RESEARCH OF THE EFFECT OF THE TRANSGLUTAMINASE ENZYME ON THE PROPERTIES OF HYDRATED PROTEINS OF ANIMAL AND PLANT ORIGIN
Abstract
Meeting consumer demand for dietary proteins requires the search for and implementation of advanced technologies in both meat processing and the use of protein-containing raw materials of plant origin. Protein modification research is gaining great interest among domestic and foreign scientists. Microbial transglutaminase is an enzyme of the transferase class that is widely known to modify the functional properties of proteins in food systems. The main mechanism of action is polymerisation, which leads to a change in the hydrophobicity of the molecule. Among the functional properties of microbial transglutaminase is the effect on solubility and thus on gelation, emulsification, viscosity and water retention, which depend on protein solubility. Thanks to these properties, it is widely used in the food industry, in particular in the meat processing and dairy industries, as well as in the manufacture of bakery products and food films. Transglutaminase catalyses the acyl transfer reaction, in which the γ-carboxamide group of peptide-bound glutamine residues is the acyl donor. This research compares the effect of the amount of enzyme (0.05%, 0.1%, 0.15% and 0.2%) of microbial transglutaminase (activity 100-120 units) on animal protein, which is Grade 2 beef meat and vegetable protein, soy isolate ISOPRO 510A. In the hydrated samples, instrumental analysis was carried out using a pH meter (pH 50 VIO lab) and a textrometer (Shimadzu EZ-LX) for animal proteins before and after heat treatment. For hydrated plant proteins, similar research was carried out at 45±2°C in the centre of the test sample after 1 hour of fermentation and after gelation with 12 hours of incubation at 6±2°C. The results of the pH research indicate that the enzyme efficiency reaches its optimum at the active acidity of the experimental protein systems in the pH range from 5 to 8. The use of the microbial transglutaminase enzyme in hydrated proteins of animal and plant origin has been shown to have a positive effect on the restructuring of these proteins through a cross-linking reaction. The increase in pH is due to the formation of ammonia (NH3) as a result of this reaction. According to research results, it is recommended to add 0.05% to 0.1% of microbial transglutaminase to hydrated protein systems.
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