Functional fusion mutant of Candida antarctica lipase B (CalB) expressed in Escherichia coli

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 3, 2009, Pages 519-525

  Seo, Hyuk Seong ^a   Kim, Seong Eun ^a   Han, Kyung Yeon ^a   Park, Jin Seung ^a   Kim, Yong Hwan ^b   Sim, Sang Jun ^c   Lee, Jeewon ^a  

^a Korea University   (South Korea)

^b Kwangwoon University   (South Korea)

^c Sungkyunkwan University   (South Korea)

Author keywords

Bioactivity; CalB; Escherichia coli; Functional expression; Fusion mutant

Indexed keywords

DIMER; HYBRID PROTEIN; ISOMERASE; LIPASE B; MALATE DEHYDROGENASE; PERIPLASMIC PROTEIN; PUTRESCINE BINDING PERIPLASMIC PROTEIN; SPERMIDINE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CANDIDA ANTARCTICA; CYTOPLASM; ENZYME ACTIVE SITE; ESCHERICHIA COLI; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEOMICS;

CANDIDA; DIMERIZATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; LIPASE; MALATE DEHYDROGENASE; MEMBRANE TRANSPORT PROTEINS; MODELS, MOLECULAR; PEPTIDYLPROLYL ISOMERASE; PERIPLASMIC BINDING PROTEINS; PROTEIN CONFORMATION; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; SOLUBILITY;

CANDIDA ANTARCTICA; ESCHERICHIA COLI;

EID: 59349084955     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.12.007     Document Type: Article

References (25)

1. Kirk O., and Christensen M.W. Lipases from Candida antarctica: unique biocatalysts from a unique origin. Org. Process Res. Dev. 6 (2002) 446-451
2. Uppenberg J., Patkar S., Bergfors T., and Jones T.A. Crystallization and preliminary X-ray studies of lipase B from Candida antarctica. J. Mol. Biol. 235 (1994) 790-792
3. Uppenberg J., Ohrner N., Norin M., Hult K., Kleywegt G.J., Patkar S., Waagen V., Anthonsen T., and Jones T.A. Crystallographic and molecular-modeling studies of lipase B from Candidaantarctica reveal a stereospecificity pocket for secondary alcohols. Biochemistry 34 (1995) 16838-16851
4. Brzozowski A.M., Derewenda U., Derewenda Z.S., Dodson G.G., Lawson D.M., Turkenburg J.P., Bjorkling F., Hugejensen B., Patkar S.A., and Thim L. A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature 351 (1991) 491-494
5. Holmquist M., Tessier D.C., and Cygler M. High-level production of recombinant Geotrichum candidum lipases in yeast Pichia pastoris. Protein Expr. Purif. 11 (1997) 35-40
6. Martinelle M., and Hult K. Kinetics of acyl transfer reactions in organic media catalysed by Candida antarctica lipase B. Biochim. Biophys. Acta 1251 (1995) 191-197
7. Rotticci D., Norin T., Hult K., and Martinelle M. An active-site titration method for lipases. Biochim. Biophys. Acta 1483 (2000) 132-140
8. Overbeeke P.L.A., Govardhan C., Khalaf N., Jongejan J.A., and Heijnen J.J. Influence of lid conformation on lipase enantioselectivity. J. Mol. Catal., B Enzym. 10 (2000) 385-393
9. Zhang N., Suen W.C., Windsor W., Xiao L., Madison V., and Zaks A. Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution. Protein Eng. 16 (2003) 599-605
10. Rotticci-Mulder J.C., Gustavsson M., Holmquist M., Hult K., and Martinelle M. Expression in Pichia pastoris of Candida antarctica lipase B and lipase B fused to a cellulose-binding domain. Protein Expr. Purif. 21 (2001) 386-392
11. Kim S.Y., Sohn J.H., Pyun Y.R., Yang I.S., Kim K.H., and Choi E.S. In vitro evolution of lipase B from Candida antarctica using surface display in Hansenula polymorpha. J. Microbiol. Biotechnol. 17 (2007) 1308-1315
12. Rotticci-Mulder J.C. Expression and Mutagenesis Studies of Candida antartica Lipase B (2003), Stockholm AlbaNova University Centre 1-74
13. Chodorge M., Fourage L., Ullmann C., Duvivier V., Masson J.M., and Lefevre F. Rational strategies for directed evolution of biocatalysts - application to Candida antarctica lipase B (CALB). Adv. Synth. Catal. 347 (2005) 1022-1026
14. Blank K., Morfill J., Gumpp H., and Gaub H.E. Functional expression of Candida antarctica lipase B in Eschericha coli. J. Biotechnol. 125 (2006) 474-483
15. Liu D., Schmid R.D., and Rusnak M. Functional expression of Candida antarctica lipase B in the Escherichia coli cytoplasm-a screening system for a frequently used biocatalyst. Appl. Microbiol. Biotechnol. 72 (2006) 1024-1032
16. Jung S., and Park S. Improving the expression yield of Candida antarctica lipase B in Escherichia coli by mutagenesis. Biotechnol. Lett. 30 (2008) 717-722
17. Han K.Y., Park J.S., Seo H.S., Ahn K.Y., and Lee J. Multiple stressor-induced proteome responses of Escherichia coli BL21(DE3). J. Proteome Res. 7 5 (2008) 1891-1903
18. Park J.S., Han K.Y., Song S.A., Ahn K.Y., Seo H.S., and Lee J. Escherichia coli malate dehydrogenase, a novel solubility enhancer for heterologous proteins synthesized in Escherichia coli. Biotechnol. Lett. 29 (2007) 1513-1518
19. Han K.Y., Seo H.S., Song J.A., Ahn K.Y., Park J.S., and Lee J. Transport proteins PotD and Crr of Escherichia coli, novel fusion partners for heterologous protein expression. Biochim. Biophys. Acta 1774 (2007) 1536-1543
20. Han K.Y., Song J.A., Ahn K.A., Park J.S., Seo H.S., and Lee J. Solubilization of aggregation-prone heterologous proteins by covalent fusion of stress-responsive Escherichia coli protein, SlyD. Protein Eng. Des. Sel. 20 (2007) 543-549
21. Xu Y., Yasin A., Wucherpfennig T., and Chou C.P. Enhancing functional expression of heterologous lipase in the periplasm of Escherichia coli. World J. Microbiol. Biotechnol. 24 (2008) 2827-2835
22. Davis G.D., Elisee C., Newham D.M., and Harrison R.G. New fusion protein systems designed to give soluble expression in Escherichia coli. Biotechnol. Bioeng. 65 (1999) 382-388
23. Garcia-Alles L.F., and Gotor V.V. Alcohol inhibition and specificity studies of lipase B from Candida antarctica in organic solvents. Biotechnol. Bioeng. 59 (1998) 163-170
24. Kirk O., Björkling F., Godtfredsen S.E., and Larsen T.O. Fatty acid specificity in lipase-catalyzed synthesis of glucoside esters. Biocatalysis 6 (1992) 127-134
25. Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105-132