메뉴 건너뛰기




Volumn 101, Issue 2, 2017, Pages 513-519

Comparison of lipases and glycoside hydrolases as catalysts in synthesis reactions

Author keywords

Glycoside hydrolase; Lipase; Transesterification; Transglycosylation

Indexed keywords

BIOCHEMICAL ENGINEERING; CATALYSIS; ENZYMES; LIPASES; NUCLEOPHILES; PLANTS (BOTANY); REACTION INTERMEDIATES; SUGARS; TRANSESTERIFICATION;

EID: 85006410860     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-016-8055-x     Document Type: Review
Times cited : (25)

References (32)
  • 1
    • 0027273474 scopus 로고
    • Activation of enzymes in organic media at low water activity by polyols and saccharides
    • COI: 1:CAS:528:DyaK3sXmsV2lsr4%3D, PID: 8490046
    • Adlercreutz P (1993) Activation of enzymes in organic media at low water activity by polyols and saccharides. Biochim Biophys Acta 1163(2):144–148
    • (1993) Biochim Biophys Acta , vol.1163 , Issue.2 , pp. 144-148
    • Adlercreutz, P.1
  • 2
    • 84880105945 scopus 로고    scopus 로고
    • Immobilisation and application of lipases in organic media
    • COI: 1:CAS:528:DC%2BC3sXhtVKhtrvN, PID: 23403895
    • Adlercreutz P (2013) Immobilisation and application of lipases in organic media. Chem Soc Rev 42(15):6406–6436. doi:10.1039/c3cs35446f
    • (2013) Chem Soc Rev , vol.42 , Issue.15 , pp. 6406-6436
    • Adlercreutz, P.1
  • 3
    • 84929941359 scopus 로고    scopus 로고
    • Glycosynthesis in a waterworld: new insight into the molecular basis of transglycosylation in retaining glycoside hydrolases
    • COI: 1:CAS:528:DC%2BC2MXkvVOrsr0%3D, PID: 25793417
    • Bissaro B, Monsan P, Faure R, O'Donohue MJ (2015) Glycosynthesis in a waterworld: new insight into the molecular basis of transglycosylation in retaining glycoside hydrolases. Biochem J 467(1):17–35. doi:10.1042/bj20141412
    • (2015) Biochem J , vol.467 , Issue.1 , pp. 17-35
    • Bissaro, B.1    Monsan, P.2    Faure, R.3    O'Donohue, M.J.4
  • 5
    • 77953220531 scopus 로고    scopus 로고
    • The XTH gene family: an update on enzyme structure, function, and phylogeny in xyloglucan remodeling
    • PID: 20421457
    • Eklof JM, Brumer H (2010) The XTH gene family: an update on enzyme structure, function, and phylogeny in xyloglucan remodeling. Plant Physiol 153(2):456–466. doi:10.1104/pp.110.156844
    • (2010) Plant Physiol , vol.153 , Issue.2 , pp. 456-466
    • Eklof, J.M.1    Brumer, H.2
  • 6
    • 27744561670 scopus 로고    scopus 로고
    • Converting a β-glycosidase into a β-transglycosidase by directed evolution
    • COI: 1:CAS:528:DC%2BD2MXhtFKhtLrL, PID: 16085651
    • Feng H-Y, Drone J, Hoffmann L, Tran V, Tellier C, Rabiller C, Dion M (2005) Converting a β-glycosidase into a β-transglycosidase by directed evolution. J Biol Chem 280(44):37088–37097. doi:10.1074/jbc.M502873200
    • (2005) J Biol Chem , vol.280 , Issue.44 , pp. 37088-37097
    • Feng, H.-Y.1    Drone, J.2    Hoffmann, L.3    Tran, V.4    Tellier, C.5    Rabiller, C.6    Dion, M.7
  • 7
    • 0026517617 scopus 로고
    • Enzyme function in organic solvents
    • COI: 1:CAS:528:DyaK38Xht1elsrc%3D, PID: 1730231
    • Gupta MN (1992) Enzyme function in organic solvents. Eur J Biochem 203(1–2):25–32. doi:10.1111/j.1432-1033.1992.tb19823.x
    • (1992) Eur J Biochem , vol.203 , Issue.1-2 , pp. 25-32
    • Gupta, M.N.1
  • 8
    • 0028396938 scopus 로고
    • Thermodynamic predictions for biocatalysis in nonconventional media: theory, tests and recommendations for experimental design and analysis
    • COI: 1:CAS:528:DyaK2cXitFWisbk%3D
    • Halling PJ (1994) Thermodynamic predictions for biocatalysis in nonconventional media: theory, tests and recommendations for experimental design and analysis. Enzym Microb Technol 16:178–206
    • (1994) Enzym Microb Technol , vol.16 , pp. 178-206
    • Halling, P.J.1
  • 9
    • 0035924115 scopus 로고    scopus 로고
    • Enhanced transglucosylation/hydrolysis ratio of mutants of Pyrococcus furiosus β-glucosidase: effects of donor concentration, water content, and temperature on activity and selectivity in hexanol
    • COI: 1:CAS:528:DC%2BD3MXovFOhs78%3D, PID: 11745143
    • Hansson T, Adlercreutz P (2001) Enhanced transglucosylation/hydrolysis ratio of mutants of Pyrococcus furiosus β-glucosidase: effects of donor concentration, water content, and temperature on activity and selectivity in hexanol. Biotechnol Bioeng 75:656–665
    • (2001) Biotechnol Bioeng , vol.75 , pp. 656-665
    • Hansson, T.1    Adlercreutz, P.2
  • 10
    • 0035813475 scopus 로고    scopus 로고
    • Influence of water activity on the competition between β-glycosidase-catalysed transglycosylation and hydrolysis in aqueous hexanol
    • COI: 1:CAS:528:DC%2BD3MXnsVSls7k%3D
    • Hansson T, Andersson M, Wehtje E, Adlercreutz P (2001) Influence of water activity on the competition between β-glycosidase-catalysed transglycosylation and hydrolysis in aqueous hexanol. Enzym Microb Technol 29:527–534
    • (2001) Enzym Microb Technol , vol.29 , pp. 527-534
    • Hansson, T.1    Andersson, M.2    Wehtje, E.3    Adlercreutz, P.4
  • 11
    • 0032946805 scopus 로고    scopus 로고
    • Kinetics of lipase-catalyzed esterification in organic media: correct model and solvent effects on parameters
    • COI: 1:CAS:528:DyaK1MXjtVOjsb0%3D
    • Janssen AEM, Sjursnes BJ, Vakurov AV, Halling P (1999) Kinetics of lipase-catalyzed esterification in organic media: correct model and solvent effects on parameters. Enzym Microb Technol 24:463–470
    • (1999) Enzym Microb Technol , vol.24 , pp. 463-470
    • Janssen, A.E.M.1    Sjursnes, B.J.2    Vakurov, A.V.3    Halling, P.4
  • 12
    • 34848871965 scopus 로고    scopus 로고
    • Conversion of a cyclodextrin glucanotransferase into an alpha-amylase: assessment of directed evolution strategies
    • COI: 1:CAS:528:DC%2BD2sXhtVSgs7jK, PID: 17824673
    • Kelly RM, Leemhuis H, Dijkhuizen L (2007) Conversion of a cyclodextrin glucanotransferase into an alpha-amylase: assessment of directed evolution strategies. Biochemistry 46(39):11216–11222. doi:10.1021/bi701160h
    • (2007) Biochemistry , vol.46 , Issue.39 , pp. 11216-11222
    • Kelly, R.M.1    Leemhuis, H.2    Dijkhuizen, L.3
  • 13
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • COI: 1:CAS:528:DC%2BD3MXlvFWiuw%3D%3D, PID: 11196652
    • Klibanov AM (2001) Improving enzymes by using them in organic solvents. Nature 409:241–246
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 14
    • 0028166876 scopus 로고
    • Enzymatic synthesis of octyl-β-glucoside in octanol at controlled water activity
    • COI: 1:CAS:528:DyaK2cXmsFKitrc%3D
    • Ljunger G, Adlercreutz P, Mattiasson B (1994) Enzymatic synthesis of octyl-β-glucoside in octanol at controlled water activity. Enzym Microb Technol 16(9):751–755
    • (1994) Enzym Microb Technol , vol.16 , Issue.9 , pp. 751-755
    • Ljunger, G.1    Adlercreutz, P.2    Mattiasson, B.3
  • 15
    • 84877140768 scopus 로고    scopus 로고
    • Improved transferase/hydrolase ratio through rational design of a family 1 β-glucosidase from Thermotoga neapolitana
    • COI: 1:CAS:528:DC%2BC3sXotFamt70%3D, PID: 23524680
    • Lundemo P, Adlercreutz P, Karlsson EN (2013) Improved transferase/hydrolase ratio through rational design of a family 1 β-glucosidase from Thermotoga neapolitana. Appl Environ Microbiol 79(11):3400–3405. doi:10.1128/aem.00359-13
    • (2013) Appl Environ Microbiol , vol.79 , Issue.11 , pp. 3400-3405
    • Lundemo, P.1    Adlercreutz, P.2    Karlsson, E.N.3
  • 16
    • 84904191330 scopus 로고    scopus 로고
    • Preparation of two glycoside hydrolases for use in micro-aqueous media
    • COI: 1:CAS:528:DC%2BC2cXht1OrurvL
    • Lundemo P, Karlsson EN, Adlercreutz P (2014) Preparation of two glycoside hydrolases for use in micro-aqueous media. Journal of Molecular Catalysis B-Enzymatic 108:1–6. doi:10.1016/j.molcatb.2014.06.009
    • (2014) Journal of Molecular Catalysis B-Enzymatic , vol.108 , pp. 1-6
    • Lundemo, P.1    Karlsson, E.N.2    Adlercreutz, P.3
  • 17
    • 84988723863 scopus 로고    scopus 로고
    • Eliminating hydrolytic activity without affecting the transglycosylation of a GH1 β-glucosidase
    • Lundemo P, Nordberg Karlsson E, Adlercreutz P (2016) Eliminating hydrolytic activity without affecting the transglycosylation of a GH1 β-glucosidase. Appl Microbiol Biotechnol. doi:10.1007/s00253-016-7833-9
    • (2016) Appl Microbiol Biotechnol
    • Lundemo, P.1    Nordberg Karlsson, E.2    Adlercreutz, P.3
  • 18
    • 0037010874 scopus 로고    scopus 로고
    • Water activity dependence of lipase catalysis in organic media explains successful transesterification reactions
    • COI: 1:CAS:528:DC%2BD38XovFGqsbg%3D
    • Ma L, Persson M, Adlercreutz P (2002) Water activity dependence of lipase catalysis in organic media explains successful transesterification reactions. Enzym Microb Technol 31:1024–1029
    • (2002) Enzym Microb Technol , vol.31 , pp. 1024-1029
    • Ma, L.1    Persson, M.2    Adlercreutz, P.3
  • 19
    • 84940928537 scopus 로고    scopus 로고
    • Enzymatic preparation of oligosaccharides by transglycosylation: a comparative study of glucosidases
    • COI: 1:CAS:528:DC%2BC2MXhsVKgsrrI
    • Mangas-Sanchez J, Adlercreutz P (2015) Enzymatic preparation of oligosaccharides by transglycosylation: a comparative study of glucosidases. J Mol Catal B: Enz 122:51–55
    • (2015) J Mol Catal B: Enz , vol.122 , pp. 51-55
    • Mangas-Sanchez, J.1    Adlercreutz, P.2
  • 20
    • 77952899716 scopus 로고    scopus 로고
    • Transglucosidases as efficient tools for oligosaccharide and glucoconjugate synthesis
    • COI: 1:CAS:528:DC%2BC3cXntVSlurg%3D, PID: 20362489
    • Monsan P, Remaud-Simeon M, Andre I (2010) Transglucosidases as efficient tools for oligosaccharide and glucoconjugate synthesis. Curr Opin Microbiol 13(3):293–300. doi:10.1016/j.mib.2010.03.002
    • (2010) Curr Opin Microbiol , vol.13 , Issue.3 , pp. 293-300
    • Monsan, P.1    Remaud-Simeon, M.2    Andre, I.3
  • 21
    • 84885929452 scopus 로고    scopus 로고
    • Immobilisation procedure and reaction conditions for optimal performance of Candida antarctica lipase B in transesterification and hydrolysis
    • Nordblad M, Adlercreutz P (2013) Immobilisation procedure and reaction conditions for optimal performance of Candida antarctica lipase B in transesterification and hydrolysis. Biocatal Biotransform 31(5):237–245. doi:10.3109/10242422.2013.837240
    • (2013) Biocatal Biotransform , vol.31 , Issue.5 , pp. 237-245
    • Nordblad, M.1    Adlercreutz, P.2
  • 22
    • 0348050009 scopus 로고    scopus 로고
    • Oligosaccharide synthesis by glycosynthases
    • COI: 1:CAS:528:DC%2BD3sXpvFyrsL4%3D, PID: 14690620
    • Perugino G, Trincone A, Rossi M, Moracci M (2004) Oligosaccharide synthesis by glycosynthases. Trends Biotechnol 22(1):31–37. doi:10.1016/j.tibtech.2003.10.008
    • (2004) Trends Biotechnol , vol.22 , Issue.1 , pp. 31-37
    • Perugino, G.1    Trincone, A.2    Rossi, M.3    Moracci, M.4
  • 23
    • 29144449264 scopus 로고    scopus 로고
    • Wax esters produced by solvent-free energy-efficient enzymatic synthesis and their applicability as wood coatings
    • COI: 1:CAS:528:DC%2BD2MXht1ensLfI
    • Petersson AEV, Gustafsson LM, Nordblad M, Borjesson P, Mattiasson B, Adlercreutz P (2005) Wax esters produced by solvent-free energy-efficient enzymatic synthesis and their applicability as wood coatings. Green Chem 7(12):837–843
    • (2005) Green Chem , vol.7 , Issue.12 , pp. 837-843
    • Petersson, A.E.V.1    Gustafsson, L.M.2    Nordblad, M.3    Borjesson, P.4    Mattiasson, B.5    Adlercreutz, P.6
  • 24
    • 0032479388 scopus 로고    scopus 로고
    • Lipases: interfacial enzymes with attractive applications
    • Schmid RD, Verger R (1998) Lipases: interfacial enzymes with attractive applications. Angew Chem Int Ed 37:1608–1633
    • (1998) Angew Chem Int Ed , vol.37 , pp. 1608-1633
    • Schmid, R.D.1    Verger, R.2
  • 26
    • 84883214913 scopus 로고    scopus 로고
    • Conserved water molecules in family 1 glycosidases: a DXMS and molecular dynamics study
    • COI: 1:CAS:528:DC%2BC3sXhtFOgtr7L, PID: 23895259
    • Teze D, Hendrickx J, Dion M, Tellier C, Woods VL Jr, Tran V, Sanejouand Y-H (2013) Conserved water molecules in family 1 glycosidases: a DXMS and molecular dynamics study. Biochemistry 52(34):5900–5910. doi:10.1021/bi400260b
    • (2013) Biochemistry , vol.52 , Issue.34 , pp. 5900-5910
    • Teze, D.1    Hendrickx, J.2    Dion, M.3    Tellier, C.4    Woods, V.L.5    Tran, V.6    Sanejouand, Y.-H.7
  • 27
    • 0026547688 scopus 로고
    • Rhizomucor miehei lipase remains highly active at water activity below 0.0001
    • COI: 1:CAS:528:DyaK38XktVeitbc%3D, PID: 1577162
    • Valivety RH, Halling PJ, Macrae AR (1992a) Rhizomucor miehei lipase remains highly active at water activity below 0.0001. FEBS Lett 301:258–260
    • (1992) FEBS Lett , vol.301 , pp. 258-260
    • Valivety, R.H.1    Halling, P.J.2    Macrae, A.R.3
  • 28
    • 0026635877 scopus 로고
    • Lipases from different sources vary widely in dependence of catalytic activity on water activity
    • COI: 1:CAS:528:DyaK38XlvVOisLc%3D, PID: 1643087
    • Valivety RH, Halling PJ, Peilow AD, Macrae AR (1992b) Lipases from different sources vary widely in dependence of catalytic activity on water activity. Biochim Biophys Acta 1122:143–146
    • (1992) Biochim Biophys Acta , vol.1122 , pp. 143-146
    • Valivety, R.H.1    Halling, P.J.2    Peilow, A.D.3    Macrae, A.R.4
  • 29
    • 0035976993 scopus 로고    scopus 로고
    • Hydrophobic amino acid residues in the acceptor binding site are main determinants for reaction mechanism and specificity of cyclodextrin-glycosyltransferase
    • PID: 11555657
    • van der Veen BA, Leemhuis H, Kralj S, Uitdehaag JCM, Dijkstra BW, Dijkhuizen L (2001) Hydrophobic amino acid residues in the acceptor binding site are main determinants for reaction mechanism and specificity of cyclodextrin-glycosyltransferase. J Biol Chem 276(48):44557–44562. doi:10.1074/jbc.M107533200
    • (2001) J Biol Chem , vol.276 , Issue.48 , pp. 44557-44562
    • van der Veen, B.A.1    Leemhuis, H.2    Kralj, S.3    Uitdehaag, J.C.M.4    Dijkstra, B.W.5    Dijkhuizen, L.6
  • 31
    • 0031554889 scopus 로고    scopus 로고
    • Water activity and substrate concentration effects on lipase activity
    • COI: 1:CAS:528:DyaK2sXkslyhuro%3D, PID: 18636590
    • Wehtje E, Adlercreutz P (1997) Water activity and substrate concentration effects on lipase activity. Biotechnol Bioeng 55(5):798–806
    • (1997) Biotechnol Bioeng , vol.55 , Issue.5 , pp. 798-806
    • Wehtje, E.1    Adlercreutz, P.2
  • 32
    • 0033963529 scopus 로고    scopus 로고
    • Glycosidase mechanisms: anatomy of a finely tuned catalyst
    • COI: 1:CAS:528:DyaK1MXnsFOnsrs%3D, PID: 10639071
    • Zechel DL, Withers SG (2000) Glycosidase mechanisms: anatomy of a finely tuned catalyst. Acc Chem Res 33(1):11–18. doi:10.1021/ar970172+
    • (2000) Acc Chem Res , vol.33 , Issue.1 , pp. 11-18
    • Zechel, D.L.1    Withers, S.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.