INTRODUCTION: This study investigated the impact of adding crude fibre concentrate (CFC) to broiler chicken diets on slaughter results and breast muscle quality. MATERIAL AND METHODS: A total of 990 male Ross 308 chicks were divided into control (C), experimental 1 (A1) and experimental 2 (A2) groups. Experimental diets contained CFC at different levels: A1 had 0.4% in the starter diet, 0.8% in the first grower diet, 0.8% in the second grower diet and 0.2% in the finisher diet, and A2 had 0.6%, 1.0%, 1.2% and 0.4% in the same diets. On day 42, 20 birds per group were slaughtered and dissected. Breast muscles were weighed and visually assessed for myopathic defects (white striping, wooden breast and "spaghetti" meat). The tissue was also analysed for residual myopathy incidence and associated physicochemical properties, namely drip loss, shear force, pH, water holding capacity, collagen content, colour parameters and basal chemical composition. RESULTS: Consumption of the CFC additive statistically significantly reduced (P-value ≤ 0.05) white striping defects and increased final live weight by 2.1% for birds in group A1 and by 3.3% in group A2. Group A1 carcasses also weighed 6.7% more and group A2 carcasses 4.1% more. Additionally, A1 carcasses yielded 1.5% more and A2 carcasses 0.8% more leg muscle, also statistically significantly greater yields than C carcasses (P-value ≤ 0.05). The slaughter yield of birds in group A1 was 3.3% higher (P-value ≤ 0.001) than that of birds in group C. The use of the CFC additive in the diets of both experimental groups had no adverse effect on the other analysed parameters. CONCLUSION: Crude fibre concentrate addition to the complete feed mixture is recommended for improving the results of the slaughter analysis and the visual quality of meat.

• Klíčová slova
• breast muscle quality, chicken broiler, crude fibre, slaughter performance,
• Publikační typ
• časopisecké články MeSH

The stability of collagen, the most abundant protein in humans and many animals, is related to the hydroxylation of L-proline, a post-translational modification occurring at carbon 3 and 4 on its pyrrolidine ring. Collagens of different origins have shown different proline hydroxylation levels, making hydroxyprolines useful biomarkers in structure characterizations. The presence of two chiral carbon atoms, 3-hydroxyproline and 4-hydroxyproline, results in eight stereoisomers (four pairs of enantiomers) whose quantitation in collagen hydrolysates requires enantioselective analytical methods. Capillary electrophoresis was applied for the separation and quantitation of the eight stereoisomers of 3- and 4-hydroxyproline and D,L-proline in collagen hydrolysates. The developed method is based on the derivatization with the chiral reagent (R)-(-)-4-(3-Isothiocyanatopyrrolidin-yl)-7-nitro-2,1,3-benzoxadiazole, enabling the use of a light-emitting diode-induced fluorescence detector for high sensitivity. The separation of the considered compounds was accomplished in less than 10 min, using a 500 mM acetate buffer pH 3.5 supplemented with 5 mM of heptakis(2,6-di-O-methyl)-β-cyclodextrin as the chiral selector. The method was fully validated and showed the adequate sensitivity for the application to samples of collagen hydrolysates. The analysis of samples extracted from chicken Pectoralis major muscles affected by growth-related myopathies showed different stereoisomer patterns compared to those from the unaffected control samples.

• Klíčová slova
• capillary electrophoresis, chiral separations, collagen, cyclodextrins, derivatization, fast-growing chickens, fluorescent detection, hydroxyprolines, spaghetti meat, wooden breast,
• MeSH
• cyklodextriny * chemie   MeSH
• elektroforéza kapilární metody   MeSH
• hydroxyprolin * chemie   analýza   MeSH
• kolagen * chemie   MeSH
• kur domácí MeSH
• prolin * chemie   analýza   MeSH
• proteinové hydrolyzáty * chemie   MeSH
• stereoizomerie MeSH
• zvířata MeSH
• Check Tag
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• cyklodextriny * MeSH
• hydroxyprolin * MeSH
• kolagen * MeSH
• prolin * MeSH
• proteinové hydrolyzáty * MeSH