Effect of gelatin drying methods on its amphiphilicity

Abstract

Gelatin is a natural amphiphilic biopolymer that is widely used in food products, pharmaceuticals, and cosmetics. We studied the effect of spray and freeze drying on the solubility and amphiphilicity of gelatin samples. The control sample was a commercially produced edible gelatin. The experimental samples were spray- and freeze-dried gelatins obtained by enzymatic-acid hydrolysis of cattle bone. Amino acid sequences were determined by matrix-activated laser desorption/ionization. Solubility was assessed visually. Bloom strength of the gelatin gels was measured by a texture analyzer. The ProtScale online service was used to predict the amphiphilic topology of gelatin proteins. Molecular weight distribution of proteins was carried out by electrophoresis in polyacrylamide gel in the presence of sodium dodecyl sulfate. Spray drying reduced protein degradation and retained more α-chains, while freeze drying increased gelatin’s hydrophobicity and decreased its solubility. The predicted topology of protein hydrophobicity based on the amino acid sequences was in line with our results on solubility. The freeze-dried gelatin had a 18% larger amount of low-molecular weight peptides, compared to the control and the spray-dried samples. This was probably caused by the cleavage of peptides during the drying process. Thus, freeze drying can lead to maximum degradation of gelatin components, which may be associated with a longer heat treatment, compared to spray drying. Thus, spray drying is more suitable for gelatin, since this method improves the stability of its outer and inner structure, ensuring high hydrophilic properties.