In situ observation of pressure-induced increased thermostability of two β-galactosidases with FT-IR spectroscopy in the diamond anvil cell

Enzyme and Microbial Technology

Volumn 31, Issue 5, 2002, Pages 673-684

  Degraeve, Pascal ^a,c   Rubens, Peter ^b   Lemay, Pierre ^a   Heremans, Karel ^b  

^a UMR792 INGÉNIERIE DES SYSTÈMES BIOLOGIQUES ET DES PROCÉDÉS   (France)

^b UNIVERSITY OF LEUVEN   (Belgium)

^c Lab Rech Genie Industriel A   (France)

Author keywords

Galactosidase; Aspergillus oryzae; Escherichia coli; High pressure; Infrared spectroscopy; Stability; Temperature

Indexed keywords

CELLS; ESCHERICHIA COLI; FOURIER TRANSFORM INFRARED SPECTROSCOPY; THERMODYNAMIC STABILITY;

SITU OBSERVATION;

ENZYMES;

AMIDE; BETA GALACTOSIDASE; FUNGAL ENZYME; PEPTIDE; SOLVENT;

ARTICLE; ASPERGILLUS ORYZAE; CONFORMATIONAL TRANSITION; ENZYME STABILITY; ENZYME STRUCTURE; INCUBATION TIME; INFRARED SPECTROSCOPY; ION EXCHANGE; NONHUMAN; PRESSURE; TEMPERATURE DEPENDENCE; THERMOSTABILITY;

ASPERGILLUS; ASPERGILLUS ORYZAE; ESCHERICHIA COLI;

EID: 0037015417     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(02)00163-1     Document Type: Article

References (41)

1. Silva J.L., Weber G. Pressure stability of proteins. Ann. Rev. Phys. Chem. 44:1993;89-113.
2. Heremans K., Smeller L. Protein structures and dynamics at high pressure. Biochim. Biophys. Acta. 1386:1998;353-370.
3. Farr D. High pressure technology in the food industry. Trends Food Sci. Technol. 1:1990;14-16.
4. Athès V., Degraeve P., Cavaillé-Lefebvre D., Espeillac S., Lemay P., Combes D. Increased thermostability of three mesophilic β-galactosidases under high pressure. Biotechnol. Lett. 19:1997;273-276.
5. Richmond M., Gray J., Stine C. Beta-galactosidase: review of recent research related to technological application, nutritional concerns and immobilization. J. Dairy Sci. 64:1981;1759-1771.
6. Vian A., Carrascosa A.V., Garcia J.L., Cortes E. Structure of the β-galactosidase gene from Thermus sp. Strain T2: expression in Escherichia coli and purification in a single step of an active fusion protein. Appl. Environ. Microb. 64:1998;2187-2191.
7. Ladero M., Santos A., Garcia J.L., Garcia-Ochoa F. Activity over lactose and ONPG of a genetically engineered β-galactosidase from Escherichia coli in solution and immobilized: kinetic modelling. Enzyme Microb. Technol. 29:2001;181-193.
8. Hawley S.A. Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry. 10:1971;2436-2442.
9. Zipp A., Kauzmann W. Pressure denaturation of metmyoglobin. Biochemistry. 12:1973;4217-4228.
10. 1H NMR J. Mol. Biol. 298:2000;293-302.
11. Hei D.J., Clark D.S. Pressure stabilization of proteins from extremophiles. Appl. Environ. Microbiol. 60:1994;932-939.
12. Konisky J., Michels P.C., Clark D.S. Pressure stabilization is not a general property of thermophilic enzymes: the adenylate kinases of Methanococcus voltae, Methanococcus maripaludis, Methanococcus thermolithotrophicus and Methanococcus jannaschii. Appl. Environ. Microbiol. 61:1995;2762-2764.
13. Goossens K., Smeller L., Frank J., Heremans K. Pressure-tuning the conformation of bovine pancreatic trypsin inhibitor studied by Fourier transform infrared spectroscopy. Eur. J. Biochem. 236:1996;254-262.
14. Baello B.I., Pancoska P., Keiderling T.A. Enhanced prediction accuracy of protein secondary structure using hydrogen exchange Fourier transform infrared spectroscopy. Anal. Biochem. 280:2000;46-57.
15. Robertson A.D., Purisima E.O., Eastman M.A., Scheraga H.A. Proton NMR assignments and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution. Biochemistry. 28:1989;5930-5938.
16. Parker FS, editor. Applications of Infrared Spectroscopy in Biochemistry, Biology and Medicine. New York: Plenum Press, 1971.
17. Wong P.T.T., Heremans K. Pressure effects on protein secondary structure and hydrogen deuterium exchange in chymotrypsinogen: a Fourier transform infrared spectroscopic study. Biochim. Biophys. Acta. 956:1988;1-9.
18. Dzwolak W., Kato M., Shimizu A., Taniguchi Y. Fourier transform infrared spectroscopy study of the pressure-induced changes in the structure of the bovine α-lactalbumin: the stabilizing role of calcium. Biochim. Biophys. Acta. 1433:1999;45-55.
19. 1-proteinase inhibitor and ovalbumin in aqueous solution. Arch. Biochem. Biophys. 383:2000;148-155.
20. Miller JH. Purification of β-galactosidase. In: Miller JH, editor. Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, 1972. p. 398-404.
21. Wong P.T.T., Moffat D.J. A new internal pressure calibrant for high-pressure infrared spectroscopy of aqueous systems. Appl. Spectrosc. 43:1989;1279-1281.
22. Wong P.T.T. Pressure effect on hydrogen isotope exchange kinetics in chymotrypsinogen investigated by FT-IR spectroscopy. Can. J. Chem. 69:1991;1699-1704.
23. Arrondo J.L.R., Muga A., Castresana J., Bernabeu C., Goñi F.M. An infrared spectroscopic study of β-galactosidase structure in aqueous solutions. FEBS Lett. 252:1989;118-120.
24. Muga A., Arrondo J.L.R., Bellon T., Sancho J., Bernabeu C. Structural and functional studies on the interaction of sodium dodecyl sulfate with β-galactosidase. Arch. Biochem. Biophys. 300:1993;451-457.
25. Degraeve P., Lemay P. High pressure-induced modulation of the activity and stability of Escherichia coli (lac z) β-galactosidase: potential applications. Enzyme Microb. Technol. 20:1997;550-557.
26. Garnier J., Osguthorpe D.J., Robson R. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120:1978;97-120.
27. Edwards R.A., Jacobson A.L., Huber R.E. Thermal denaturation of β-galactosidase and of two site-specific mutants. Biochemistry. 29:1990;11001-11008.
28. Surewicz W.K., Mantsch H.H., Chapman D. Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. Biochemistry. 32:1993;389-394.
29. Kelly S.M., Price N.C. The unfolding and refolding of pig heart fumarase. Biochem. J. 275:1991;745-749.
30. Ma Y.Z., Tsou C.L. Comparison of the activity and conformational changes of lactate deshydrogenase H4 during denaturation by guanidium chloride. Biochem. J. 277:1991;207-211.
31. West S.M., Price N.C. The unfolding and refolding of glutamate deshydrogenases from bovine liver baker's yeast and Clostridium symbosium. Biochem. J. 251:1988;135-139.
32. Rubens P, Goossens K, Heremans K, Weemaes C, Hendrickx M, Tobback P. On the relation between pressure and temperature stability of α-amylases from Bacillus species: A FT-IR study. In: Heremans K, editor. High Pressure Research in the Biosciences and Biotechnology. Leuven, Belgium: Leuven University Press, 1997. p. 327-30.
33. Smeller L., Rubens P., Heremans K. Pressure effect on the temperature-induced unfolding and tendency to aggregate of myoglobin. Biochemistry. 38:1999;3816-3820.
34. Robertson A.D., Baldwin R.L. Hydrogen exchange in thermally denatured ribonuclease A. Biochemistry. 30:1991;9907-9914.
35. Hummer G., Garde S., Garcia A.E., Paulaitis M.E., Pratt L.R. The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proc. Natl. Acad. Sci. U.S.A. 95:1998;1552-1555.
36. Bec N., Villa A., Tortora P., Mozhaev V.V., Balny C., Lange R. Enhanced stability of carboxypeptidase from Sulfolobus solfataricus at high pressure. Biotechnol. Lett. 18:1996;483-488.
37. Wroblowski B., Diaz J.F., Heremans K., Engelborghs Y. Molecular mechanisms of pressure-induced conformational changes in BPTI. Proteins. 25:1996;446-455.
38. Mozhaev V.V., Heremans K., Frank J., Masson P., Balny C. Exploiting the effects of high hydrostatic pressure in biotechnological applications. TIBTECH. 12:1994;493-501.
39. Hendrickx M., Ludikhuyze L., Van den Broeck I., Weemaes C. Effects of high pressure on enzymes related to food quality. Trends Food Sci. Technol. 9:1998;197-203.
40. Mozhaev V.V., Lange R., Kudryashova E.V., Balny C. Application of high hydrostatic pressure for increasing activity and stability of enzymes. Biotech. Bioeng. 52:1996;320-331.
41. Rastogi N.K., Eshtiaghi M.N., Knorr D. Effects of combined high pressure and heat treatment on the reduction of peroxidase and polyphenoloxidase in red grapes. Food Biotechnol. 13:1999;195-208.