메뉴 건너뛰기




Volumn 57, Issue 1-2, 2013, Pages 37-40

Immobilization of lipases from Rhizomucor miehei and Thermomyces lanuginosus by adsorption on variously grafted silica gels

Author keywords

Immobilization; Kinetic resolution; Lipase; Rhizomucor miehei; Silica gel; Surface modification; Thermomyces lanuginosus

Indexed keywords

GRAFTING (CHEMICAL); LIPASES; MESOPOROUS MATERIALS; SURFACE TREATMENT;

EID: 84880411261     PISSN: 03245853     EISSN: 15873765     Source Type: Journal    
DOI: 10.3311/ppch.2168     Document Type: Article
Times cited : (8)

References (18)
  • 2
    • 0036525716 scopus 로고    scopus 로고
    • Lipases as practical biocatalysts
    • DOI 10.1016/S1367-5931(02)00297-1
    • Reetz MT, Lipases as practical biocatalysts, Curr Opin Chem Biol, 6, (2001), 145-150, DOI 10.1016/S1367-5931(02)00297-1.
    • (2001) Curr Opin Chem Biol , vol.6 , pp. 145-150
    • Reetz, M.T.1
  • 5
    • 3142773489 scopus 로고    scopus 로고
    • Bacterial lipases: An overview of production, purification and biochemical properties
    • DOI 10.1007/s00253-004-1568-8
    • Gupta R, Gupta N, Rathi P, Bacterial lipases: an overview of production, purification and biochemical properties, Appl Microbiol Biotechnol, 64, (2004), 763-781, DOI 10.1007/s00253-004-1568-8.
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 763-781
    • Gupta, R.1    Gupta, N.2    Rathi, P.3
  • 6
    • 34547209337 scopus 로고    scopus 로고
    • Enzyme Immobilization: The Quest for Optimum Performance
    • DOI 10.1002/adsc.200700082
    • Sheldon RA, Enzyme Immobilization: The Quest for Optimum Performance, Adv Synth Catal, 349, (2007), 1289-1307, DOI 10.1002/adsc.200700082.
    • (2007) Adv Synth Catal , vol.349 , pp. 1289-1307
    • Sheldon, R.A.1
  • 7
    • 33947602594 scopus 로고    scopus 로고
    • Improvement of enzyme activity, stability and selectivity via immobilization techniques
    • DOI 10.1016/j.enzmictec.2007.01.018
    • Mateo C, Palomo JM, Fernandez-Lorente G, Guisan JM, Fernandez-Lafuente R, Improvement of enzyme activity, stability and selectivity via immobilization techniques, Enzyme Microb Technol, 40, (2007), 1451-1463, DOI 10.1016/j.enzmictec.2007.01.018.
    • (2007) Enzyme Microb Technol , vol.40 , pp. 1451-1463
    • Mateo, C.1    Palomo, J.M.2    Fernandez-Lorente, G.3    Guisan, J.M.4    Fernandez-Lafuente, R.5
  • 8
    • 27844518415 scopus 로고    scopus 로고
    • Nanostructures for enzyme stabilization
    • DOI 10.1016/j.ces.2005.05.067
    • Kim J, Grate JW, Wang P, Nanostructures for enzyme stabilization, Chem Eng Sci, 61, (2006), 1017-1026, DOI 10.1016/j.ces.2005.05.067.
    • (2006) Chem Eng Sci , vol.61 , pp. 1017-1026
    • Kim, J.1    Grate, J.W.2    Wang, P.3
  • 9
    • 33644860341 scopus 로고    scopus 로고
    • Recent bio-applications of sol-gel materials
    • DOI 10.1039/B512706H
    • Avnir D, Coradin T, Lev O, Livage J, Recent bio-applications of sol-gel materials, J Mater Chem, 16, (2006), 1013-1030, DOI 10.1039/B512706H.
    • (2006) J Mater Chem , vol.16 , pp. 1013-1030
    • Avnir, D.1    Coradin, T.2    Lev, O.3    Livage, J.4
  • 11
    • 78650250734 scopus 로고    scopus 로고
    • Fine tuning the second generation sol-gel lipase immobilization with ternary alkoxysilane precursor systems
    • DOI 10.1016/j.procbio.2010.07.02
    • Tomin A, Weiser D, Hellner G, Bata Z, Corici L, Péter F, Koczka B, Poppe L, Fine tuning the second generation sol-gel lipase immobilization with ternary alkoxysilane precursor systems, Proc Biochem, 46, (2011), 52-58, DOI 10.1016/j.procbio.2010.07.02.
    • (2011) Proc Biochem , vol.46 , pp. 52-58
    • Tomin, A.1    Weiser, D.2    Hellner, G.3    Bata, Z.4    Corici, L.5    Péter, F.6    Koczka, B.7    Poppe, L.8
  • 12
    • 84880058423 scopus 로고    scopus 로고
    • Novel hydrophobic silica gels as carriers for lipases-Separation of lipase A and lipase B from Candida antarctica
    • Boros Z, Abaháziova E, Oláh M, Sátorhelyi P, Erdélyi B, Poppe L, Novel hydrophobic silica gels as carriers for lipases-Separation of lipase A and lipase B from Candida antarctica, Chim Oggi/Chem Today, 30, (2012), 28-31.
    • (2012) Chim Oggi/Chem Today , vol.30 , pp. 28-31
    • Boros, Z.1    Abaháziova, E.2    Oláh, M.3    Sátorhelyi, P.4    Erdélyi, B.5    Poppe, L.6
  • 13
    • 84869065871 scopus 로고    scopus 로고
    • How the mode of Candida antarctica lipase B immobilization affects the continuous-flow kinetic resolution of racemic amines at various temperatures
    • DOI 10.1016/j.molcatb.2012.09.004
    • Boros Z, Falus P, Márkus M, Weiser D, Oláh M, Hornyánszky G, Nagy J, Poppe L, How the mode of Candida antarctica lipase B immobilization affects the continuous-flow kinetic resolution of racemic amines at various temperatures, J Mol Catal B Enzym, 85-86, (2012), 119-125, DOI 10.1016/j.molcatb.2012.09.004.
    • (2012) J Mol Catal B Enzym , vol.85-86 , pp. 119-125
    • Boros, Z.1    Falus, P.2    Márkus, M.3    Weiser, D.4    Oláh, M.5    Hornyánszky, G.6    Nagy, J.7    Poppe, L.8
  • 14
    • 84856209683 scopus 로고    scopus 로고
    • Disubstituted dialkoxysilane precursors in binary and ternary sol-gel systems for lipase immobilization
    • DOI 10.1016/j.procbio.2011.11.023
    • Weiser D, Boros Z, Hornyánszky G, Tóth A, Poppe L, Disubstituted dialkoxysilane precursors in binary and ternary sol-gel systems for lipase immobilization, Proc Biochem, 47, (2012), 428-434, DOI 10.1016/j.procbio.2011.11.023.
    • (2012) Proc Biochem , vol.47 , pp. 428-434
    • Weiser, D.1    Boros, Z.2    Hornyánszky, G.3    Tóth, A.4    Poppe, L.5
  • 16
    • 80052794860 scopus 로고    scopus 로고
    • Novel sol-gel lipases by designed bioimprinting for continuous-flow kinetic resolutions
    • DOI 10.1002/adsc.201100329
    • Hellner G, Boros Z, Tomin A, Poppe L, Novel sol-gel lipases by designed bioimprinting for continuous-flow kinetic resolutions, Adv Synth Catal, 353, (2011), 2481-2491, DOI 10.1002/adsc.201100329.
    • (2011) Adv Synth Catal , vol.353 , pp. 2481-2491
    • Hellner, G.1    Boros, Z.2    Tomin, A.3    Poppe, L.4
  • 18
    • 20644469267 scopus 로고
    • Quantitative analyses of biochemical kinetic resolutions of enantiomers
    • DOI 10.1021/ja00389a064
    • Chen CS, Fujimoto Y, Girdaukas G, Sih C J, Quantitative analyses of biochemical kinetic resolutions of enantiomers, J Am Chem Soc, 104, (1982), 7294-7299, DOI 10.1021/ja00389a064.
    • (1982) J Am Chem Soc , vol.104 , pp. 7294-7299
    • Chen, C.S.1    Fujimoto, Y.2    Girdaukas, G.3    Sih, C.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.