Changes in chymotrypsin hydrolysis of β-lactoglobulin A induced by high hydrostatic pressure

Journal of Agricultural and Food Chemistry

Volumn 54, Issue 6, 2006, Pages 2333-2341

  Chicón, Rosa ^a   López Fandiño, Rosina ^a   Quirós, Ana ^a   Belloque, Josefina ^a  

^a INSTITUTO DE FERMENTACIONES INDUSTRIALES CSIC   (Spain)

Author keywords

Lactoglobulin; Chymotrypsin; High hydrostatic pressure; Milk whey proteins; Proteolysis

Indexed keywords

CHYMOTRYPSIN; LACTOGLOBULIN; PEPTIDE FRAGMENT;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; ELECTROSPRAY MASS SPECTROMETRY; ENZYME SPECIFICITY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROLYSIS; HYDROSTATIC PRESSURE; METABOLISM; POLYACRYLAMIDE GEL ELECTROPHORESIS;

CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CHYMOTRYPSIN; DIMERIZATION; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HYDROLYSIS; HYDROSTATIC PRESSURE; LACTOGLOBULINS; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SUBSTRATE SPECIFICITY;

EID: 33645760729     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf051983s     Document Type: Article

References (22)

1. Olsen, K.; Kristiansen, K. R.; Skibsted, L. H. Effect of high hydrostatic pressure on the steady-state kinetics of tryptic hydrolysis of β-lactoglobulin. Food Chem. 2003, 80, 255-260.
2. Bonomi, F.; Fiocchi, A.; Frøkiær, H.; Gaiaschi, A.; Iametti, S.; Poiesi, C.; Rasmussen, P.; Restain, P.; Rovere, P. Reduction of immunoreactivity of bovine β-lactoglobulin upon combined physical and proteolytic treatment. J. Dairy Res. 2003, 70, 51-59.
3. Dufour, E.; Hervé, G.; Haertle, T. Hydrolysis of β-lactoglobulin by thermolysin and pepsin under high hydrostatic pressure. Biopolymers 1995, 35, 475-483.
4. Maynard, F.; Weingand, A.; Hau, J.; Jost, R. Effect of high-pressure treatment on the tryptic hydrolysis of bovine β-lactoglobulin AB. Int. Dairy J. 1998, 8, 125-133.
5. Van Willige, R. W. G.; Fitzgerald, R. J. Tryptic and chymotryptic hydrolysis of β-lactoglobulin A, B and AB at ambient and high pressure. Milchwissenschaft 1995, 50, 183-186.
6. Knudsen, J. C.; Otte, J.; Olsen, K.; Skibsted, L. H. Effect of high hydrostatic pressure on the conformation of β-lactoglobulin A as assessed by proteolytic peptide profiling Int. Dairy J. 2002, 12, 791-803.
7. Chicón, R.; Belloque, J.; Recio, I.; López-Fandiño, R. Influence of high hydrostatic pressure on the proteolysis of β-lactoglobulin A by trypsin. J. Dairy Res. 2006, 73, 121-128.
8. Hosseini-nia, T.; Ismail, A. A.; Kubow, S. Pressure-induced conformational changes of β-lactoglobulin by variable-pressure Fourier transform infrared spectroscopy. J. Agric. Food Chem. 1999, 47, 4537-4542.
9. Pittia, P.; Wilde, P. J.; Husband, F. A.; Clark, D. C. Functional and structural properties of β-lactoglobulin as affected by high-pressure treatment. J. Food Sci. 1996, 61, 1123-1128.
10. 1H NMR study on the effects of high pressure on the structure of β-lactoglobulin. J. Agric. Food Chem. 2000, 48, 3906-3912.
11. Ebeler, S. E.; Phillips, L. G.; Kinsella, J. E. Purification of β-lactoglobulin: isolation of genetic variants and influence of purification method on secondary structure. Milchwissenschaft 1990, 45, 694-698.
12. PeptideCutter, ExPASy, Swiss Institute of Bioinformatics. Special cleavage rules for trypsin and chymotrypsin; http://www.expasy.org/tools/ peptidecutter_special_enzymes.html.
13. Keil, B. Specificity of Proteolysis; Springer-Verlag: Berlin, Germany, 1992; 335 pp.
14. Mozhaev, V. V.; Lange, R.; Kudrashova, E. V.; Balny, C. Application of high hydrostatic pressure for increasing activity and stability of enzymes. Biotechnol. Bioeng. 1996, 52, 320-331.
15. Creamer, L. K.; Bienvenue, A.; Nilsson, H.; Paulsson, M.; Van Wanrou, M.; Lowe, E. K.; Anema, S. G.; Boland, M. J.; Jiménez-Flores, R. Heat-induced redistribution of disulfide bonds in milk proteins. 1. Bovine β-lactoglobulin. J. Agric. Food Chem. 2004, 52, 7660-7668.
16. Bauer, R.; Hansen, S.; Øgendal, L. Detection of intermediate oligomers, important for the formation of heat aggregates of β-lactoglobulin. Int. Dairy J. 1998, 8, 105-112.
17. 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. 1997, 45, 23-29.
18. Iametti, S.; Rasmussen, P.; Frøkiær, H.; Ferranti, P.; Addeo, F.; Bonomi, F. Proteolysis of bovine β-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity. Eur. J. Biochem. 2002, 269, 1362-1372.
19. Panick, G.; Malessa, R.; Winter, R. Differences between the pressure- and temperature-induced denaturation and aggregation of β-lactoglobulin A, B and AB monitored by FTIR spectroscopy and small-angle X-ray scattering. Biochemistry 1999, 38, 6512-6519.
20. 1H NMR study. J. Agric. Food Chem. 1998, 46, 1805-1813.
21. Edwards, P. J. B.; Jameson, G. B.; Palmano, K. P.; Creamer, L. K. Heat-resistant structural features of bovine β-lactoglobulin. Int. Dairy J. 2002, 12, 331-344.
22. Brownlow, S.; Morais Cabral, J. H.; Cooper, R.; Flower, D. R.; Yewdall, S. J.; Polikarpov, I.; North, A. C.; Sawyer, L. Bovine β-lactoglobulin at 1.8 A resolution - still an enigmatic lipocalin. Structure 1997, 15, 481-495.