Abstract
AbstractThe present article is concerned with the practical and theoretical aspects of gelation in protein systems. The processes involved are, inter alia, so complicated that several types of protein molecule assemblies and conformational changes during the association have to be considered. The gel network can be stabilized by five types of interaction: covalent crosslinking, polar interactions, hydrogen bonding, salt bridges and hydrophobic interactions. The microstructures of gels formed from fibrillated proteins (collagen) and from globular proteins (e.g. α‐ and β‐ casein) differ considerably. Of practical interest are methods of controlling the solubility of gels, including e.g. the use of cross‐linking agents and addition of salts.
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