Induced structural change to β-lactoglobulin by combined pressure and temperature

Biochemical Engineering Journal

Volumn 5, Issue 1, 2000, Pages 73-76

  Tedford, L A ^a   Schaschke, C J ^a  

^a UNIVERSITY OF STRATHCLYDE   (United Kingdom)

Author keywords

Denaturation; Food processing; High pressure; Protein structure

Indexed keywords

BETA LACTOGLOBULIN;

ARTICLE; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; PH; PRESSURE; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; TEMPERATURE;

EID: 0034006622     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-703X(99)00068-6     Document Type: Article

References (22)

1. Papiz M.Z., Sawyer L., Eliopoulos E.E., North A.C.T., Findlay J.B.C., Sivaprasadarao R., Jones T.A., Newcomer M.E., Kraulis P.J. The structure of β-lactoglobulin and its similarity to plasma retinol-binding proteins. Nature. 324:1986;383-385
2. Hoover D., Metrick C., Papineau A., Farkas D., Knorr D. Biological effects of high hydrostatic pressure on food microorganisms. Food Technol. 43:1989;99-106
3. Cheftel J.C. Review: high pressure, microbial inactivation and food preservation. Food Sci. Technol. Int. 1:1995;75-90
4. Hayakawa I., Kanno T., Tomita M., Fujio Y. Application of high pressure for spore inactivation and protein denaturation. J. Food Sci. 59:1994;159-163
5. 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
6. Jaenicke R. Enzymes under extremes of physical conditions. Annu. Rev. Biophys. Bioeng. 10:1981;1-68
7. Hayashi R. Utilisation of pressure in addition to temperature in food science and technology. High Pressure and Biotech. 224:1992;185-193
8. Hayakawa I., Kajuhara J., Morikawa K., Oda M., Fujio Y. Denaturation of bovine serum albumin (BSA) and ovalbumin by high hydrostatic pressure heat and chemicals. J. Food Sci. 57:1992;288-292
9. Heremans K. High pressure effects on proteins and other biomolecules. Annu. Rev. Biophys. Bioeng. 11:1992;1-21
10. Balny C., Masson P., Travers F. Some recent aspects of the use of high pressure for protein solution investigations. High Pressure Res. 2:1989;1-28
11. Dumay E.M., Kalichevsky M.T., Cheftel J.C. High-pressure unfolding and aggregation of β-lactoglobulin and the baroprotective effects of sucrose. J. Agric. Food Chem. 42:1994;1861-1868
12. Hayashi R., Kawamura Y., Kunugi S. Introduction of high pressure to food processing: preferential proteolysis of β-lactoglobulin in milk whey. J. Food Sci. 52:1987;1107-1108
13. Funtenberger S., Dumay E.M., Cheftel J.C. Pressure-induced aggregation of β-lactoglobulin in pH 7.0 buffers. Lebensm. -Wiss. u.-Technol. 28:1995;410-418
14. Hayakawa I., Linko Y.-Y., Linko P. Mechanism of high pressure denaturation of proteins. Lebensm. -Wiss. u.-Technol. 29:1996;756-762
15. Iametti S., Transidico P., Bonomi F., Vecchio G., Pittia P., Rovere P., Dall'Aglio G. Molecular modifications of β-lactoglobulin upon exposure to high pressure. J. Agric. Food Chem. 45:1997;23-29
16. N.C. Price, in: R. Meyers (Ed,), Circular Dichroism In Protein Analysis, Mol. Biol. Biotech., 1995, 179-185.
17. Tanaka N., Koyasu A., Kobayashi I., Kunugi S. Pressure induced change in proteins studied through chemical modifications. Int. J. Biol. Macromolecules. 18:1996;275-280
18. Bell K., McKenzie H.A., Murphy W.H., Shaw D.C. β-lactoglobulin: a unique protein variant. Biochem. et Biophys. Acta. 214:1970;427-436
19. Tedford L.-A., Kelly S.M., Price N.C., Schaschke C.J. Combined effects of thermal and pressure processing on food protein structure. Trans. IChemE. 76(C):1998;80-86
20. Qi X.L., Brownlow S., Holt C., Sellers P. Thermal denaturation of β-lactoglobulin: effect of protein concentration at pH 6.75 and 8.05. Biochem. et Biophys. Acta. 1248:1995;43-49
21. Pittia P., Wilde P., Husband F., Clark D. Functional and structural properties of β-lactoglobulin as affected by high pressure treatment. J. Food Sci. 61:1996;1123-1128
22. De Wit J.N., Klarenbeek G.A. A differential scanning calorimetric study of the thermal behaviour of bovine β-lactoglobulin at temperatures up to 160°C. J. Dairy Res. 48:1981;293-302