107 Quality Parameters of Pet Treats Generated from Beef Processing Co-products

By-products such as beef liver (BL) and beef heart (BH), while rich in protein, vitamins, and minerals, can be difficult products for incorporation into mixtures. Sodium alginate (SA) and calcium lactate (CL) can be used to improve structure of protein sources. The objective was to determine the quality of restructured BL and BH pet treats using ALGIN as a structure forming agent. Quality parameters assessed were pH, expressible moisture, cooking loss, and water activity of raw and dehydrated pet treats. After grinding, BL and BH, were mixed: 25%BL:75%BH, 50%BL:50%BH, and 75%BL:25%BH. The 3 BL:BH combinations were mixed with 2 dosages of ALGIN (0.5% SA + 0.425% CL, and 1% SA + 0.85% CL) to produce 6 treatments. Each treatment was then extruded into 20-mm-thick jerky slices and refrigerated at 3°C for 48 h. Samples were dehydrated at 93°C for 2.5 h for cooking loss analysis. Ten raw samples (25.4 mm × 25.4 mm) were used to measure expressible moisture, and another ten raw samples were used to measure pH. Water activity was assessed on ten raw and ten dehydrated samples. Data were analyzed with the GLIMMIX procedure of SAS and means were separated at P ≤ 0.05. Cooking loss decreased as ALGIN dosage increased in all BL and BH mixtures (P < 0.0001); however, cooking loss percentage increased as BH proportions increased (P = 0.0001). Water activity of dehydrated samples decreased as BL proportions increased (P < 0.0001), but with increasing ALGIN dosage, water activity of dehydrated treats increased (P = 0.0193). Raw pH was not affected by treatment. Expressible moisture of samples increased with increasing BL proportions (P < 0.0001) but decreased as ALGIN dosage decreased (P < 0.0001). Use of ALGIN allowed for BL and BH to be restructured into an acceptable form for use in pet treats.

Study of the effect of various ingredients on the organoleptic and functional-technological properties of beef heart

Offals are of interest to both factures of meat products and consumers. At the same time, the ambiguity of the organoleptic properties of offals and the lasted of their processing create barriers to the growth of their consumption. The studies carried out allowed us to demonstrate the most effective approaches to obtain the necessary organoleptic properties of a product with high functional -technological characteristics. The most effective approach to improve the properties of products from beef heart is using of lactic acid starter culture and citric acid.

Effects of replacement of black soldier fly (Hermetia illucens) larvae meal in the diets on growth performance of discus fish (Symphysodon sp.)

This study was conducted to evaluate the replacement of fishmeal by black soldier fly larvae (Hermetia illucens) (BSF) meal, frozen beef heart, and commercial pellet on growth performance, survival rate, and feed utilization of discus fish (Symphysodon sp.). Discus juveniles were graded into small, medium and large size groups as block in a completely randomized block design. Five trial diets included frozen beef heart (T1), commercial feed for discus fish (T2) and three diets containing graded levels of BSF as replacements for protein from fishmeal of 0% (T3), 25% (T4), and 50% (T5). The results showed that TAN and nitrite levels in the beef heart treatment were higher than those in the other ones. Moreover, discus fish in treatment 1 had a higher growth rate and a lower feed conversion ratio than those in the other treatments. On the other hand, no statistically significant differences among the pellet treatments were observed for growth rates of discus's weight, length and height and feed conversion ratio (P > 0.05). Moreover, the results showed that discus fish in the two BSF treatments did not suffer from diseases and had higher survival rates than those in the other treatments.

Proteomic Analysis of Peroxynitrite-Induced Protein Nitration in Isolated Beef Heart Mitochondria

Mitochondria are exposed to reactive nitrogen species under physiological conditions and even more under several pathologic states. In order to reveal the mechanism of these processes we studied the effects of peroxynitrite on isolated beef heart mitochondria in vitro. Peroxynitrite has the potential to nitrate protein tyrosine moieties, break the peptide bond, and eventually release the membrane proteins into the solution. All these effects were found in our experiments. Mitochondrial proteins were resolved by 2D electrophoresis and the protein nitration was detected by immunochemical methods and by nano LC-MS/MS. Mass spectrometry confirmed nitration of ATP synthase subunit beta, pyruvate dehydrogenase E1 component subunit beta, citrate synthase and acetyl-CoA acetyltransferase. Immunoblot detection using chemiluminiscence showed possible nitration of other proteins such as cytochrome b-c1 complex subunit 1, NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, elongation factor Tu, NADH dehydrogenase [ubiquinone] flavoprotein 2, heat shock protein beta-1 and NADH dehydrogenase [ubiquinone] iron-sulfur protein 8. ATP synthase beta subunit was nitrated both in membrane and in fraction prepared by osmotic lysis. The high sensitivity of proteins to nitration by peroxynitrite is of potential biological importance, as these enzymes are involved in various pathways associated with energy production in the heart.

Proteomic Analysis of Peroxynitrite-Induced Protein Nitration in Isolated Beef Heart Mitochondria

Mitochondria are exposed to reactive nitrogen species under physiological conditions and even more under several pathologic states. In order to reveal the mechanism of these processes we studied the effects of peroxynitrite on isolated beef heart mitochondria in vitro. Peroxynitrite has the potential to nitrate protein tyrosine moieties, break the peptide bond, and eventually release the membrane proteins into the solution. All these effects were found in our experiments. Mitochondrial proteins were resolved by 2D electrophoresis and the protein nitration was detected by immunochemical methods and by nano LC-MS/MS. Mass spectrometry confirmed nitration of ATP synthase subunit beta, pyruvate dehydrogenase E1 component subunit beta, citrate synthase and acetyl-CoA acetyltransferase. Immunoblot detection using chemiluminiscence showed possible nitration of other proteins such as cytochrome b-c1 complex subunit 1, NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, elongation factor Tu, NADH dehydrogenase [ubiquinone] flavoprotein 2, heat shock protein beta-1 and NADH dehydrogenase [ubiquinone] iron-sulfur protein 8. ATP synthase beta subunit was nitrated both in membrane and in fraction prepared by osmotic lysis. The high sensitivity of proteins to nitration by peroxynitrite is of potential biological importance, as these enzymes are involved in various pathways associated with energy production in the heart.

Comparison of the Effects of Tert-Butyl Hydroperoxide and Peroxynitrite on the Oxidative Damage to Isolated Beef Heart Mitochondria

Isolated beef heart mitochondria have been exposed to tert-butyl hydroperoxide (tBHP) and peroxynitrite (PeN) in order to model the effects of reactive oxygen and nitrogen species on mitochondria in vivo. The formation of malondialdehyde (MDA), protein carbonyls, lipofuscin-like pigments (LFP), and nitrotyrosine was studied during incubations with various concentrations of oxidants for up to 24 h. The oxidants differed in their ability to oxidize particular substrates. Fatty acids were more sensitive to the low concentrations of tBHP, whereas higher concentrations of PeN consumed MDA. Oxidation of proteins producing carbonyls had different kinetics and also a probable mechanism with tBHP or PeN. Diverse proteins were affected by tBHP or PeN. In both cases, prolonged incubation led to the appearance of proteins with molecular weights lower than 29 kDa bearing carbonyl groups that might have been caused by protein fragmentation. PeN induced nitration of protein tyrosines that was more intensive in the soluble proteins than in the insoluble ones. LFP, the end products of lipid peroxidation, were formed more readily by PeN. On the other hand, fluorometric and chromatographic techniques have confirmed destruction of LFP by higher PeN concentrations. This is a unique feature that has not been described so far for any oxidant.