The interaction between beta-Lactoglobulin and allyl-isothiocyanate

Ersoz N., DUDAK ŞEKER F. C.

FOOD BIOSCIENCE, cilt.36, 2020 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 36
  • Basım Tarihi: 2020
  • Doi Numarası: 10.1016/j.fbio.2020.100600
  • Dergi Adı: FOOD BIOSCIENCE
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Food Science & Technology Abstracts, INSPEC
  • Hacettepe Üniversitesi Adresli: Evet

Özet

Beta-Lactoglobulin (beta-Lg) is a globular milk protein and a major component of whey (similar to 50% dry weight). beta-Lg binds strongly to various hydrophobic ligands and may act as a transporter for these molecules. Monomeric beta-Lg has two disulfide bonds and one free thiol group that have important roles in the formation of the tertiary structures of beta-Lg. As a result, beta-Lg reacts to pH changes in a very specific manner. In this study, isothermal titration calorimetry (ITC) and circular dichroism (CD) were used to investigate the interaction between beta-Lg and allyl isothiocyanate (AITC) at different pH values 3.0, 6.5 and 8.5. The interaction was characterized using total reflectance Fourier-transform infrared spectroscopy and molecular docking. The final thermograms from ITC were fitted to three sites of a sequential binding model (Koshland model), showing the high affinity between beta-Lg and AITC with binding constants of 10(4)-10(5) M-1. ITC and CD results showed that AITC binding at different pH changes the secondary structure of beta-Lg. FTIR results showed the binding of AITC with strong isothiocyanate peaks between 1900 and 2150 cm(-1). Three different AITC-binding sites to beta-Lg were confirmed using molecular docking. The results showed that the characteristic properties of the interaction between beta-Lg and AITC can be used to predict the nanotransporter capacity of beta-Lg for bioactive materials at different pH values.