Bovine alpha-lactalbumin assemblies with capsaicin: Formation, interactions, loading and physiochemical characterization
Autor: | Alon Romano, Carolina Lajterer, Avi Shpigelman, Uri Lesmes |
---|---|
Rok vydání: | 2020 |
Předmět: |
Chemical Phenomena
01 natural sciences Analytical Chemistry Hydrophobic effect Colloid chemistry.chemical_compound 0404 agricultural biotechnology Animals Humans biology Hydrogen bond Chemistry 010401 analytical chemistry 04 agricultural and veterinary sciences General Medicine 040401 food science Binding constant 0104 chemical sciences Characterization (materials science) Molecular Docking Simulation Capsaicin Alpha-lactalbumin biology.protein Biophysics Lactalbumin Cattle Hydrophobic and Hydrophilic Interactions Stoichiometry Food Science Protein Binding |
Zdroj: | Food chemistry. 352 |
ISSN: | 1873-7072 |
Popis: | Numerous human conditions can benefit from diets rich in proteins and bioactives, such as capsaicin (CAP), yet their effective delivery is a sensorial, scientific and technological challenge. This study hypothesized that CAP can form various complexes with native bovine alpha-lactalbumin (holo-ALA) and decalcified-ALA (apo-ALA). Calorimetric and spectroscopic techniques reveals ALA-CAP molecular complexation is spontaneous, exothermic and accompanied by various conformational changes. ITC shows the interaction stoichiometry (n) and binding constant (Kb) for holo-ALA to be 0.87 ± 0.03, 1.54 ± 0.23 × 105 M−1 and for apo-ALA to be 0.64 ± 0.09, 9.41 ± 2.16 × 104 M−1. Molecular docking further elucidates that hydrogen bonds govern CAP binding to holo-ALA while hydrophobic interactions dominate binding to apo-ALA in a structural cleft. Finally, this work shows these interactions along with controlled aggregation can be utilized to form CAP-loaded colloids with encapsulation efficiency of 47.1 ± 1.0%. Thus, this study shows great promise in the prospective use of ALA as an edible delivery vehicle for CAP. |
Databáze: | OpenAIRE |
Externí odkaz: |