Abstract
Bovine cattle milk lactoferrin is industrially produced from cow’s milk and used in a variety of functional products, including baby food, nutritional supplements, dairy products, and veterinary drugs. The possibility of obtaining lactoferrin from lactic acid milk wheyrises a particular interest. The purpose of this study is to assess the possibility of using and adapting existing spectrophotometric methods for determining the concentration of total protein and an electrophoretic method for analyzing the protein composition of whey fractions and lactoferrin substances. A comparative study of two methods for determining the total protein in whey fractions and lactoferrin preparations biuret and Bradford method was carried out. The validation parameters of both methods were defined. An analytical range from 30 μg / ml to 1000 μg / ml characterizes the linearity of the Bradford method. The electrophoretic profile of milk, milk whey, whey fractions and substances of lactoferrinwere analyzed. The results obtained indicate a high information content of the electrophoretic method for characterizing the purification efficiency of whey fractions.
Highlights
Lactoferrin is a multifunctional iron-binding protein of the transferrin family [1]
The applicability of two methods of spectrophotometric determination of the total protein concentration for the analysis of milk and whey fractions and determination of the purity of lactoferrin substances was analyzed in this work
It was found that the linearity of the dependence of the solution absorbance on the concentration of lactoferrin when using the biuret method is characterized by a rather narrow analytical range - from 5 μg / ml to 400 μg / ml
Summary
Lactoferrin is a multifunctional iron-binding protein of the transferrin family [1]. In the organism of mammals, it is part of various secretory fluids and has a wide range of biological activities [2]. Lactoferrin accumulates in neutrophils, and its increased concentration is found in inflammation sites. The biological activity of lactoferrinis established by the ability to bind iron ions and the presence of hydrophobic and charged areas on the protein surface. Specific receptors for this protein have been found on the cell surface. The high binding constant of iron is due to the presence of an alphahelix in the bridge that binds two domains of this protein [3]
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