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Volumn 46, Issue 8, 2011, Pages 1688-1692

A novel nanoprotein particle synthesis: Nanolipase

Author keywords

Nanolipase; Photosensitive cross linking; Photosensitive microemulsion polymerization; Proteinous polymeric particles

Indexed keywords

ACYLGLYCEROLS; AVERAGE PARTICLE SIZE; CARBOXYLESTERASES; CATALYSE; HYDROLYTIC ACTIVITIES; MICROEMULSION POLYMERIZATION; NANO-STRUCTURED; NANOLIPASE; NOVEL METHODS; PARTICLE SYNTHESIS; PHOTOSENSITIVE CROSS-LINKING; PHOTOSENSITIVE MICROEMULSION POLYMERIZATION; POLYMERIC PARTICLES; REUSABLE CATALYSTS; TRIACYLGLYCEROLS;

EID: 79959978845     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2011.04.011     Document Type: Article
Times cited : (28)

References (30)
  • 1
    • 33646867639 scopus 로고    scopus 로고
    • Lipases: Useful biocatalysts for the preparation of pharmaceuticals
    • DOI 10.1016/j.molcatb.2006.02.010, PII S1381117706000750
    • V. Gotor-Fernández, R. Brieva, and V. Gotor Lipases: useful biocatalysts for the preperation of pharmaceuticals J Mol Catal B: Enzym 40 2006 111 120 (Pubitemid 43783304)
    • (2006) Journal of Molecular Catalysis B: Enzymatic , vol.40 , Issue.3-4 , pp. 111-120
    • Gotor-Fernandez, V.1    Brieva, R.2    Gotor, V.3
  • 2
    • 0035843122 scopus 로고    scopus 로고
    • Enzymes for chemical synthesis
    • DOI 10.1038/35051706
    • K.M. Koeller, and C.H. Wong Enzymes for chemical synthesis Nature 409 2001 232 240 (Pubitemid 32146169)
    • (2001) Nature , vol.409 , Issue.6817 , pp. 232-240
    • Koeller, K.M.1    Wong, C.-H.2
  • 3
    • 0036525716 scopus 로고    scopus 로고
    • Lipases as practical biocatalysts
    • DOI 10.1016/S1367-5931(02)00297-1, PII S1367593102002971
    • M.T. Reetz Lipases as practical biocatalysts Curr Opin Chem Biol 6 2002 145 150 (Pubitemid 34251368)
    • (2002) Current Opinion in Chemical Biology , vol.6 , Issue.2 , pp. 145-150
    • Reetz, M.T.1
  • 4
    • 38949099381 scopus 로고    scopus 로고
    • Glutaraldehyde activation of polymer Nylon-6 for lipase immobilization: Enzyme characteristics and stability
    • DOI 10.1016/j.biortech.2007.04.042, PII S096085240700380X
    • S. Pahujani, S.S. Kanwar, G. Chauhan, and R. Gupta Glutaraldehyde activation of polymer Nylon-6 for lipase immobilization: enzyme characteristics and stability Bioresour Technol 99 2008 2566 2570 (Pubitemid 351217048)
    • (2008) Bioresource Technology , vol.99 , Issue.7 , pp. 2566-2570
    • Pahujani, S.1    Kanwar, S.S.2    Chauhan, G.3    Gupta, R.4
  • 5
    • 33751100404 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates (CLEAs) with controlled particles: Application to Candida rugosa lipase
    • DOI 10.1016/j.molcatb.2006.07.001, PII S1381117706002141
    • H.W. Yu, H. Chen, X. Wang, Y.Y. Yang, and C.B. Ching Cross-linked enzyme aggregates (CLEAs) with controlled particles: application to Candida rugosa lipase J Mol Catal B: Enzym 43 2006 124 127 (Pubitemid 44767836)
    • (2006) Journal of Molecular Catalysis B: Enzymatic , vol.43 , Issue.1-4 , pp. 124-127
    • Yu, H.W.1    Chen, H.2    Wang, X.3    Yang, Y.Y.4    Ching, C.B.5
  • 6
    • 34548133013 scopus 로고    scopus 로고
    • Adsorption and activity of lipase from Candida rugosa on the chitosan-modified poly(acrylonitrile-co-maleic acid) membrane surface
    • DOI 10.1016/j.colsurfb.2007.05.022, PII S0927776507002214
    • P. Ye, J. Jiang, and Z.K. Xu Adsorption and activity of lipase from Candida rugosa on the chitosan-modified poly(acrylonitrile-co-maleic acid) membrane surface Colloids Surf B: Biointerface 60 2007 62 67 (Pubitemid 47302295)
    • (2007) Colloids and Surfaces B: Biointerfaces , vol.60 , Issue.1 , pp. 62-67
    • Ye, P.1    Jiang, J.2    Xu, Z.-K.3
  • 7
    • 0001824363 scopus 로고    scopus 로고
    • A Novel Method for Enzyme Immobilization: Direct Encapsulation of Acid Phosphatase in Nanoporous Silica Host Materials
    • DOI 10.1166/jnn.2001.014
    • Y. Wei, J. Xu, Q. Feng, M. Lin, H. Dong, and W.-J. Zhang A novel method for enzyme immobilization: direct encapsulation of acid phosphatase in nanoporous silica host materials J Nanosci Nanotechnol 1 2001 83 93 (Pubitemid 33689634)
    • (2001) Journal of Nanoscience and Nanotechnology , vol.1 , Issue.1 , pp. 83-93
    • Wei, Y.1    Xu, J.2    Feng, Q.3    Lin, M.4    Dong, H.5    Zhang, W.-J.6    Wang, C.7
  • 8
    • 10944220573 scopus 로고    scopus 로고
    • Immobilized Pseudomonas cepacia lipase for biodiesel fuel production from soybean oil
    • DOI 10.1016/j.biortech.2004.05.029, PII S0960852404002779
    • H. Noureddini, X. Gao, and R.S. Philkana Immobilized Pseudomonas cepacia lipase for biodiesel fuel production from soybean oil Bioresour Technol 96 2005 769 777 (Pubitemid 40017778)
    • (2005) Bioresource Technology , vol.96 , Issue.7 , pp. 769-777
    • Noureddini, H.1    Gao, X.2    Philkana, R.S.3
  • 9
    • 2442590857 scopus 로고    scopus 로고
    • Influence of the sol-gel chemistry on the activity of a lipase encapsulated in a silica aerogel
    • DOI 10.1016/j.molcatb.2003.12.015, PII S1381117704000487
    • S. Maury, P. Buisson, A. Perrard, and A.C. Pierre Influence of the sol-gel chemistry on the activity of a lipase encapsulated in a silica aerogel J Mol Catal B: Enzym 29 2004 133 148 (Pubitemid 38624083)
    • (2004) Journal of Molecular Catalysis B: Enzymatic , vol.29 , Issue.1-6 , pp. 133-148
    • Maury, S.1    Buisson, P.2    Perrard, A.3    Pierre, A.C.4
  • 10
    • 0028939393 scopus 로고    scopus 로고
    • Expand + interfacial activation-based molecular bioimprinting of lipolytic enzymes
    • I. Mingarro, C. Abad, and L. Braco Expand + interfacial activation-based molecular bioimprinting of lipolytic enzymes Proc Natl Acad Sci USA 92 2005 3308 3312
    • (2005) Proc Natl Acad Sci USA , vol.92 , pp. 3308-3312
    • Mingarro, I.1    Abad, C.2    Braco, L.3
  • 11
    • 58149252235 scopus 로고    scopus 로고
    • Improving esterification activity of Burkholderia cepacia lipase encapsulated in silica by bioimprinting with substrate analogues
    • X. Cao, J. Yang, L. Shu, B. Yu, and Y. Yan Improving esterification activity of Burkholderia cepacia lipase encapsulated in silica by bioimprinting with substrate analogues Process Biochem 44 2009 177 182
    • (2009) Process Biochem , vol.44 , pp. 177-182
    • Cao, X.1    Yang, J.2    Shu, L.3    Yu, B.4    Yan, Y.5
  • 13
    • 0034099693 scopus 로고    scopus 로고
    • Entrapment of lipases in hydrophobic sol-gel-materials: Efficient heterogeneous biocatalysts in aqueous medium
    • M.T. Reetz, R. Wenkel, and D. Avnir Entrapment of lipases in hydrophobic sol-gel-materials: efficient heterogeneous biocatalysts in aqueous medium Synthesis 6 2000 781 783 (Pubitemid 30407577)
    • (2000) Synthesis , Issue.6 , pp. 781-783
    • Reetz, M.T.1    Wenkel, R.2    Avnir, D.3
  • 14
    • 0030569931 scopus 로고    scopus 로고
    • Efficient immobilization of lipases by entrapment in hydrophobic sol-gel materials
    • DOI 10.1002/(SICI)1097-0290(19960305)49:5<527::AID-BIT5>3.0.CO;2-L
    • M.T. Reetz, A. Zonta, and J. Simpelkamp Efficient immobilization of lipases by entrapment in hydrophobic sol-gel materials Biotechnol Bioeng 49 1996 527 534 (Pubitemid 26062610)
    • (1996) Biotechnology and Bioengineering , vol.49 , Issue.5 , pp. 527-534
    • Reetz, M.T.1    Zonta, A.2    Simpelkamp, J.3
  • 15
    • 0035963691 scopus 로고    scopus 로고
    • Enantioselective Aminolysis of an α-Chloroester Catalyzed by Candida cylindracea Lipase Encapsulated in Sol-Gel Silica Glass
    • DOI 10.1021/ol015989o
    • J.D. Banjic, E.N. Kadnikova, and N.M. Kostic Enantioselective aminolysis of an α-chloroester catalyzed by candida cylindracea lipase encapsulated in sol-gel silica glass Org Lett 13 2001 2025 2028 (Pubitemid 33631705)
    • (2001) Organic Letters , vol.3 , Issue.13 , pp. 2025-2028
    • Badjic, J.D.1    Kadnikova, E.N.2    Kostic, N.M.3
  • 16
    • 0035817408 scopus 로고    scopus 로고
    • Enzyme stabilization by covalent binding in nanoporous sol-gel glass for nonaqueous biocatalysis
    • DOI 10.1002/bit.1114
    • P. Wang, S. Dai, S.D. Waeszada, A.Y. Tsao, and B.H. Davison Enzyme stabilization by covalent binding in nanoporous sol-gel glass for nonaqueous biocatalysis Biotechnol Bioeng 74 2001 249 255 (Pubitemid 32685696)
    • (2001) Biotechnology and Bioengineering , vol.74 , Issue.3 , pp. 249-255
    • Wang, P.1    Dai, S.2    Waezsada, S.D.3    Tsao, A.Y.4    Davison, B.H.5
  • 17
    • 33747840618 scopus 로고    scopus 로고
    • Polymer conjugates as anticancer nanomedicines
    • DOI 10.1038/nrc1958, PII NRC1958
    • R. Duncan Polymer conjugates as anticancer nanomedicines Nat Rev Cancer 6 2006 688 701 (Pubitemid 44286001)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.9 , pp. 688-701
    • Duncan, R.1
  • 18
    • 34250211933 scopus 로고    scopus 로고
    • Well-defined protein-polymer conjugates - Synthesis and potential applications
    • DOI 10.1007/s00253-006-0574-4
    • P. Thordarson, B.L. Droumaguet, and K. Velonia Well-defined protein-polymer conjugates-synthesis and potential applications Appl Microbiol Biotechnol 73 2006 243 254 (Pubitemid 350262602)
    • (2006) Applied Microbiology and Biotechnology , vol.73 , Issue.2 , pp. 243-254
    • Thordarson, P.1    Le Droumaguet, B.2    Velonia, K.3
  • 19
    • 51549092094 scopus 로고    scopus 로고
    • The impact of PEGylation on biological therapies
    • F.M. Veronese, and A. Mero The impact of PEGylation on biological therapies Biodrugs 22 2008 315 329
    • (2008) Biodrugs , vol.22 , pp. 315-329
    • Veronese, F.M.1    Mero, A.2
  • 20
    • 42949093817 scopus 로고    scopus 로고
    • Effect of PEG molecular weight and linking chemistry on the biological activity and thermal stability of PEGylated trypsin
    • DOI 10.1016/j.ijpharm.2008.01.016, PII S0378517308000379
    • B. Treetharnmathurot, C. Ovartlarnporn, J. Wungsintaweekul, R. Duncan, and R. Wiwattanapatapee Effect of PEG molecular weight and linking chemistry on the biological activity and thermal stability of PEGylated trypsin Int J Pharm 357 2008 252 259 (Pubitemid 351614974)
    • (2008) International Journal of Pharmaceutics , vol.357 , Issue.1-2 , pp. 252-259
    • Treetharnmathurot, B.1    Ovartlarnporn, C.2    Wungsintaweekul, J.3    Duncan, R.4    Wiwattanapatapee, R.5
  • 21
    • 77950914419 scopus 로고    scopus 로고
    • Nano-encapsulation of lipase by self-assembled nanogels: Induction of high enzyme activity and thermal stabilization
    • S. Sawada, and K. Akiyoshi Nano-encapsulation of lipase by self-assembled nanogels: induction of high enzyme activity and thermal stabilization Macromol Biosci 10 2010 353 358
    • (2010) Macromol Biosci , vol.10 , pp. 353-358
    • Sawada, S.1    Akiyoshi, K.2
  • 22
    • 0033987939 scopus 로고    scopus 로고
    • Protein stability in controlled-release systems
    • DOI 10.1038/71875
    • K. Fu, A.M. Klibanov, and R. Langer Protein stability in controlled-release systems Nat Biotechnol 18 2000 24 25 (Pubitemid 30041164)
    • (2000) Nature Biotechnology , vol.18 , Issue.1 , pp. 24-25
    • Fu, K.1    Klibanov, A.M.2    Langer, R.3
  • 23
    • 23744448576 scopus 로고    scopus 로고
    • Characterization of stable lysozyme-entrapped polyion complex (PIC) micelles with crosslinked core by glutaraldehyde
    • DOI 10.1016/j.polymer.2005.02.121, PII S0032386105004908, Stimuli Responsive Polymers
    • X. Yuan, Y. Yamasaki, A. Harada, and K. Kataoka Characterization of stable lysozyme-entrapped polyion complex (PIC) micelles with crosslinked core by glutaraldehyde Polymer 46 2005 7749 7758 (Pubitemid 41125236)
    • (2005) Polymer , vol.46 , Issue.18 , pp. 7749-7758
    • Yuan, X.1    Yamasaki, Y.2    Harada, A.3    Kataoka, K.4
  • 24
    • 84988203488 scopus 로고
    • Polymerization in microemulsions - A new approach to ultrafine, highly functionalized polymer dispersions
    • M. Antonietti, R. Basten, and S. Lohmann Polymerization in microemulsions - a new approach to ultrafine, highly functionalized polymer dispersions Macromol Chem Phys 196 1995 441 466
    • (1995) Macromol Chem Phys , vol.196 , pp. 441-466
    • Antonietti, M.1    Basten, R.2    Lohmann, S.3
  • 26
    • 18144424793 scopus 로고    scopus 로고
    • Kinetics modeling of microemulsion copolymerization
    • V.M. Ovando Kinetics modeling of microemulsion copolymerization Polymer Bull 54 2005 129 140
    • (2005) Polymer Bull , vol.54 , pp. 129-140
    • Ovando, V.M.1
  • 29
    • 17844387710 scopus 로고
    • Dichlorotetrakis(dimethyl sulphoxide) ruthenium(II) and its use as a source material for some new ruthenium(II) complexes
    • I.P. Evans, G. Spencer, and G. Wilkinson Dichlorotetrakis(dimethyl sulphoxide) ruthenium(II) and its use as a source material for some new ruthenium(II) complexes J Chem Soc Dalton Trans 2 1973 204 209
    • (1973) J Chem Soc Dalton Trans , vol.2 , pp. 204-209
    • Evans, I.P.1    Spencer, G.2    Wilkinson, G.3
  • 30
    • 84942966183 scopus 로고
    • The effect of pH and temperature on the stability and enzymatic activity of prostatic acid phosphatase. Studies on the optimization of a continuous monitored determination of acid phosphatase, II
    • G. Gundlach, and E. Luttermann-Semmer The effect of pH and temperature on the stability and enzymatic activity of prostatic acid phosphatase. Studies on the optimization of a continuous monitored determination of acid phosphatase, II J Clin Chem Clin Biochem 7 1987 441 446 (Pubitemid 17101057)
    • (1987) Journal of Clinical Chemistry and Clinical Biochemistry , vol.25 , Issue.7 , pp. 441-446
    • Gundlach, G.1    Luttermann-Semmer, E.2


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