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

TARHAN Ö., Hamaker B. R., Campanella O. H.

Biotechnology Progress, cilt.37, sa.3, 2021 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 37 Sayı: 3
  • Basım Tarihi: 2021
  • Doi Numarası: 10.1002/btpr.3127
  • Dergi Adı: Biotechnology Progress
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Applied Science & Technology Source, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Chemical Abstracts Core, Compendex, Computer & Applied Sciences, EMBASE, Environment Index, Food Science & Technology Abstracts, MEDLINE, Pollution Abstracts, Veterinary Science Database
  • Anahtar Kelimeler: active agent binding, circular dichroism, nanotubes, protein gel, α-lactalbumin
  • Uşak Üniversitesi Adresli: Evet

Özet

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.