e-journal
Interactions between bovine serum albumin and alginate: An evaluation of alginate as protein carrier
Abstract.
The intermolecular interactions between the model protein, bovine serum albumin (BSA) and a
biocompatible polysaccharide, sodium alginate, have been investigated. Both the native BSA and the heat
pre-denatured BSA were utilized to study, in parallel, the effect of protein conformational change during
the protein–alginate complex formation. In this work, a comparison was performed between the native
BSA and the heat-denatured BSA incubated sodium alginate mixtures by using zeta potential analyzer,
dynamic light scattering (DLS) and turbidimetric analysis of the systems in combination with protein
conformational tools, Fourier transform infrared spectroscopy (FT-IR) and size exclusion chromatography
(SE-HPLC). The experimental results demonstrate that the intermolecular chain associations were formed
between alginate chains and protein molecules in either the native form or the heat pre-denatured
form, mainly driven by the electrostatic interactions between the oppositely charged amino acids and
the anionic polysaccharide macromolecules. However, the majority of BSA was recovered from the
dissociation of protein–alginate complexes and maintained its secondary structure and conformational
property. Therefore, alginate is promising as a bioactive compound carrier.
Keywords:
Intermolecular interactions
Complexes
Denaturation
Carboxyl groups
Dissociation
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