Loosening of globular structure under alkaline pH affects accessibility of β-lactoglobulin to tyrosinase-induced oxidation and subsequent cross-linking

Enzyme and Microbial Technology

Volumn 49, Issue 2, 2011, Pages 131-138

  Partanen, Riitta ^a   Torkkeli, Mika ^b   Hellman, Maarit ^c   Permi, Perttu ^c   Serimaa, Ritva ^b   Buchert, Johanna ^a   Mattinen, Maija Liisa ^a  

^a VTT TECHNICAL RESEARCH CENTRE OF FINLAND   (Finland)

^b UNIVERSITY OF HELSINKI   (Finland)

^c UNIVERSITY OF HELSINKI   (Finland)

Author keywords

lactoglobulin; Accessibility; Cross linking; Hydrolysis; Oxidation; Tyrosinase; Unfolding

Indexed keywords

ACCESSIBILITY; AGARICUS BISPORUS; ALKALINE CONDITIONS; ALKALINE PH; BASIC RESEARCH; GLOBULAR PROTEINS; GLOBULAR STRUCTURE; INCREASED FLEXIBILITY; INTERMOLECULAR CROSSLINKING; LACTOGLOBULIN; OXYGEN CONSUMPTION; PARTIAL HYDROLYSIS; REACTION CONDITIONS; RESEARCH RESULTS; SMALL ANGLE X-RAY SCATTERING; SODIUM DODECYL SULPHATE; STRUCTURAL CHANGE; THREE-DIMENSIONAL STRUCTURE; TRICHODERMA REESEI; TRYPTOPHAN FLUORESCENCE; TYROSINASE; UNFOLDING;

AMINO ACIDS; DICHROISM; ELECTROPHORESIS; ENZYMES; HYDROLYSIS; OXIDATION; PROTEIN FOLDING; PROTEINS; SODIUM;

ALKALINITY;

BETA LACTOGLOBULIN; MONOMER; MONOPHENOL MONOOXYGENASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; TRYPTOPHAN;

ALKALINITY; ARTICLE; CATALYSIS; CIRCULAR DICHROISM; CORRELATION ANALYSIS; FLUORESCENCE ANALYSIS; HYDROPHOBICITY; HYPOCREA JECORINA; NONHUMAN; OXIDATION; OXYGEN CONSUMPTION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN CONFORMATION; PROTEIN CROSS LINKING; PROTEIN FOLDING; PROTEIN HYDROLYSIS; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

ANIMALS; CATTLE; CIRCULAR DICHROISM; CROSS-LINKING REAGENTS; HYDROGEN-ION CONCENTRATION; LACTOGLOBULINS; MODELS, MOLECULAR; MONOPHENOL MONOOXYGENASE; OXIDATION-REDUCTION; PROTEIN CONFORMATION; SCATTERING, SMALL ANGLE; SPECTROMETRY, FLUORESCENCE; X-RAY DIFFRACTION;

AGARICUS BISPORUS; HYPOCREA JECORINA;

EID: 79959908730     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2011.04.010     Document Type: Article

References (36)

1. P.F.Fox P.F., McSweeney P.L.H. Dairy Chemistry and Biochemistry 1998, Blackie Academic & Professional, London.
2. Brownlow S., Cabral J.H.M., Cooper R., Flower D.F., Yewdall S.J., Polikarpov I., et al. Bovine β-lactoglobulin at 1.8Å resolution-still an anigmatic lipocalin. Structure 1997, 5:481-495.
3. Qin B.Y., Bewley M.C., Creamer L.K., Baker H.M., Baker E.N., Jameson G.B. Structural basis of the Tanford transition of bovine β-lactoglobulin. Biochemistry 1998, 37:14014-14023.
4. Kuwata K., Hoshino M., Forge V., Era S., Batt C.A., Goto Y. Solution structure and dynamics of bovine β-lactoglobulin A. Protein Sci 1999, 8:2541-2545.
5. Barteri M., Gaudiano M.C., Rotella S., Benagiano G., Pala A. Effect of pH on the structure and aggragation of human glycodelin A. A comparison with β-lactoglobulin A. Biochem Biophys Acta 2000, 1479:255-264.
6. Sakurai K., Goto Y. Dynamics and mechanism of the Tanford transition of bovine β-lactoglobulin studied using heteronuclear NMR spectroscopy. J Mol Biol 2006, 356:483-496.
7. Oliveira K., Valente-Mesquita V., Botelho M., Sawyer L., Ferreira S., Polikarpov I. Crystal structures of bovine β-lactoglobulin in the orthorhombic space group C2221, Structural differences between genetic variants A and B and features of the Tanford transition. Eur J Biochem 2001, 268:477-483.
8. Considine T., Patel H.A., Anema S.G., Singh H., Creamer L.K. Interactions of milk proteins during heat and high hydrostatic pressure treatments-a review. IFSET 2007, 8:1-23.
9. Taulier N., Chakilian T.V. Characterization of pH-induced transitions of β-lactoglobulin: ultrasonic, densimetric and spectroscopic studies. J Mol Biol 2001, 314:873-889.
10. Cheison S.C., Schmitt M., Leeb E., Letzel T., Kulozik U. Influence of temperature and degree of hydrolysis on the peptide composition of trypsin hydrolysates of b-lactoglobulin: analysis by LC-ESI-TOF/MS. Food Chem 2010, 121:457-467.
11. Lorenzen P.C. Effects of varying time/temperature-conditions of pre-heating and enzymatic cross-linking on techno-functional properties of reconstituted dairy ingredients. Food Res Int 2007, 40:700-708.
12. Hiller B., Lorenzen P.C. Surface hydrophobicity of physicochemically and enzymatically treated milk proteins in relation to techno-functional properties. J Agric Food Chem 2008, 56:461-468.
13. Selinheimo E., Lampila P., Mattinen M.-L., Buchert J. Formation of protein-oligosaccharide conjugates by laccase and tyrosinase. J Agric Food Chem 2008, 56:3118-3128.
14. Monogioudi E., Creusot N., Kruus K., Gruppen H., Buchert J., Mattinen M.-L. Cross-linking of β-casein by Trichoderma reesei tyrosinase and Streptoverticillium mobaraense transglutaminase followed by SEC-MALLS. Food Hydroc 2009, 23:2008-2015.
15. Jaros D., Partschefeld C., Henle T., Rohm H. Transglutaminase in dairy products: chemistry, physics, applications. J Text Stud 2006, 37:113-155.
16. Lerch K. Neurosprora tyrosinase: structural, spectroscopic and catalytic properties. Mol Cell Biochem 1983, 52:138-152.
17. Robb D.A. Tyrosinase. Copper Proteins and Copper Enzymes 1984, vol. 2:207-270. CRC Press, Inc, Boca Raton.
18. Ito S., Kato T., Shinpo K., Fujita K. Oxidation of tyrosine residues in proteins by tyrosinase. Biochem J 1984, 222:407-411.
19. Burzio L.A., Waite J.H. Cross-linking in adhesive quinoproteins: studies with model decapeptides. Biochemistry 2000, 39:11147-11153.
20. Bittner S. When quinones meet amino acids: chemical, physical and biological consequences. Amino Acids 2006, 30:205-224.
21. Mattinen M.-L., Lantto R., Selinheimo E., Kruus K., Buchert J. Oxidation of peptides and proteins by Trichoderma reesei and Agaricus bisporus tyrosinases. J Biotechnol 2008, 133:395-402.
22. Hellman M., Mattinen M.-L., Fu B., Buchert J. P Permi, Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear NMR spectroscopy. J Biotech 2011, 151:143-150.
23. Yasunobu K.T., Dandliker W.B. Action of tyrosinase on α-lactalbumin, β-lactoglobulin, and ribonuclease. J Biol Chem 1957, 224:1065-1072.
24. Thalmann R., Lötzbeyer T. Enzymatic cross-linking of proteins by tyrosinase. Eur Food Res Technol 2002, 214:276-281.
25. M. Faergemand, K.B. Qvist, Functional properties of enzymatically crosslinked milk proteins-cross-linking of (-lactoglobulin, in: Proceedings of the Conference on Structure and Functionality of Food Products, Mragowo, Poland (1998), pp. 53-54, cited from de Jong and Koppelman (2002).
26. Selinheimo E., Nieidhin D., Steffensen C., Nielsen J., Lomascolo A., Halaouli S., et al. Comparison of the characteristics of fungal and plant tyrosinases. J Biotechnol 2007, 130:471-480.
27. Selinheimo E., Saloheimo M., Ahola E., Westerholm-Parvinen A., Kalkkinen N., Buchert J., et al. Production and characterization of a secreted C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei. FEBS J 2006, 273:4322-4335.
28. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
29. Svergun D.I. Mathematical methods in small-angle scattering data analysis. J Appl Cryst 1991, 24:485-492.
30. Kelly S., Jess T., Price N. How to study proteins by circular dichroism. Biochim Biophys Acta 2005, 1751:119-139.
31. Yang J., Dunker K., Powers J.R., Clark S., Swanson B. β-Lactoglobulin molten globule induced by high pressure. J Agric Food Chem 2001, 49:3236-3243.
32. Hamada D., Goto Y. The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure. J Mol Biol 1997, 269:479-487.
33. Sakurai K., Konuma T., Yagi M., Goto Y. Structural dynamics and folding of β-lactoglobulin probed by heteronuclear NMR. Biochem Biophys Acta 2009, 1790:527-537.
34. Kim Y.-J., Uyama H. Review. Tyrosinase inhibitors from natural and synthetic sources: structure, inhibition mechanisms and perspective for the future. Cell Mol Life Sci 2005, 62:1707-1723.
35. de Jong G.A.H., Koppelman S.J. Transglutaminase catalyzed reactions: impact on food applications. J Food Sci 2002, 67:2798-2806.
36. O'Sullivan M.M., Kelly A.L., Fox P.F. Effect of transglutaminase on the heat stability of milk: a possible mechanism. J Dairy Sci 2002, 85:1-7.