메뉴 건너뛰기




Volumn 48, Issue 8, 2013, Pages 1181-1187

Thermostabilization of Candida antarctica lipase B by double immobilization: Adsorption on a macroporous polyacrylate carrier and R1 silaffin-mediated biosilicification

Author keywords

Biosilicification; Candida antarctica lipase B; Immobilization; R1 peptide; Silaffin; Thermostability

Indexed keywords

BIOSILICIFICATION; CANDIDA ANTARCTICA LIPASE B; INDUSTRIAL ENZYMES; PHYSICAL ADSORPTION; PROTEIN ENGINEERING; SILAFFIN; THERMOSTABILITY; THERMOSTABILIZATION;

EID: 84881132106     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2013.06.010     Document Type: Article
Times cited : (19)

References (38)
  • 3
    • 35448955322 scopus 로고    scopus 로고
    • Lipase-catalyzed synthesis of glycerol carbonate from renewable glycerol and dimethyl carbonate through transesterification
    • S.C. Kim, Y.H. Kim, H. Lee, D.Y. Yoon, and B.K. Song Lipase-catalyzed synthesis of glycerol carbonate from renewable glycerol and dimethyl carbonate through transesterification Journal of Molecular Catalysis B: Enzymatic 49 2007 75 78
    • (2007) Journal of Molecular Catalysis B: Enzymatic , vol.49 , pp. 75-78
    • Kim, S.C.1    Kim, Y.H.2    Lee, H.3    Yoon, D.Y.4    Song, B.K.5
  • 4
    • 0142011500 scopus 로고    scopus 로고
    • Measurement of the temperature dependent viscosity of biodiesel fuels
    • S. Kerschbaum, and G. Rinke Measurement of the temperature dependent viscosity of biodiesel fuels Fuel 83 2004 287 291
    • (2004) Fuel , vol.83 , pp. 287-291
    • Kerschbaum, S.1    Rinke, G.2
  • 5
    • 0032165861 scopus 로고    scopus 로고
    • Production of specific-structured triacylglycerols by lipase-catalyzed interesterification in a laboratory-scale continuous reactor
    • H. Mu, X. Xu, and C.E. Høy Production of specific-structured triacylglycerols by lipase-catalyzed interesterification in a laboratory-scale continuous reactor Journal of the American Oil Chemists' Society 75 1998 1187 1193
    • (1998) Journal of the American Oil Chemists' Society , vol.75 , pp. 1187-1193
    • Mu, H.1    Xu, X.2    Høy, C.E.3
  • 6
    • 78650678219 scopus 로고    scopus 로고
    • Thermostabilization of Bacillus circulans xylanase: Computational optimization of unstable residues based on thermal fluctuation analysis
    • J.C. Joo, S.P. Pack, Y.H. Kim, and Y.J. Yoo Thermostabilization of Bacillus circulans xylanase: computational optimization of unstable residues based on thermal fluctuation analysis Journal of Biotechnology 151 2011 56 65
    • (2011) Journal of Biotechnology , vol.151 , pp. 56-65
    • Joo, J.C.1    Pack, S.P.2    Kim, Y.H.3    Yoo, Y.J.4
  • 7
    • 77957131531 scopus 로고    scopus 로고
    • The development of a thermostable CiP (Coprinus cinereus peroxidase) through in silico design
    • S.J. Kim, J.A. Lee, J.C. Joo, Y.J. Yoo, Y.H. Kim, and B.K. Song The development of a thermostable CiP (Coprinus cinereus peroxidase) through in silico design Biotechnology Progress 26 2010 1038 1046
    • (2010) Biotechnology Progress , vol.26 , pp. 1038-1046
    • Kim, S.J.1    Lee, J.A.2    Joo, J.C.3    Yoo, Y.J.4    Kim, Y.H.5    Song, B.K.6
  • 8
    • 79958011043 scopus 로고    scopus 로고
    • Utilizing natural diversity to evolve protein function: Applications towards thermostability
    • M.F. Cole, and E.A. Gaucher Utilizing natural diversity to evolve protein function: applications towards thermostability Current Opinion in Chemical Biology 15 2011 399 406
    • (2011) Current Opinion in Chemical Biology , vol.15 , pp. 399-406
    • Cole, M.F.1    Gaucher, E.A.2
  • 10
    • 77249085574 scopus 로고    scopus 로고
    • Thermostabilization of Bacillus circulans xylanase via computational design of a flexible surface cavity
    • J.C. Joo, S. Pohkrel, S.P. Pack, and Y.J. Yoo Thermostabilization of Bacillus circulans xylanase via computational design of a flexible surface cavity Journal of Biotechnology 146 2010 31 39
    • (2010) Journal of Biotechnology , vol.146 , pp. 31-39
    • Joo, J.C.1    Pohkrel, S.2    Pack, S.P.3    Yoo, Y.J.4
  • 12
    • 79959407879 scopus 로고    scopus 로고
    • Rational redesign of Candida antarctica lipase B for the ring opening polymerization of d,d-lactide
    • M. Takwa, M.W. Larsen, K. Hult, and M. Martinelle Rational redesign of Candida antarctica lipase B for the ring opening polymerization of d,d-lactide Chemical Communications 47 2011 7392 7394
    • (2011) Chemical Communications , vol.47 , pp. 7392-7394
    • Takwa, M.1    Larsen, M.W.2    Hult, K.3    Martinelle, M.4
  • 13
    • 20444448921 scopus 로고    scopus 로고
    • Creating space for large secondary alcohols by rational redesign of Candida antarctica lipase B
    • A.O. Magnusson, J.C. Rotticci-Mulder, A. Santagostino, and K. Hult Creating space for large secondary alcohols by rational redesign of Candida antarctica lipase B ChemBioChem 6 2005 1051 1056
    • (2005) ChemBioChem , vol.6 , pp. 1051-1056
    • Magnusson, A.O.1    Rotticci-Mulder, J.C.2    Santagostino, A.3    Hult, K.4
  • 14
    • 77953621626 scopus 로고    scopus 로고
    • Development of thermostable lipase B from Candida antarctica (CalB) through in silico design employing B-factor and RosettaDesign
    • H.S. Kim, Q.A.T. Le, and Y.H. Kim Development of thermostable lipase B from Candida antarctica (CalB) through in silico design employing B-factor and RosettaDesign Enzyme and Microbial Technology 47 2010 1 5
    • (2010) Enzyme and Microbial Technology , vol.47 , pp. 1-5
    • Kim, H.S.1    Le, Q.A.T.2    Kim, Y.H.3
  • 16
    • 0141817121 scopus 로고    scopus 로고
    • Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution
    • N. Zhang, W.C. Suen, W. Windsor, L. Xiao, V. Madison, and A. Zaks Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution Protein Engineering 16 2003 599 605
    • (2003) Protein Engineering , vol.16 , pp. 599-605
    • Zhang, N.1    Suen, W.C.2    Windsor, W.3    Xiao, L.4    Madison, V.5    Zaks, A.6
  • 19
    • 0034237721 scopus 로고    scopus 로고
    • Bioencapsulation within synthetic polymers. Part 1. Sol-gel encapsulated biologicals
    • I. Gill, and A. Ballesteros Bioencapsulation within synthetic polymers. Part 1. Sol-gel encapsulated biologicals Trends in Biotechnology 18 2000 282 296
    • (2000) Trends in Biotechnology , vol.18 , pp. 282-296
    • Gill, I.1    Ballesteros, A.2
  • 20
    • 34249678567 scopus 로고    scopus 로고
    • Silica immobilization of an enzyme through genetic engineering of the diatom Thalassiosira pseudonana
    • N. Poulsen, C. Berne, J. Spain, and N. Kröger Silica immobilization of an enzyme through genetic engineering of the diatom Thalassiosira pseudonana Angewandte Chemie - International Edition 46 2007 1843 1846
    • (2007) Angewandte Chemie - International Edition , vol.46 , pp. 1843-1846
    • Poulsen, N.1    Berne, C.2    Spain, J.3    Kröger, N.4
  • 21
    • 4043074831 scopus 로고    scopus 로고
    • Silica formation in diatoms: The function of long-chain polyamines and silaffins
    • M. Sumper, and N. Kröger Silica formation in diatoms: the function of long-chain polyamines and silaffins Journal of Materials Chemistry 14 2004 2059 2065
    • (2004) Journal of Materials Chemistry , vol.14 , pp. 2059-2065
    • Sumper, M.1    Kröger, N.2
  • 22
    • 73249121302 scopus 로고    scopus 로고
    • A novel route for immobilization of proteins to silica particles incorporating silaffin domains
    • D.H. Nam, K. Won, Y.H. Kim, and B.I. Sang A novel route for immobilization of proteins to silica particles incorporating silaffin domains Biotechnology Progress 25 2009 1643 1649
    • (2009) Biotechnology Progress , vol.25 , pp. 1643-1649
    • Nam, D.H.1    Won, K.2    Kim, Y.H.3    Sang, B.I.4
  • 23
    • 0347915684 scopus 로고    scopus 로고
    • High efficiency transformation by electroporation of Pichia pastoris pretreated with lithium acetate and dithiothreitol
    • S. Wu, and G.J. Letchworth High efficiency transformation by electroporation of Pichia pastoris pretreated with lithium acetate and dithiothreitol BioTechniques 36 2004 152 154
    • (2004) BioTechniques , vol.36 , pp. 152-154
    • Wu, S.1    Letchworth, G.J.2
  • 24
    • 1442264832 scopus 로고    scopus 로고
    • Expression of the GM2-activator protein in the methylotrophic yeast Pichia pastoris, purification, isotopic labeling, and biophysical characterization
    • M. Wendeler, J. Hoernschemeyer, M. John, N. Werth, M. Schoeniger, and T. Lemm Expression of the GM2-activator protein in the methylotrophic yeast Pichia pastoris, purification, isotopic labeling, and biophysical characterization Protein Expression and Purification 34 2004 147 157
    • (2004) Protein Expression and Purification , vol.34 , pp. 147-157
    • Wendeler, M.1    Hoernschemeyer, J.2    John, M.3    Werth, N.4    Schoeniger, M.5    Lemm, T.6
  • 25
    • 66149185690 scopus 로고    scopus 로고
    • Enzyme immobilization via silaffin-mediated autoencapsulation in a biosilica support
    • W.D. Marner Ii, A.S. Shaikh, S.J. Muller, and J.D. Keasling Enzyme immobilization via silaffin-mediated autoencapsulation in a biosilica support Biotechnology Progress 25 2009 417 423
    • (2009) Biotechnology Progress , vol.25 , pp. 417-423
    • Marner Ii, W.D.1    Shaikh, A.S.2    Muller, S.J.3    Keasling, J.D.4
  • 26
    • 34247637888 scopus 로고    scopus 로고
    • Improving biocatalytic activity of enzyme-loaded nanofibers by dispersing entangled nanofiber structure
    • S. Nair, J. Kim, B. Crawford, and S.H. Kim Improving biocatalytic activity of enzyme-loaded nanofibers by dispersing entangled nanofiber structure Biomacromolecules 8 2007 1266 1270
    • (2007) Biomacromolecules , vol.8 , pp. 1266-1270
    • Nair, S.1    Kim, J.2    Crawford, B.3    Kim, S.H.4
  • 29
    • 0037687640 scopus 로고    scopus 로고
    • Imaging the distribution and secondary structure of immobilized enzymes using infrared microspectroscopy
    • Y. Mei, L. Miller, W. Gao, and R.A. Gross Imaging the distribution and secondary structure of immobilized enzymes using infrared microspectroscopy Biomacromolecules 4 2003 70 74
    • (2003) Biomacromolecules , vol.4 , pp. 70-74
    • Mei, Y.1    Miller, L.2    Gao, W.3    Gross, R.A.4
  • 30
    • 79953903057 scopus 로고    scopus 로고
    • Development of an amphiphilic matrix for immobilization of Candida antartica lipase B for biodiesel production
    • K. Lee, K. Min, K. Park, and Y. Yoo Development of an amphiphilic matrix for immobilization of Candida antartica lipase B for biodiesel production Biotechnology and Bioprocess Engineering 15 2010 603 607
    • (2010) Biotechnology and Bioprocess Engineering , vol.15 , pp. 603-607
    • Lee, K.1    Min, K.2    Park, K.3    Yoo, Y.4
  • 32
    • 84857385217 scopus 로고    scopus 로고
    • Enhancing the thermal robustness of an enzyme by directed evolution: Least favorable starting points and inferior mutants can map superior evolutionary pathways
    • Y. Gumulya, and M.T. Reetz Enhancing the thermal robustness of an enzyme by directed evolution: least favorable starting points and inferior mutants can map superior evolutionary pathways ChemBioChem 12 2011 2502 2510
    • (2011) ChemBioChem , vol.12 , pp. 2502-2510
    • Gumulya, Y.1    Reetz, M.T.2
  • 33
    • 84857440017 scopus 로고    scopus 로고
    • Development of thermostable Candida antarctica lipase B through novel in silico design of disulfide bridge
    • Q.A.T. Le, J.C. Joo, Y.J. Yoo, and Y.H. Kim Development of thermostable Candida antarctica lipase B through novel in silico design of disulfide bridge Biotechnology and Bioengineering 109 2012 867 876
    • (2012) Biotechnology and Bioengineering , vol.109 , pp. 867-876
    • Le, Q.A.T.1    Joo, J.C.2    Yoo, Y.J.3    Kim, Y.H.4
  • 34
  • 36
    • 84861899828 scopus 로고    scopus 로고
    • Versatility of glutaraldehyde to immobilize lipases: Effect of the immobilization protocol on the properties of lipase B from Candida antarctica
    • O. Barbosa, R. Torres, C. Ortiz, and R. Fernandez-Lafuente Versatility of glutaraldehyde to immobilize lipases: effect of the immobilization protocol on the properties of lipase B from Candida antarctica Process Biochemistry 47 2012 1220 1227
    • (2012) Process Biochemistry , vol.47 , pp. 1220-1227
    • Barbosa, O.1    Torres, R.2    Ortiz, C.3    Fernandez-Lafuente, R.4
  • 37
    • 39749162076 scopus 로고    scopus 로고
    • Candida antarctica lipase B chemically immobilized on epoxy-activated micro- and nanobeads: Catalysts for polyester synthesis
    • B. Chen, J. Hu, E.M. Miller, W. Xie, M. Cai, and R.A. Gross Candida antarctica lipase B chemically immobilized on epoxy-activated micro- and nanobeads: catalysts for polyester synthesis Biomacromolecules 9 2008 463 471
    • (2008) Biomacromolecules , vol.9 , pp. 463-471
    • Chen, B.1    Hu, J.2    Miller, E.M.3    Xie, W.4    Cai, M.5    Gross, R.A.6
  • 38
    • 34548838013 scopus 로고    scopus 로고
    • Biomimetic synthesis of lysozyme - Silica hybrid hollow particles using sonochemical treatment: Influence of pH and lysozyme a concentration on morphology
    • T. Shiomi, T. Tsunoda, A. Kawai, F. Mizukami, and K. Sakaguchi Biomimetic synthesis of lysozyme - silica hybrid hollow particles using sonochemical treatment: influence of pH and lysozyme a concentration on morphology Chemistry of Materials 19 2007 4486 4493
    • (2007) Chemistry of Materials , vol.19 , pp. 4486-4493
    • Shiomi, T.1    Tsunoda, T.2    Kawai, A.3    Mizukami, F.4    Sakaguchi, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.