26 research outputs found
Effect of collagen on technological quality of meat
Kolagen stanowi 20 - 30 % bia艂ek w organizmie ssak贸w oraz ptak贸w i jest podstawowym sk艂adnikiem 艣r贸dmi臋艣niowej tkanki 艂膮cznej. G艂贸wnym magazynem kolagenu w mi臋艣niach jest omi臋sna zewn臋trzna (epimysium) i wewn臋trzna (perimysium) oraz 艣r贸dmi臋sna (endomysium). W艣r贸d ponad 20 typ贸w genetycznych kolagenu w mi臋艣niach szkieletowych znaczn膮 cz臋艣膰 stanowi kolagen typu I i III. Morfologia, sk艂ad i ilo艣膰 tkanki 艂膮cznej w mi臋艣niach zale偶y w g艂贸wnej mierze od ich typu oraz gatunku, rasy i wieku zwierz臋cia. R贸偶nice w metodach oznaczania kolagenu sprawiaj膮, 偶e zawarto艣膰 tego bia艂ka w poszczeg贸lnych mi臋艣niach mo偶e by膰 zr贸偶nicowana. Du偶a zawarto艣膰 tego niepe艂nowarto艣ciowego bia艂ka w tkance 艂膮cznej mi臋艣ni ma znacz膮cy wp艂yw na krucho艣膰 mi臋sa, obni偶aj膮c jego jako艣膰. Zwi臋kszaj膮ce si臋 wraz z wiekiem zwierz臋cia usieciowanie kolagenu w mi臋艣niach o wysokiej aktywno艣ci za 偶ycia sprawia, 偶e mi臋so staje si臋 twarde. Mniejsz膮 zawarto艣膰 kolagenu stwierdzono w mi臋艣niach o d艂u偶szych sarkomerach oraz w mi臋sie ze zwierz膮t p贸藕no dojrzewaj膮cych i wykastrowanych.Collagen constitutes 20 - 30 % of proteins in the organism of mammals and birds, and it is a major
component of the intramuscular connective tissue. In the muscles, collagen is mainly stored in epimysium, perimysium, and endomysium. There are more than 20 genetic types of collagen in the skeletal muscles and, among them, collagen type I and type III are a significant portion. The morphology, composition, and quantity of the connective tissue in the muscles depend predominantly on their type, as well as on the species, breed, and age of the animal. Owing to differences in the methods of determining collagen, the content of this protein can differ in individual muscles. A high content of this incomplete protein in the connective tissue of the muscles has a significant impact on the tenderness of meat and decreases its quality. The cross-linking of collagen in the muscles that are highly active in live animals increases with age of animals and causes the meat to become hard. A lower content of collagen was found in the muscles with longer sarcomeres and in the meat from late maturing and castrated animals
Heme iron in meat as the main source of iron in the human diet
Iron is a trace element involved in many cardinal metabolic processes of almost all living organisms. It is well known that iron participates in oxygen transport as well as it is a cofactor in many fundamental enzymatic and nonenzymatic processes. Accordingly, disturbances of iron homeostasis can cause serious clinical consequences. In humans, dietary iron can enter the body in two main forms: heme and nonheme. The former is a component of many hemoproteins (including myoglobin, hemoglobin, cytochromes b and c) and is easily absorbed in the duodenal enterocytes. Red meat is an excellent source of heme iron, while the less bioavailable nonheme form is found in large amounts in milk products and vegetables. For this reason, consumers of meat have a better iron status than vegetarians and vegans. The aim of this paper was to discuss the role of heme iron in the human diet. Heme iron found in muscle protein should be supplied to humans to prevent iron deficiency, which can lead to anemia. It is easily absorbed by the human body and its main source is red meat. In addition, heme iron, which is mainly found in myoglobin in meat, contributes to the desirable bright red color and to the most undesirable brown color of meat. Both heme and nonheme iron are catalysts of lipid oxidation in meat. This process lowers the nutritive value through oxidation of polyunsaturated fatty acids, which produces an undesirable flavor and aroma. The present review is focused on the role of heme iron, which is mainly found in meat and is the principal source of iron in the human diet