Structure and binding ability of self-assembled α-lactalbumin protein nanotubular gels.

Abstract

Partial hydrolysis of whey-based α-lactalbumin (α-La) with Bacillus licheniformis protease (BLP) induces the formation of nanotubular structures in the presence of calcium ions by a self-assembly process. α-La nanotubes (α-LaNTs) exist in the form of regular hollow strands with well-defined average dimensions. The growth of nanotubes induces the formation of stiff transparent protein gels due to the well-arranged networks that the strands can form; these gels can be used for entrapment, transportation, and target delivery of bioactive agents in the industry. High purity of α-La (free of other whey protein fractions) is desirable for nanotube formation; however, pure proteins are very expensive and not practically obtained for industrial applications. Thus, the purpose of this research was to construct α-LaNTs from an α-La preparation with lower purity and to study the gelation phenomena triggered by the self-assembled nanotubes. Some structural features of nanotube gels and their active agent-binding abilities were also investigated. A lower amount of α-LaNTs was observed when low purity α-La was used for nanotube formation. Nanotube growth induced gel formation and higher gel stiffness was obtained when compared to α-La hydrolysates. α-La was denatured after hydrolysis and self-assembly, and remarkable changes were observed in the α-helix and β-sheet domains of α-La structure. Increased intensity in Amide I and II regions indicated potential locations for binding of active agents to α-LaNTs. Whey-based α-La without much purification can be used to produce nanotubular gels and these gels can be considered carrying matrices for active agents in various industrial applications.