Molecular differences in the formation and structure of fine-stranded and particulate β-lactoglobulin gels

Abstract

In order to reveal at a molecular level differences between fine‐stranded and particulate gels, we present an Fourier transform infrared spectroscopic study of the thermal behavior of β‐lactoglobulin (β‐lg) in salt‐free D2O solutions and low ionic strength at different pDs. Differences are found in the denaturation mechanism, in the unfolded state of the protein, in the aggregate formation, and in the strength of the intermolecular interactions. For fine‐stranded gels (pD 2.8 and 7.8), heating induces the dissociation of the dimers into monomers. The protein undergoes extensive structural modifications before aggregation begins. Aggregation is characterized by the appearance of a new band attributed to intermolecular β‐sheets which is located in the 1613–1619 cm−1 range. For particulate gels (pD 4.4 and 5.4), the protein structure is almost preserved up to 75–80°C with no splitting of the dimers. The band characteristic of aggregation originates from the component initially located at 1623 cm−1, suggesting that at the beginning of aggregation, globular β‐lg in the dimeric form associate to constitute oligomers with higher molecular mass. Aggregation may result in the association of globular slightly denatured dimers, leading to the formation of spherical particles rather than linear strands. The aggregation band is always located in the 1620–1623 cm−1 range for particulate gels showing that hydrogen bonds are weaker for these aggregates than for fine‐stranded ones. This has been related to a more extensive protein unfolding for fine‐stranded gels that allows a closer alignment of the polypeptide chains, and then to the formation of much stronger hydrogen bonds. Small differences are also found in protein organization and in intermolecular hydrogen bond strength vs pD within the same type of gel. Protein conformation and protein–protein interactions in the gel state may be responsible of the specific macroscopic properties of each gel network. A coarse representation of the different modes of gelation is described. © 2000 John Wiley & Sons, Inc. Biopoly 54: 578–586, 2000

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Designed amphiphilic peptide forms stable nanoweb, slowly releases encapsulated hydrophobic drug, and accelerates animal hemostasis

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