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Quality parameters of chicken breast meat affected by carcass scalding conditions
Rosana Aparecida da Silva-Buzanello,Alexia Francielli Schuch,Andre Wilhan Gasparin,Alex Sanches Torquato,Fernando Reinoldo Scremin,Cristiane Canan,Adriana Lourenco Soares 아세아·태평양축산학회 2019 Animal Bioscience Vol.32 No.8
Objective: The influence of broiler carcass scalding conditions on chicken breast meat quality parameters was investigated. Methods: Two hundred and seventy Cobb broiler chickens from 42 to 48 days old were slaughtered according to the standard industry practice and scalded in five temperature/time combinations—T1, 54°C/210 s; T2, 55°C/180 s; T3, 56°C/150 s; T4, 57°C/120 s; T5, 58°C/90 s. Results: Scalding temperature increase resulted in higher values of external and ventral lightness and in protein functionality reduction—determined by emulsification capacity and protein denaturation—in chicken breast fillets 24 h post-mortem. Protein secondary structures had conformational changes, with a decrease of the α-helix and an increase of the β-sheet and β-turn proportions, mainly in T1 and T5 samples, determined by Fourier-transform infrared spectroscopy in an attenuated reflectance mode analysis. The chemical composition, pH, water holding capacity and Warner-Bratzler shear force did not differ among the treatments. In the fatty acid profile, the 18:1n-9 was lower in T5, which suggested that the high scalding-temperature could have caused the lipid oxidation. The values of the polyunsaturated fatty acids (PUFA), such as 22:2, 20:4n-6, and 22:6n-3, were highest in the T5, thus being related to the phospholipid cellular membrane collapse in this experimental condition and subsequent release of these PUFA. Conclusion: Intermediate scalding-parameters avoided the negative changes in the chicken meat quality.
( Colussi Francieli ),( Viviane Serpa ),( Priscila Da Silva Delabona ),( Livia Regina Manzine ),( Maria Luiza Voltatodio ),( Renata Alves ),( Bruno Luan Mello ),( Nei Pereira Jr. ),( Cristiane Sanches 한국미생물 · 생명공학회 2011 Journal of microbiology and biotechnology Vol.21 No.8
Because of its elevated cellulolytic activity, the filamentous fungus Trichoderma harzianum has a considerable potential in biomass hydrolysis applications. Trichoderma harzianum cellobiohydrolase I (ThCBHI), an exoglucanase, is an important enzyme in the process of cellulose degradation. Here, we report an easy single-step ion-exchange chromatographic method for purification of ThCBHI and its initial biophysical and biochemical characterization. The ThCBHI produced by induction with microcrystalline cellulose under submerged fermentation was purified on DEAE-Sephadex A-50 media and its identity was confirmed by mass spectrometry. The ThCBHI biochemical characterization showed that the protein has a molecular mass of 66 kDa and pI of 5.23. As confirmed by smallangle X-ray scattering (SAXS), both full-length ThCBHI and its catalytic core domain (CCD) obtained by digestion with papain are monomeric in solution. Secondary structure analysis of ThCBHI by circular dichroism revealed α- helices and β-strands contents in the 28% and 38% range, respectively. The intrinsic fluorescence emission maximum of 337 nm was accounted for as different degrees of exposure of ThCBHI tryptophan residues to water. Moreover, ThCBHI displayed maximum activity at pH 5.0 and temperature of 50℃ with specific activities against Avicel and p-nitrophenyl-β-D-cellobioside of 1.25 U/mg and 1.53 U/mg, respectively.