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Published on: May 17, 2020
Molecular Interaction of Pea Glutelin and Lipophilic Bioactive Compounds: Structure-Binding Relationship and
Ogadimma D Okagu1, Raliat O Abioye1, Chibuike C Udenigwe1,2
1Department of Chemistry and Biomolecular Sciences, Faculty of Science, University of Ottawa, Ottawa, Ontario K1N 6N5, Canada.
Abstract:
This study investigated the impact of ionic strength and lipophilicity of bioactive compounds on their interaction with the alkaline soluble pea glutelin fraction (ASF) using the fluorescence quenching technique. A Stern-Volmer quenching constant, KD, of 8.9 ± 0.10, 5.3 ± 0.06, 4.0 ± 0.01, 1.1 ± 0.00, 0.9 ± 0.02, and 0.1 ± 0.00 (×104 M-1) was observed for curcumin-ASF (CuASF), astaxanthin-ASF (AsASF), cholecalciferol-ASF (ChASF), β-carotene-ASF (βCaASF), coenzyme Q10-ASF (Q10ASF), and β-sitosterol-ASF (βSiASF) complexes, respectively. An increase in ionic strength did not significantly change KD, the effective quenching constant K, and the bimolecular quenching rate constant KQ. However, it changed the mode of interaction of the ASF with cholecalciferol, β-carotene, coenzyme Q10, and β-sitosterol from static to static-dynamic quenching. Transmission electron microscopy showed that the morphology formed with protein (spherical nanocomplexes, microaggregates, or fiber-like particles) differed among the compounds. The favorable binding of CuASF, AsASF, ChASF, and βCaASF complexes provides stable matrices for formulating protein-based delivery systems for lipophilic nutraceuticals.
