • Thalén, L.K.; Zhao, D.B.; Sortais, J.B.; Paetzold, J.; Hoben, C; Bäckvall, J.E. A chemoenzymatic approach to enantiomerically pure amines using dynamic kinetic resolution: application to the synthesis of norsertraline. Chem. Eur. J., 2009, 15(14), 3403-3410.
    • (2009) Chem. Eur. J , vol.15 , Issue.14 , pp. 3403-3410
    • Thalén, L.K.1    Zhao, D.B.2    Sortais, J.B.3    Paetzold, J.4    Hoben, C.5    Bäckvall, J.E.6
  • 89
    • 0027588112 scopus 로고
    • Enzymes in the synthesis of chiral drugs
    • Margolin, A.L. Enzymes in the synthesis of chiral drugs. Enzyme Microb. Technol., 1993, 15(4) 266-280.
    • (1993) Enzyme Microb. Technol , vol.15 , Issue.4 , pp. 266-280
    • Margolin, A.L.1
  • 90
    • 13644266926 scopus 로고    scopus 로고
    • Kinetic resolution of ketoprofen ester catalyzed by lipase from a mutant of CBS 5791
    • Liu, J.H.; Zhang, Y.Y.; Qiu, L.H.; Yang, F.K.; Ye, L.; Xia, Y.M. Kinetic resolution of ketoprofen ester catalyzed by lipase from a mutant of CBS 5791. J. Ind. Microbiol. Biotechnol., 2004, 31(11) 495-499.
    • (2004) J. Ind. Microbiol. Biotechnol , vol.31 , Issue.11 , pp. 495-499
    • Liu, J.H.1    Zhang, Y.Y.2    Qiu, L.H.3    Yang, F.K.4    Ye, L.5    Xia, Y.M.6
  • 91
    • 0022003825 scopus 로고
    • Stereoselective inversion of (R)-fenoprofen to (S)-fenoprofen in human
    • Rubin, A.; Knadler, M.P.; Ho, P.P.K.; Bebechtol, L.D.; Wolden, R.L. Stereoselective inversion of (R)-fenoprofen to (S)-fenoprofen in human. J. Pharm. Sci., 1985, 74(1) 82-84.
    • (1985) J. Pharm. Sci , vol.74 , Issue.1 , pp. 82-84
    • Rubin, A.1    Knadler, M.P.2    Ho, P.P.K.3    Bebechtol, L.D.4    Wolden, R.L.5
  • 92
    • 33646158910 scopus 로고    scopus 로고
    • Enantioselective properties of extracellular lipase from Serratia marcescens ES-2 for kinetic resolution of (S)-flurbiprofen
    • Bae, H.-A.; Lee, K.-W.; Lee, Y.-H. Enantioselective properties of extracellular lipase from Serratia marcescens ES-2 for kinetic resolution of (S)-flurbiprofen, J. Mol. Cat. B: Enzym., 2006, 40, (1-2), 24-29.
    • (2006) J. Mol. Cat. B: Enzym , vol.40 , Issue.1-2 , pp. 24-29
    • Bae, H.-A.1    Lee, K.-W.2    Lee, Y.-H.3
  • 93
    • 0027990305 scopus 로고
    • High enantioselective esterification of 2-arylpropionic acids catalyzed by immobilized lipase from Candida antarctica: A mechanistic approach
    • Arroyo, M.; Sinisterra, J.V. High enantioselective esterification of 2-arylpropionic acids catalyzed by immobilized lipase from Candida antarctica: a mechanistic approach. J. Org. Chem., 1994, 59(16), 4410-4417.
    • (1994) J. Org. Chem , vol.59 , Issue.16 , pp. 4410-4417
    • Arroyo, M.1    Sinisterra, J.V.2
  • 94
    • 70350584840 scopus 로고    scopus 로고
    • R,S-azolides as novel substrates for lipase catalyzed hydrolytic resolution in organic solvents
    • Wang, P.Y.; Chen, Y.J.; Wu, A.C.; Lin, Y.S.; Kao, M.F.; Chen, J.R.; Ciou, J.F.; Tsai, S.W. R,S-azolides as novel substrates for lipase catalyzed hydrolytic resolution in organic solvents. Adv. Synth. Catal, 2009, 351(14-15), 2333-2341.
    • (2009) Adv. Synth. Catal , vol.351 , Issue.14-15 , pp. 2333-2341
    • Wang, P.Y.1    Chen, Y.J.2    Wu, A.C.3    Lin, Y.S.4    Kao, M.F.5    Chen, J.R.6    Ciou, J.F.7    Tsai, S.W.8
  • 95
    • 0033615357 scopus 로고    scopus 로고
    • Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen
    • Mayer, T.U.; Kapoor, T.M.; Haggarty, S.J.; King, R.W.; Schreiber, S.L.; Mitchison, T.J. Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen. Science, 1999, 286, 971-974.
    • (1999) Science , vol.286 , pp. 971-974
    • Mayer, T.U.1    Kapoor, T.M.2    Haggarty, S.J.3    King, R.W.4    Schreiber, S.L.5    Mitchison, T.J.6
  • 97
    • 77952957283 scopus 로고    scopus 로고
    • Asymmetric biocatalysis with microbial enzymes and cells
    • Wohlgemuth, R. Asymmetric biocatalysis with microbial enzymes and cells. Curr. Opin Microbiol., 2010, 13(3), 283-292.
    • (2010) Curr. Opin Microbiol , vol.13 , Issue.3 , pp. 283-292
    • Wohlgemuth, R.1
  • 99
    • 46849084792 scopus 로고    scopus 로고
    • New, efficient synthesis of oseltamivir phosphate (Tamiflu) via enzymatic desymmetrization of a meso-1,3-cyclohexanedicarboxylic acid diester
    • Zutter, U.; Iding, H.; Spurr, P.; Wirz, B. New, efficient synthesis of oseltamivir phosphate (Tamiflu) via enzymatic desymmetrization of a meso-1,3-cyclohexanedicarboxylic acid diester. J. Org. Chem., 2008, 73(13), 4895-4902.
    • (2008) J. Org. Chem , vol.73 , Issue.13 , pp. 4895-4902
    • Zutter, U.1    Iding, H.2    Spurr, P.3    Wirz, B.4
  • 100
    • 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.; Guisan, J.M. Partial and enantioselective hydrolysis of diethyl phenylmalonate by immobilized preparations of lipase from Thermomyces lanuginose. Enzyme Microb. Technol, 2007, 40(5), 1280-1285.
    • (2007) Enzyme Microb. Technol , vol.40 , Issue.5 , pp. 1280-1285
    • Cabrera, Z.1    Palomo, J.M.2    Fernandez-Lorente, G.3    Fernandez-Lafuente, R.4    Guisan, J.M.5
  • 101
    • 68649084001 scopus 로고    scopus 로고
    • Novozym-435 displays very different selectivity compared to lipase from Candida antarctica B adsorbed on other hydrophobic supports
    • Cabrera, Z.; Fernandez-Lorente, G.; Fernandez-Lafuente, R.; Palomo, J.M.; Guisan, J.M. Novozym-435 displays very different selectivity compared to lipase from Candida antarctica B adsorbed on other hydrophobic supports J. Mol. Catal. B: Enzym. 2009, 57(1), 171-176.
    • (2009) J. Mol. Catal. B: Enzym , vol.57 , Issue.1 , pp. 171-176
    • Cabrera, Z.1    Fernandez-Lorente, G.2    Fernandez-Lafuente, R.3    Palomo, J.M.4    Guisan, J.M.5
  • 102
    • 84856374200 scopus 로고    scopus 로고
    • Enantioselective desymmetrization of prochiral diesters catalyzed by immobilized Rhizopus oryzae lipase
    • Cabrera, Z.; Palomo, J.M. Enantioselective desymmetrization of prochiral diesters catalyzed by immobilized Rhizopus oryzae lipase. Tetrahedron: Asymmetry, 2011, 22(24), 2080-2084.
    • (2011) Tetrahedron: Asymmetry , vol.22 , Issue.24 , pp. 2080-2084
    • Cabrera, Z.1    Palomo, J.M.2
  • 103
    • 33646079849 scopus 로고    scopus 로고
    • Enzymatic desymmetrization of 2,5-dideoxystreptamine precursors
    • Chenevert, R.; Jacques, F. Enzymatic desymmetrization of 2,5-dideoxystreptamine precursors. Tetrahedron: Asymmetry, 2006, 17(6), 1017-1021.
    • (2006) Tetrahedron: Asymmetry , vol.17 , Issue.6 , pp. 1017-1021
    • Chenevert, R.1    Jacques, F.2
  • 104
    • 32444439992 scopus 로고    scopus 로고
    • Preparation of a chiral synthon for an HBV inhibitor: Enzymatic asymmetric hydrolysis of (1a,2(3,3a)-2-(benzyloxymethyl)cyclopent-4-ene-1,3-diol diacetate and enzymatic asymmetric acetylation of (1a,2p,3a)-2-(benzyloxymethyl) cyclopent-4-ene-1,3-diol
    • Patel, R.N.; Banerjee, A.; Pendri, Y. R.; Liang, J.; Chen, C.-P.; Mueller, R. Preparation of a chiral synthon for an HBV inhibitor: enzymatic asymmetric hydrolysis of (1a,2(3,3a)-2-(benzyloxymethyl)cyclopent-4-ene-1,3-diol diacetate and enzymatic asymmetric acetylation of (1a,2p,3a)-2-(benzyloxymethyl) cyclopent-4-ene-1,3-diol. Tetrahedron: Asymmetry, 2006, 17(2), 175-178.
    • (2006) Tetrahedron: Asymmetry , vol.17 , Issue.2 , pp. 175-178
    • Patel, R.N.1    Banerjee, A.2    Pendri, Y.R.3    Liang, J.4    Chen, C.-P.5    Mueller, R.6
  • 105
    • 33745123011 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of both enantiomers of a-tocotrienol
    • Chenevert, R.; Courchesne, G.; Pelchat, N. Chemoenzymatic synthesis of both enantiomers of a-tocotrienol. Bioorg. Med. Chem., 2006, 14(15), 5389-5396.
    • (2006) Bioorg. Med. Chem , vol.14 , Issue.15 , pp. 5389-5396
    • Chenevert, R.1    Courchesne, G.2    Pelchat, N.3
  • 106
    • 61349147879 scopus 로고    scopus 로고
    • Synthesis of (-)-lobeline via enzymatic desymmetrization of lobelanidine
    • Chênevert, R.; Morin, P. Synthesis of (-)-lobeline via enzymatic desymmetrization of lobelanidine. Bioorg. Med. Chem., 2009, 17(5), 1837-1839.
    • (2009) Bioorg. Med. Chem , vol.17 , Issue.5 , pp. 1837-1839
    • Chênevert, R.1    Morin, P.2
  • 107
    • 4644296823 scopus 로고    scopus 로고
    • History, biology and chemistry of alkaloids from
    • Felpin, F. X.; Lebreton, J. History, biology and chemistry of alkaloids from Lobelia inflata. Tetrahedron, 2004, 60(45), 10127-10153.
    • (2004) Lobelia Inflata. Tetrahedron , vol.60 , Issue.45 , pp. 10127-10153
    • Felpin, F.X.1    Lebreton, J.2
  • 108
    • 39749162240 scopus 로고    scopus 로고
    • Lo-beline effects on tonic and methamphetamine-induced dopamine release
    • Wilhelm, C.J.; Johnson, R.A.; Eshleman, A.J.; Janowsky, A. Lo-beline effects on tonic and methamphetamine-induced dopamine release. Biochem. Pharmacol, 2008, 75(6), 1411-1415.
    • (2008) Biochem. Pharmacol , vol.75 , Issue.6 , pp. 1411-1415
    • Wilhelm, C.J.1    Johnson, R.A.2    Eshleman, A.J.3    Janowsky, A.4
  • 109
    • 56349168456 scopus 로고    scopus 로고
    • Synthesis and evaluation of a series of homologues of lobelane at the vesicular monoamine transporter-2
    • Zeng, G.; Dwoskin, L.P.; Deaciuc, A.G.; Crooks, P.A. Synthesis and evaluation of a series of homologues of lobelane at the vesicular monoamine transporter-2. Bioorg. Med. Chem. Lett., 2008, 18(24), 6509-6512.
    • (2008) Bioorg. Med. Chem. Lett , vol.18 , Issue.24 , pp. 6509-6512
    • Zeng, G.1    Dwoskin, L.P.2    Deaciuc, A.G.3    Crooks, P.A.4
  • 110
    • 33751242500 scopus 로고    scopus 로고
    • Vesicular monoamine transporter 2: Role as a novel target for drug development
    • Zheng, G.; Dwoskin, L.P.; Crooks, P.A. Vesicular monoamine transporter 2: role as a novel target for drug development. AAPS J., 2006, 8(4), E682-E692.
    • (2006) AAPS J , vol.8 , Issue.4
    • Zheng, G.1    Dwoskin, L.P.2    Crooks, P.A.3
  • 111
    • 35548970395 scopus 로고    scopus 로고
    • First desymmetrization of 1,3-propanediamine derivatives in organic solvent. Development of a new route for the preparation of optically active amines
    • Busto, E.; Gotor-Fernandez, V.; Montejo-Bernardo, J.; Garcia-Granda, S.; Gotor, V. First desymmetrization of 1,3-propanediamine derivatives in organic solvent. Development of a new route for the preparation of optically active amines. Org. Lett, 2007, 9(21), 4203-4206.
    • (2007) Org. Lett , vol.9 , Issue.21 , pp. 4203-4206
    • Busto, E.1    Gotor-Fernandez, V.2    Montejo-Bernardo, J.3    Garcia-Granda, S.4    Gotor, V.5
  • 113
    • 34247556420 scopus 로고    scopus 로고
    • Synthesis and medical applications of oligosaccharides
    • Seeberger, P.H.; Werz D.B. Synthesis and medical applications of oligosaccharides. Nature, 2007, 446, 1046-1051
    • (2007) Nature , vol.446 , pp. 1046-1051
    • Seeberger, P.H.1    Werz, D.B.2
  • 114
    • 44849094155 scopus 로고    scopus 로고
    • The Chemical Neurobiology of Carbohydrates
    • Murrey, H.E.; Hsieh-Wilson, L.C. The Chemical Neurobiology of Carbohydrates. Chem. Rev., 2008, 108, 1708-1731.
    • (2008) Chem. Rev , vol.108 , pp. 1708-1731
    • Murrey, H.E.1    Hsieh-Wilson, L.C.2
  • 115
    • 49749126041 scopus 로고    scopus 로고
    • Sweet antibiotics -the role of glycosidic residues in antibiotic and antitumor activity and their randomization
    • Kren, V.; Rezanka, T. Sweet antibiotics -the role of glycosidic residues in antibiotic and antitumor activity and their randomization. FEMS Microbiol Rev., 2008, 32, 858-889
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 858-889
    • Kren, V.1    Rezanka, T.2
  • 117
  • 118
    • 4744343655 scopus 로고    scopus 로고
    • Gaucher disease: Complexity in a simple disorder
    • Sidransky, E. Gaucher disease: complexity in a simple disorder. Mol. Genet. Metab. 2004, 83, 6-15
    • (2004) Mol. Genet. Metab , vol.83 , pp. 6-15
    • Sidransky, E.1
  • 119
    • 28444447140 scopus 로고    scopus 로고
    • Large-scale approaches for glycobiology
    • Campbell, C.T.; Yarema, K.J. Large-scale approaches for glycobiology. Genome Biol. 2005, 6, 236-244.
    • (2005) Genome Biol , vol.6 , pp. 236-244
    • Campbell, C.T.1    Yarema, K.J.2
  • 120
    • 70350441377 scopus 로고    scopus 로고
    • Opportunities and challenges in synthetic oligosaccharide and glycoconjugate research
    • Boltje, T.J.; Buskas, T.; Boons, G.J. Opportunities and challenges in synthetic oligosaccharide and glycoconjugate research. Nat. Chem., 2009, 1, 611-622.
    • (2009) Nat. Chem , vol.1 , pp. 611-622
    • Boltje, T.J.1    Buskas, T.2    Boons, G.J.3
  • 124
    • 67749116255 scopus 로고    scopus 로고
    • Biologics through chemistry: Total synthesis of a proposed dual-acting vaccine targeting ovarian cancer by orchestration of oligosaccharide and polypeptide domains
    • Zhu, J.; Wan, Q.; Ragupathi, G.; George, C. M.; Livingston, P. O. and Danishefsky, S. J. Biologics through chemistry: Total synthesis of a proposed dual-acting vaccine targeting ovarian cancer by orchestration of oligosaccharide and polypeptide domains. J. Am. Chem. Soc., 2009, 131, 4151-4158.
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 4151-4158
    • Zhu, J.1    Wan, Q.2    Ragupathi, G.3    George, C.M.4    Livingston, P.O.5    Danishefsky, S.J.6
  • 125
    • 0031993483 scopus 로고    scopus 로고
    • Glycosidases and glycosyl transferases in glycoside and oligosaccharide synthesis
    • Crout, D.H.; Vic, G. Glycosidases and glycosyl transferases in glycoside and oligosaccharide synthesis. Curr. Opin. Chem. Biol., 1998, 2, 98-111.
    • (1998) Curr. Opin. Chem. Biol , vol.2 , pp. 98-111
    • Crout, D.H.1    Vic, G.2
  • 126
    • 84876734301 scopus 로고    scopus 로고
    • Enzymatic synthesis of oligosaccha-rides: A powerful tool for a sweet challenge
    • Filice, M.; Marciello, M. Enzymatic synthesis of oligosaccha-rides: a powerful tool for a sweet challenge. Curr. Org. Chem. 2013, 17, 701-718;
    • (2013) Curr. Org. Chem , vol.17 , pp. 701-718
    • Filice, M.1    Marciello, M.2
  • 127
    • 79960566715 scopus 로고    scopus 로고
    • Enzymes in the Synthesis of Glycoconjugates
    • Schmaltz, R.M.; Hanson, S.R.; Wong, C.-H. Enzymes in the Synthesis of Glycoconjugates. Chem. Rev., 2011, 111, 4259-4307;
    • (2011) Chem. Rev , vol.111 , pp. 4259-4307
    • Schmaltz, R.M.1    Hanson, S.R.2    Wong, C.-H.3
  • 129
    • 39849108963 scopus 로고    scopus 로고
    • Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update covering the period 2001-2002
    • Harvey, D.J. Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: an update covering the period 2001-2002. Mass Spectrom. Rev., 2008, 27, 125-201.
    • (2008) Mass Spectrom. Rev , vol.27 , pp. 125-201
    • Harvey, D.J.1
  • 130
    • 77951761659 scopus 로고    scopus 로고
    • Chemical and Chemoenzymatic Synthesis of Glycopeptide Selectin Ligands Containing Sialyl LewisX Structures
    • Pudelko, M.; Bull, J.; Kunz, H. Chemical and Chemoenzymatic Synthesis of Glycopeptide Selectin Ligands Containing Sialyl LewisX Structures. ChemBioChem, 2010, 11, 904-930;
    • (2010) ChemBioChem , vol.11 , pp. 904-930
    • Pudelko, M.1    Bull, J.2    Kunz, H.3
  • 131
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related al-pha-keto acids: An evolutionary perspective
    • Angata, T.; Varki, A. Chemical diversity in the sialic acids and related al-pha-keto acids: an evolutionary perspective. Chem. Rev., 2002, 102, 439-469.
    • (2002) Chem. Rev , vol.102 , pp. 439-469
    • Angata, T.1    Varki, A.2
  • 132
    • 33646446233 scopus 로고    scopus 로고
    • Bacterial Sialyltransferases for Carbohydrate Synthesis
    • Schwardt, O.; Visekruna, T.; Rabbani, S.; Ernst, B. Bacterial Sialyltransferases for Carbohydrate Synthesis. Chimia, 2006, 60, 234-260;
    • (2006) Chimia , vol.60 , pp. 234-260
    • Schwardt, O.1    Visekruna, T.2    Rabbani, S.3    Ernst, B.4
  • 133
    • 84862842242 scopus 로고    scopus 로고
    • Sialic acid metabolism and sialyltrans-ferases: Natural functions and applications
    • Li, Y.; Chen, X. Sialic acid metabolism and sialyltrans-ferases: natural functions and applications. Appl. Microbiol. Bio-technol., 2012, 94, 887-905.
    • (2012) Appl. Microbiol. Bio-technol , vol.94 , pp. 887-905
    • Li, Y.1    Chen, X.2
  • 136
    • 79953328716 scopus 로고    scopus 로고
    • Gly-cosyltransferases as biocatalysts
    • Palcic, M.M. Gly-cosyltransferases as biocatalysts. Curr. Opin. Chem. Biol., 2011, 15, 226-233.
    • (2011) Curr. Opin. Chem. Biol , vol.15 , pp. 226-233
    • Palcic, M.M.1
  • 137
    • 85015328820 scopus 로고    scopus 로고
    • The amazing transglycosylation activity of endo-beta-N-acetylglucosaminidases
    • Wang, L.X. The amazing transglycosylation activity of endo-beta-N-acetylglucosaminidases. Trends Glycosci. Glycotechnol., 2011, 23, 33-52.
    • (2011) Trends Glycosci. Glycotechnol , vol.23 , pp. 33-52
    • Wang, L.X.1
  • 138
    • 33750501375 scopus 로고    scopus 로고
    • A remodeling system for the oligosac-charide chains on glycoproteins with microbial endo-beta-N-acetylglucosaminidases
    • Fujita, K.; Yamamoto, K. A remodeling system for the oligosac-charide chains on glycoproteins with microbial endo-beta-N-acetylglucosaminidases. Biochim. Biophys. Acta, 2006, 1760, 1631-1635.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 1631-1635
    • Fujita, K.1    Yamamoto, K.A.2
  • 139
    • 16244410130 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of CD52 glycoproteins carrying native N-glycans
    • Li, H.; Singh, S.; Zeng, Y.; Song, H.; Wang, L.-X. Chemoenzymatic synthesis of CD52 glycoproteins carrying native N-glycans. Bioorg. Med. Chem. Lett., 2005, 15, 895-898;
    • (2005) Bioorg. Med. Chem. Lett , vol.15 , pp. 895-898
    • Li, H.1    Singh, S.2    Zeng, Y.3    Song, H.4    Wang, L.-X.5
  • 140
    • 75149148126 scopus 로고    scopus 로고
    • Chemo-enzymatic synthesis of glycosylated insulin using a GlcNAc tag
    • Toma-bechi, Y.; Suzuki, R.; Haneda, K.; Inazu, T. Chemo-enzymatic synthesis of glycosylated insulin using a GlcNAc tag. Bioorg. Med. Chem., 2010, 18, 1259-1264;
    • (2010) Bioorg. Med. Chem , vol.18 , pp. 1259-1264
    • Toma-Bechi, Y.1    Suzuki, R.2    Haneda, K.3    Inazu, T.4
  • 141
    • 52949115690 scopus 로고    scopus 로고
    • Gly-coengineering of human IgG1-Fc through combined yeast expression and in vitro chemoenzymatic glycosylation
    • Wei, Y.; Li, C.; Huang, W.; Li, B.; Strome, S.; Wang, L.-X. Gly-coengineering of human IgG1-Fc through combined yeast expression and in vitro chemoenzymatic glycosylation. Biochemistry, 2008, 47, 10294-10304;
    • (2008) Biochemistry , vol.47 , pp. 10294-10304
    • Wei, Y.1    Li, C.2    Huang, W.3    Li, B.4    Strome, S.5    Wang, L.-X.6
  • 144
    • 84870033371 scopus 로고    scopus 로고
    • Regioselective monodeprotection of peracetylated carbohydrates
    • Filice, M.; Guisan, J.M.; Terreni, M.; Palomo, J.M. Regioselective monodeprotection of peracetylated carbohydrates. Nat. Protoc, 2012, 7, 1783-1796.
    • (2012) Nat. Protoc , vol.7 , pp. 1783-1796
    • Filice, M.1    Guisan, J.M.2    Terreni, M.3    Palomo, J.M.4
  • 146
    • 0141683550 scopus 로고    scopus 로고
    • Synthesis of N-Acetyllactosamine Derivatives with Variation in the Aglycon Moiety for the Study of Inhibition of Sialyl Lewis X Expression
    • Mong, T. K. K.; Lee, L. V.; Brown, J. R.; Esko J. D.; Wong, C. H. Synthesis of N-Acetyllactosamine Derivatives with Variation in the Aglycon Moiety for the Study of Inhibition of Sialyl Lewis X Expression. ChemBioChem, 2003, 4(9), 835-840
    • (2003) ChemBioChem , vol.4 , Issue.9 , pp. 835-840
    • Mong, T.K.K.1    Lee, L.V.2    Brown, J.R.3    Esko, J.D.4    Wong, C.H.5
  • 147
    • 37849012760 scopus 로고    scopus 로고
    • Improved utilization of renewable resources: New important derivative of glycerol
    • Behr, A.; Eilting, J.; Irawadi, K.; Leschinski, J.; Lindner, F. Improved utilization of renewable resources: new important derivative of glycerol. Green Chem., 2008, 10, 13-30.
    • (2008) Green Chem , vol.10 , pp. 13-30
    • Behr, A.1    Eilting, J.2    Irawadi, K.3    Leschinski, J.4    Lindner, F.5
  • 148
    • 38549149213 scopus 로고    scopus 로고
    • Chemoselective catalytic conversion of glycerol as a biorenewable source to valuable commodity chemicals
    • Zhou, C.H.; Beltramini, J.N.; Fan, Y.X.; Lu, G.Q. Chemoselective catalytic conversion of glycerol as a biorenewable source to valuable commodity chemicals. Chem. Soc. Rev., 2008, 37, 527-549.
    • (2008) Chem. Soc. Rev , vol.37 , pp. 527-549
    • Zhou, C.H.1    Beltramini, J.N.2    Fan, Y.X.3    Lu, G.Q.4
  • 150
    • 84858752733 scopus 로고    scopus 로고
    • Design and analysis of biorefineries based on raw glycerol: Addressing the glycerol problem
    • Posada J.A.; Rincón L.E.; Cardona C.A. Design and analysis of biorefineries based on raw glycerol: addressing the glycerol problem. Bioresour Technol., 2012, 111, 282-93.
    • (2012) Bioresour Technol , vol.111 , pp. 282-293
    • Posada, J.A.1    Rincón, L.E.2    Cardona, C.A.3
  • 151
    • 84867289760 scopus 로고    scopus 로고
    • Biodiesel biorefin-ery: Opportunities and challenges for microbial production of fuels and chemicals from glycerol waste
    • doi:10.1186/1754-6834-5-48
    • Almeida, J.R.M.; Favaro, L.C.L.; Quirino, B.F. Biodiesel biorefin-ery: opportunities and challenges for microbial production of fuels and chemicals from glycerol waste. Biotechnology for Biofuels, 2012, 5:48. doi:10.1186/1754-6834-5-48
    • (2012) Biotechnology For Biofuels , vol.5 , pp. 48
    • Almeida, J.R.M.1    Favaro, L.C.L.2    Quirino, B.F.3
  • 152
    • 0026354534 scopus 로고
    • Regio- and stereoselective enzymatic esterification of glycerol and its derivatives
    • Mazur, A.W.; Hiler I.I.; Lee, S.S.C.; Armstrong, M.P.; Wendel, J.D. Regio- and stereoselective enzymatic esterification of glycerol and its derivatives. Chem. Phys, 1991, 60, 189-199.
    • (1991) Chem. Phys , vol.60 , pp. 189-199
    • Mazur, A.W.1    Hiler, I.I.2    Lee, S.S.C.3    Armstrong, M.P.4    Wendel, J.D.5
  • 154
    • 50449108577 scopus 로고    scopus 로고
    • Interfacially activated lipases against hydrophobic supports: Effect of the support nature on the biocatalytic properties
    • Fernandez-Lorente, G.; Cabrera, Z.; Godoy, C; Fernandez-Lafuente, R.; Palomo, J.M.; Guisan, J.M. Interfacially activated lipases against hydrophobic supports: Effect of the support nature on the biocatalytic properties. Process Biochem., 2008, 43, 106-1067.
    • (2008) Process Biochem , vol.43 , pp. 106-1067
    • Fernandez-Lorente, G.1    Cabrera, Z.2    Godoy, C.3    Fernandez-Lafuente, R.4    Palomo, J.M.5    Guisan, J.M.6
  • 155
    • 79959618149 scopus 로고    scopus 로고
    • Application of response surface design to solvent, temperature and lipase selection for optimal monoglyceride production
    • Cetina, D.M.; Giraldo, G.I.; Orrego, C.E. Application of response surface design to solvent, temperature and lipase selection for optimal monoglyceride production. J. Mol. Cat. B: Enzym., 2011. 72, 13-19.
    • (2011) J. Mol. Cat. B: Enzym , vol.72 , pp. 13-19
    • Cetina, D.M.1    Giraldo, G.I.2    Orrego, C.E.3
  • 156
    • 84856228207 scopus 로고    scopus 로고
    • Obtaining monoglycerides by esterification of glycerol with palmitic acid using some high preparations of Candida antarctica lipase B
    • Kappor, M.; Gupta, M.N. Obtaining monoglycerides by esterification of glycerol with palmitic acid using some high preparations of Candida antarctica lipase B. Process Biochem., 2012, 47, 503-508.
    • (2012) Process Biochem , vol.47 , pp. 503-508
    • Kappor, M.1    Gupta, M.N.2
  • 157
    • 46849110667 scopus 로고    scopus 로고
    • Lipase catalyzed synthesis of ester-based surfactants from biomass derivatives
    • Karmee, S.K. Lipase catalyzed synthesis of ester-based surfactants from biomass derivatives. Biofuels Bioprod. Bioref, 2008, 2, 144-154.
    • (2008) Biofuels Bioprod. Bioref , vol.2 , pp. 144-154
    • Karmee, S.K.1
  • 159
    • 77951221594 scopus 로고    scopus 로고
    • The solvent influence on the positional selectivity of Novozym 435 during 1,3-diolein synthesis by esterification
    • Duan, Z.Q.; Du, W.; Liu, D.H. The solvent influence on the positional selectivity of Novozym 435 during 1,3-diolein synthesis by esterification. Bioresour. Technol., 2010, 101, 2568-2571.
    • (2010) Bioresour. Technol , vol.101 , pp. 2568-2571
    • Duan, Z.Q.1    Du, W.2    Liu, D.H.3
  • 160
    • 82455175264 scopus 로고    scopus 로고
    • The mechanism of solvent effect on the positional selectivity of Candida antarctica lipase B during 1,3-diolein synthesis by esterification
    • Duan, Z.Q.; Du, W.; Liu, D.H. The mechanism of solvent effect on the positional selectivity of Candida antarctica lipase B during 1,3-diolein synthesis by esterification. Bioresour. Technol., 2011, 102, 11048-11050.
    • (2011) Bioresour. Technol , vol.102 , pp. 11048-11050
    • Duan, Z.Q.1    Du, W.2    Liu, D.H.3
  • 161
    • 0033571280 scopus 로고    scopus 로고
    • A novel method for preparation of optically active a-monobenzoyl glycerol, via lipase-catalyzed asymmetric transesterification of glycerol
    • Kato, Y.; Fujiwara, I.; Asano, Y. A novel method for preparation of optically active a-monobenzoyl glycerol, via lipase-catalyzed asymmetric transesterification of glycerol. Bioorg. Med. Chem. Lett., 1999, 9, 3207-3210.
    • (1999) Bioorg. Med. Chem. Lett , vol.9 , pp. 3207-3210
    • Kato, Y.1    Fujiwara, I.2    Asano, Y.3
  • 162
    • 0034697218 scopus 로고    scopus 로고
    • Synthesis of optically active a-monobenzoyl glycerol by asymmetric transesterification of glycerol
    • Kato, Y.; Fujiwara, I.; Asano, Y. Synthesis of optically active a-monobenzoyl glycerol by asymmetric transesterification of glycerol. J. Mol. Catal. B: Enzym., 2000, 9, 193-200.
    • (2000) J. Mol. Catal. B: Enzym , vol.9 , pp. 193-200
    • Kato, Y.1    Fujiwara, I.2    Asano, Y.3
  • 163
    • 84855802459 scopus 로고    scopus 로고
    • Esterification of benzoic acid and glycerol to a-monobenzoate glycerol in solventless media using an industrial free Candida antarctica lipase B
    • Tamayo, J.J.; Ladero, M.; Santos, V.E.; Garcia-Ochoa, F. Esterification of benzoic acid and glycerol to a-monobenzoate glycerol in solventless media using an industrial free Candida antarctica lipase B. Process Biochem., 2012, 47, 243.250.
    • (2012) Process Biochem , vol.47 , Issue.243 , pp. 250
    • Tamayo, J.J.1    Ladero, M.2    Santos, V.E.3    Garcia-Ochoa, F.4
  • 164
    • 78650700231 scopus 로고    scopus 로고
    • Kinetically controlled synthesis of monoglyceryl esters from chiral and prochiral acids methylesters catalyzed by immobilized Rhizomucor miehei lipase
    • Acosta, A.; Filice, M.; Frenandez-Lorente, G.; Palomo, J.M.; Guisan, J.M. Kinetically controlled synthesis of monoglyceryl esters from chiral and prochiral acids methylesters catalyzed by immobilized Rhizomucor miehei lipase. Bioresour Technol, 2011, 102, 507-512.
    • (2011) Bioresour Technol , vol.102 , pp. 507-512
    • Acosta, A.1    Filice, M.2    Frenandez-Lorente, G.3    Palomo, J.M.4    Guisan, J.M.5
  • 165
    • 84861347987 scopus 로고    scopus 로고
    • A biocatalytic approach for regioselective monoacetylation of 3-aryloxy-1,2-propanediols by porcine pancreatic lipase
    • Meena, V.S.; Banerjee, U.C. A biocatalytic approach for regioselective monoacetylation of 3-aryloxy-1,2-propanediols by porcine pancreatic lipase. Monatsh Chem., 2012, 143, 951-953.
    • (2012) Monatsh Chem , vol.143 , pp. 951-953
    • Meena, V.S.1    Banerjee, U.C.2
  • 166
    • 0242718982 scopus 로고    scopus 로고
    • Lipase-catalyzed enantiotope selective acetylation of 2-acyloxypropane-1,3-diols.Influence of the acyl moiety on selectivity
    • Egri, G.; Bálint, J.; Peredi, R.; Fogassy, E.; Novák, L.; Poppe, L. Lipase-catalyzed enantiotope selective acetylation of 2-acyloxypropane-1,3-diols.Influence of the acyl moiety on selectivity. J. Mol. Catal. B, Enzym., 2000, 10, 583-596.
    • (2000) J. Mol. Catal. B, Enzym , vol.10 , pp. 583-596
    • Egri, G.1    Bálint, J.2    Peredi, R.3    Fogassy, E.4    Novák, L.5    Poppe, L.6
  • 167
    • 8144223103 scopus 로고    scopus 로고
    • Lipase-mediated desymmetrization of glycerol with aromatic and aliphatic anhydrides
    • Batovska, D.I.; Tsubota, S.; Kato, Y.; Asano, Y.; Ubukata, M. Lipase-mediated desymmetrization of glycerol with aromatic and aliphatic anhydrides. Tetrahedron: Asymmetry, 2004, 15, 3551-3559.
    • (2004) Tetrahedron: Asymmetry , vol.15 , pp. 3551-3559
    • Batovska, D.I.1    Tsubota, S.2    Kato, Y.3    Asano, Y.4    Ubukata, M.5
  • 168
    • 33749856055 scopus 로고    scopus 로고
    • Enzymatic Glycerolysis and transesterification of vegetable oil for enhanced production of feruloy-lated glycerol
    • Laszlo, J.A.; Compton, D.L. Enzymatic Glycerolysis and transesterification of vegetable oil for enhanced production of feruloy-lated glycerol. J. Am. Oil Chem. Soc, 2006, 83, 765-770.
    • (2006) J. Am. Oil Chem. Soc , vol.83 , pp. 765-770
    • Laszlo, J.A.1    Compton, D.L.2
  • 169
    • 33645297655 scopus 로고    scopus 로고
    • Lipase-catalyzed transesterification of trilinolein or trilinolenin with selected phenolic acids
    • Sabally, K.; Karboune, S.; St-Louis, R.; Kermasha, S. Lipase-catalyzed transesterification of trilinolein or trilinolenin with selected phenolic acids. J. Am. Oil Chem. Soc, 2006, 83, 101-107.
    • (2006) J. Am. Oil Chem. Soc , vol.83 , pp. 101-107
    • Sabally, K.1    Karboune, S.2    St-Louis, R.3    Kermasha, S.4
  • 170
    • 35748942247 scopus 로고    scopus 로고
    • A novel, two consecutive enzyme synthesis of feruloylated monoa-cyl- and diacyl-glycerols in a solvent-free system
    • Sun, S.D.; Shan, L.; Liu, Y.F.; Jin, Q.Z.; Wang, X.G.; Wang, Z.M. A novel, two consecutive enzyme synthesis of feruloylated monoa-cyl- and diacyl-glycerols in a solvent-free system. Biotechnol. Lett., 2007, 29, 1947-1950.
    • (2007) Biotechnol. Lett , vol.29 , pp. 1947-1950
    • Sun, S.D.1    Shan, L.2    Liu, Y.F.3    Jin, Q.Z.4    Wang, X.G.5    Wang, Z.M.6
  • 171
    • 38949218356 scopus 로고    scopus 로고
    • Solvent-free enzymatic preparation of feruloylated monoacylglyc-erols optimized by response surface methodology
    • Sun, S.D.; Shan, L.; Liu, Y.F.; Jin, Q.Z.; Zhang, L.X.; Wang, X.G. Solvent-free enzymatic preparation of feruloylated monoacylglyc-erols optimized by response surface methodology. J. Agric. Food Chem., 2008, 56, 442-447.
    • (2008) J. Agric. Food Chem , vol.56 , pp. 442-447
    • Sun, S.D.1    Shan, L.2    Liu, Y.F.3    Jin, Q.Z.4    Zhang, L.X.5    Wang, X.G.6
  • 172
    • 80052961416 scopus 로고    scopus 로고
    • Lipase-catalyzed synthesis of 4-mrthoxy cinnamoyl glycerol
    • Patil, D.; Dev, B.; Nag, A. Lipase-catalyzed synthesis of 4-mrthoxy cinnamoyl glycerol. J. Mol. Catal. B: Enzym., 2011, 73, 5-8.
    • (2011) J. Mol. Catal. B: Enzym , vol.73 , pp. 5-8
    • Patil, D.1    Dev, B.2    Nag, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.