메뉴 건너뛰기




Volumn 169, Issue 2, 2013, Pages 351-358

Improved thermostability of lipase b from candida antarctica by directed evolution and display on yeast surface

Author keywords

Candida antarctica lipase B; Multi site saturation mutagenesis; Thermostability; Yeast cell surface display

Indexed keywords

AMINO ACID SUBSTITUTION; AQUEOUS SYSTEM; CANDIDA ANTARCTICA LIPASE B; DIRECTED EVOLUTION; LIPASE B FROM CANDIDA ANTARCTICA; MULTI-SITE; RESIDUAL ACTIVITY; SATURATION MUTAGENESIS; SURFACE DISPLAYS; SURFACE DOMAINS; THERMOSTABILITY; YEAST CELL SURFACE;

EID: 84873080431     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-012-9954-7     Document Type: Article
Times cited : (30)

References (13)
  • 1
    • 50049086082 scopus 로고    scopus 로고
    • Activation of immobilized lipase in non-aqueous systems by hydrophobic poly-DL-tryptophan tethers
    • 10.1002/bit.21870
    • Karl, F.; Schilke, & Kelly, C. (2008). Activation of immobilized lipase in non-aqueous systems by hydrophobic poly-DL-tryptophan tethers. Biotech and Bioeng, 101(1), 9-18.
    • (2008) Biotech and Bioeng , vol.101 , Issue.1 , pp. 9-18
    • Karl, F.1    Schilke2    Kelly, C.3
  • 2
    • 0141817121 scopus 로고    scopus 로고
    • Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution
    • 10.1093/protein/gzg074 1:CAS:528:DC%2BD3sXnt1Kis70%3D
    • Zhang, N.; Suen, W. C.; Windsor, W.; Xiao, L.; Madison, V.; & Zaks, A. (2003). Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution. Protein Engineering, 16(8), 599-605.
    • (2003) Protein Engineering , vol.16 , Issue.8 , pp. 599-605
    • Zhang, N.1    Suen, W.C.2    Windsor, W.3    Xiao, L.4    Madison, V.5    Zaks, A.6
  • 4
    • 33747518326 scopus 로고    scopus 로고
    • Industrial applications of microbial lipases
    • 10.1016/j.enzmictec.2005.10.016 1:CAS:528:DC%2BD28XkslSksbc%3D
    • Hasan, F.; Ali, S. A.; & Hameed, A. (2006). Industrial applications of microbial lipases. Enzyme and Microbial Technology, 39(2), 235-251.
    • (2006) Enzyme and Microbial Technology , vol.39 , Issue.2 , pp. 235-251
    • Hasan, F.1    Ali, S.A.2    Hameed, A.3
  • 5
    • 0035903602 scopus 로고    scopus 로고
    • Investigating and engineering enzymes by genetic selection
    • 10.1002/1521-3773(20010917)40:18<3310: AID-ANIE3310>3.0.CO;2-P
    • Taylor, S. V.; Kast, P.; & Hilvert, D. (2001). Investigating and engineering enzymes by genetic selection. Angewandte Chemie (International Ed. in English), 40(18), 3310-3335.
    • (2001) Angewandte Chemie (International Ed. in English) , vol.40 , Issue.18 , pp. 3310-3335
    • Taylor, S.V.1    Kast, P.2    Hilvert, D.3
  • 7
    • 29144503012 scopus 로고    scopus 로고
    • A statistical analysis of random mutagenesis methods used for directed protein evolution
    • 10.1016/j.jmb.2005.10.082 1:CAS:528:DC%2BD2MXhtlCrt73K
    • Wong, T. S.; Roccatano, D.; Zacharias, M.; & Schwaneberg, U. (2006). A statistical analysis of random mutagenesis methods used for directed protein evolution. Journal of Molecular Biology, 355(4), 858-871.
    • (2006) Journal of Molecular Biology , vol.355 , Issue.4 , pp. 858-871
    • Wong, T.S.1    Roccatano, D.2    Zacharias, M.3    Schwaneberg, U.4
  • 8
    • 34248567845 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes
    • 10.1038/nprot.2007.72 1:CAS:528:DC%2BD2sXhtFGnur%2FP
    • Reetz, M. T.; & Carballeira, J. D. (2007). Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes. Nature protocols, 2(4), 891-903.
    • (2007) Nature Protocols , vol.2 , Issue.4 , pp. 891-903
    • Reetz, M.T.1    Carballeira, J.D.2
  • 9
    • 77952890040 scopus 로고    scopus 로고
    • Display of Candida antarctica lipase B on Pichia pastoris and its application to flavor ester synthesis
    • 10.1007/s00253-009-2382-0
    • Guo-dong, S.; Huang, D.-f.; Han, S.-y.; Zheng, S.-p.; & Ying, L. (2010). Display of Candida antarctica lipase B on Pichia pastoris and its application to flavor ester synthesis. Applied Microbiology and Biotechnology, 86(5), 1493-1501.
    • (2010) Applied Microbiology and Biotechnology , vol.86 , Issue.5 , pp. 1493-1501
    • Guo-Dong, S.1    Huang, D.-F.2    Han, S.-Y.3    Zheng, S.-P.4    Ying, L.5
  • 10
    • 0028773288 scopus 로고
    • The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica
    • 10.1016/S0969-2126(00)00031-9 1:CAS:528:DyaK2MXhslyktg%3D%3D
    • Uppenberg, J.; Hansen, M. T.; Patkar, S.; & Jones, T. A. (1994). The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Structure, 2(4), 293-308.
    • (1994) Structure , vol.2 , Issue.4 , pp. 293-308
    • Uppenberg, J.1    Hansen, M.T.2    Patkar, S.3    Jones, T.A.4
  • 11
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • 10.1107/S0021889892009944 1:CAS:528:DyaK3sXit12lurY%3D
    • Laskowski, R. A.; Macarthur, M. W.; Moss, D. S.; & Thornton, J. M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. Journal of Applied Crystallography, 26(2), 283-291.
    • (1993) Journal of Applied Crystallography , vol.26 , Issue.2 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 12
    • 84857440017 scopus 로고    scopus 로고
    • Development of thermostable Candida antarctica lipase B through novel in silico design of disulfide bridge
    • 10.1002/bit.24371 1:CAS:528:DC%2BC3MXhsFSisL3F
    • Le, Q. A.; Joo, J. C.; Yoo, Y. J.; & Kim, Y. H. (2012). Development of thermostable Candida antarctica lipase B through novel in silico design of disulfide bridge. Biotechnology and Bioengineering, 109(4), 867-876.
    • (2012) Biotechnology and Bioengineering , vol.109 , Issue.4 , pp. 867-876
    • Le, Q.A.1    Joo, J.C.2    Yoo, Y.J.3    Kim, Y.H.4
  • 13
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • 10.1093/protein/13.3.179 1:CAS:528:DC%2BD3cXjtlKmur8%3D
    • Kumar, S.; Tsai, C. J.; & Nussinov, R. (2000). Factors enhancing protein thermostability. Protein Engineering, 13(3), 179-191.
    • (2000) Protein Engineering , vol.13 , Issue.3 , pp. 179-191
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.