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BIOLOGICALLY ACTIVE SUBSTANCES OF APICOMPONENTS FOR STABILIZATION OF THE STRUCTURE OF COLLAGEN FIBERS IN THE TECHNOLOGICAL CYCLE OF PRODUCTION OF MEAT PRODUCTS
Abstract
One of the directions of the rational use of the secondary raw materials of meat industry, including collagen-containing, is its modification in order to obtain protein products enriched with micronutrients for the further use in food production. The presence of active carboxyl end groups in the collagen molecule and complex spatial structure cause the complexation of this protein with various minor nutrients, thereby promoting the creation of a biologically active composite for the enrichment of meat products. To confirm the complexation of collagen with biological active substances, a differential scanning microcalorimetry method was used, which allows determining the change in the structure of collagen after the introduction of ascorbic acid derived from bee products (bee pollen) by the amount of heat absorption. The results of our own research allow us to conclude that the selected minor components are immobilized on the spatial mesh of modified collagen fibers, which is confirmed by the enthalpy of the denaturation transition of the main component equal to 6.3 J / g, respectively, and the peak maximum temperature ? 42.8 (for ascorbic acid) °?. Testing of the developed biologically active composites in the technology of meat products has proved that the immobilization of ascorbic acid, isolated from apicomponents, on the fibers of modified collagen contributes to their preservation in finished products in an amount up to 73 %.
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References6
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