Heterologous expression of bovine and porcine β-lactoglobulins in Pichia pastoris: Towards a comparative functional characterisation

Journal of Biotechnology

Volumn 109, Issue 1-2, 2004, Pages 169-178

  Invernizzi, Gaetano ^a   Ragona, Laura ^b   Brocca, Stefania ^a   Pedrazzoli, Eros ^a   Molinari, Henriette ^d   Morandini, Piero ^c   Catalano, Maddalena ^b,d   Lotti, Marina ^a  

^a UNIVERSITY OF MILANO BICOCCA   (Italy)

^b CNR   (Italy)

^c UNIVERSITY OF MILAN   (Italy)

^d UNIVERSITY OF VERONA   (Italy)

Author keywords

Lactoglobulin; Expression; NMR; Pichia pastoris

Indexed keywords

CELL CULTURE; CHROMATOGRAPHY; CLONING; GENES; ION EXCHANGE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS;

ION EXCHANGE CHROMATOGRAPHY; RECOMBINANT PROTEINS;

BIOTECHNOLOGY;

BETA LACTOGLOBULIN; LIPOCALIN; RECOMBINANT PROTEIN;

AERATION; CATTLE; CELL CULTURE; COMPARATIVE STUDY; CONCENTRATION (PARAMETERS); CONFERENCE PAPER; CONTROLLED STUDY; CULTURE MEDIUM; GENETIC CODE; HOST CELL; ION EXCHANGE CHROMATOGRAPHY; MOLECULAR CLONING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PICHIA PASTORIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SWINE;

ANIMALS; CATTLE; CLONING, MOLECULAR; GENE EXPRESSION; LACTOGLOBULINS; MAGNETIC RESONANCE SPECTROSCOPY; PICHIA; PROMOTER REGIONS (GENETICS); RECOMBINANT PROTEINS; SWINE;

BOVINAE; PICHIA; PICHIA PASTORIS; SUIDAE;

EID: 1842582875     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2003.10.034     Document Type: Conference Paper

References (20)

1. Bartels C., Xia T., Billeter M., Güntert P., Wüthrich K. The program XEASY for computers-supported NMR spectra analysis of biological macromolecules. J. Biomol. NMR. 5:1995;1-10.
2. Batt C.A., Rabson L.D., Wong D.W., Kinsella J.E. Expression of recombinant bovine beta-lactoglobulin in Escherichia coli. Agric. Biol. Chem. 54(4):1990;949-955.
3. Bax A., Davis D.G. MLEV-17 based two-dimensional homonuclear magnetisation transfer spectroscopy. J. Magn. Reson. 65:1985;355-360.
4. De Jong P. β-Lactoglobulin as a major responsible of heat exchanger inefficiency. Trends Food Sci. Technol. 8:1997;401-405.
5. Flower S.R., North A.C.T., Sansom C.E. The lipocalin protein family: structural and sequence overview. Biochim. Biophys. Acta. 1482:2000;9-24.
6. Fogolari F., Ragona L., Zetta L., Romagnoli S., De Kruif K.G., Molinari H. Monomeric bovine β-lactoglobulin adopts a β-barrel fold at pH. FEBS Lett. 436:1998;149-154.
7. Fogolari F., Licciardi S., Romagnoli S., Ragona L., Michelutti R., Ugolini R., Molinari H. Electrostatic properties of bovine beta lactoglobulin. Proteins: Struct. Funct. Genet. 39:2000;317-330.
8. Ho S.M., Hunt H.D., Horton R.M., Pullen J.K., Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene. 77:1989;51-59.
9. Hyttinen J.M., Korhonen V.P., Hiltunen M.O., Myohanen S., Janne J. High-level expression of bovine beta-lactoglobulin gene in transgenic mice. J. Biotechnol. 61(3):1998;191-198.
10. Kim T.R., Goto Y., Hirota N., Kuwata K., Denton H., Wu S.Y., Sawyer L., Batt C.A. High-level expression of bovine beta-lactoglobulin in Pichia pastoris and characterization of its physical properties. Protein Eng. 10(11):1997;1339-1345.
11. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature. 227:1970;680-685.
12. Ragona L., Pusterla F., Zetta L., Monaco H.L., Molinari H. Identification of a conserved hydrophobic cluster in partially folded bovine lactoglobulin at pH 2. Fold. Des. 2(5):1997;281-290.
13. Schlehuber S., Skerra A. Tuning ligand affinity specificity and folding stability of an engineered lipocalin variant - a so-called "anticalin" - using a molecular random approach. Biophys. Chem. 96:2000;213-228.
14. Scorer C.A., Clare J.J., McCombie W.R., Romanos M.A., Sreekrishna K. Rapid selection using G418 of high copy number transformants of Pichia pastoris for high-level foreign gene expression. Biotechnology. 12:1994;181-184.
15. 15N HSQC experiments optimised to retain full sensitivity J. Magn. Reson., Ser. A. 102:1993;241-245.
16. Totsuka M., Katakura Y., Shimizu M., Kumagai I., Miura K., Kaminogawa S. Expression and secretion of bovine beta-lactoglobulin in Saccharomyces cerevisiae. Agric. Biol. Chem. 54(12):1990;3111-3116.
17. Ugolini R., Ragona L., Silletti E., Fogolari F., Visschers R.W., Alting A.C., Molinari H. Dimerization, stability and electrostatic properties of porcine beta-lactoglobulin. Eur. J. Biochem. 268:2001;4477-4488.
18. 15C chemical shifts for bovine β-lactoglobulin: secondary structure and topology of the native state is retained in a partially unfolded form J. Biomol. NMR. 12:1998;89-107.
19. Vittayanont M., Steffe J.F., Fleger F.L., Smith D.M. Gelling properties of heat-denatured beta-lactoglobulin aggregates in high-salt buffer. J. Agric. Food Chem. 50(10):2002;2987-2992.
20. 15N random coil NMR chemical shifts of the common amino acids. Investigations of nearest-neighbor effects J. Biomol. NMR. 5:1995;67-81.