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Published online before print April 9, 2004, 10.1110/ps.03513204
Protein Science (2004), 13:1340-1346. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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Spectroscopic characterization of heat-induced nonnative {beta}-lactoglobulin monomers

Thomas Croguennec1, Daniel Mollé1, Raj Mehra2 and Saïd Bouhallab1

1 Unité Mixte de Recherche (UMR) École Nationale Supérieure Agronomique-Institut National de Recherche Agronomique (ENSA-INRA), 35 042 Rennes Cedex, France
2 Dairy Products Research Center, Teagasc, Moorepark, Fermoy, County Cork, Ireland

(RECEIVED November 14, 2003; FINAL REVISION January 12, 2004; ACCEPTED February 1, 2004)



Abstract

Previous studies have shown that two altered monomeric species were formed in the early steps of thermal denaturation of bovine {beta}-lactoglobulin ({beta}-lg), the well-known Cys121-exposed intermediate (Mcys121), and a new, stable monomer with exposed nonnative Cys119 (Mcys119). In this study, circular dichroism and fluorescence spectroscopies were used to characterize the structural features of these molecules. The structural characteristics of MCys121 after heating and cooling cycles are similar to those of native {beta}-lg. In contrast, Mcys119 monomer exhibits some characteristics of the well-known molten-globule state. Combined with other published data, these results indicate that heating induces at least two molten globule-like states of {beta}-lg, a highly reactive Mcys121 that returns to native state after cooling, and a less-reactive Mcys119 that is trapped and stabilized in a molten globule-like state by nonnative disulfide bond.

Keywords: {beta}-lactoglobulin heat denaturation; molten globule; stability; sulfhydryl groups

Reprint requests to: Thomas Croguennec, UMR ENSA-INRA, CS 842l5, 65, rue de St. Brieuc, 35 042 Rennes Cedex, France; e-mail: Thomas.Croguennec{at}agrorennes.educagri.fr; fax: 33-2-23-48-55-78.

Article published ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03513204.


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