Open AccessBovine serum albumin with gallic acid: Molecular modeling and physicochemical profiling
Author(s) -
Nikita Fedortsov,
Elena V. Budkevich,
И. А. Евдокимов,
S.A. Ryabtseva,
Roman O. Budkevich
Publication year - 2022
Publication title -
foods and raw materials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.212
H-Index - 8
eISSN - 2310-9599
pISSN - 2308-4057
DOI - 10.21603/2308-4057-2022-1-163-170
Subject(s) - gallic acid , chemistry , bovine serum albumin , serum albumin , chromatography , polyphenol , sodium dodecyl sulfate , biochemistry , gel electrophoresis , antioxidant
. Gallic acid is a biologically active natural compound with strong antioxidant properties. Gallic acid is highly soluble and stable. It is known to increase the thermal stability of protein. However, its bioavailability is low, but interaction with proteins can solve this problem. Bovine serum albumin can bind various ligands, including polyphenols. The resulting complex of gallic acid and bovine serum albumin can become a promising functional food additive.
Study objects and methods. This research featured in silico molecular modeling of gallic acid and bovine serum albumin using the HyperChem program. The methods of infrared spectrometry, potentiometry, and sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) made it possible to describe the physicochemical profile of the complex.
Results and discussion. The molecular modeling confirmed that hydrophobic interactions were responsible for the chemical bond between gallic acid and bovine serum albumin. The SDS-PAGE test showed that the protein molecule remained intact. The reducing properties of the complex grew as the concentration of gallic acid increased. At 100 mg/L of gallic acid, the reducing properties were 7.8 ± 1.3 mg/L equivalent of gallic acid. At 200 and 300 mg/L, the values reached 15.90 ± 2.65 and 23.30 ± 5.05 mg/L, respectively. The IR spectrometry revealed a significant difference between the samples with different concentrations of gallic acid.
Conclusion. The research managed to predict the properties of the complex of bovine serum albumin and gallic acid during its formation. The resulting complex had the highest reducing properties at 0.69 g of bovine serum albumin and 300 mg of gallic acid. The obtained parameters can be used in the food industry to develop new food additives.