Academic Journal
Investigation of glutathione peroxidase activity in chicken meat under different experimental conditions Investigação da atividade de glutationa peroxidase em carne de frango submetida a diferentes condições experimentais
| العنوان: | Investigation of glutathione peroxidase activity in chicken meat under different experimental conditions Investigação da atividade de glutationa peroxidase em carne de frango submetida a diferentes condições experimentais |
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| المؤلفون: | Alexandre José Cichoski, Renata Bezerra Rotta, Gerson Scheuermann, Anildo Cunha Junior, Juliano Smanioto Barin |
| المصدر: | Food Science and Technology, Vol 32, Iss 4, Pp 661-667 (2012) |
| بيانات النشر: | Sociedade Brasileira de Ciência e Tecnologia de Alimentos |
| سنة النشر: | 2012 |
| المجموعة: | Directory of Open Access Journals: DOAJ Articles |
| مصطلحات موضوعية: | GSH-Px, carne de frango, atividade enzimática, selênio, tampão, substrato, meat chicken, enzymatic activity, selenium, buffers, substrate, Nutrition. Foods and food supply, TX341-641, Technology (General), T1-995 |
| الوصف: | Due to the fact that previous studies on the enzymatic activity of Glutathione peroxidase (GSH-Px) diverge widely in their methodology and results, this study aimed to investigate the influence of different analytical conditions on GSH-Px activity in chicken thighs from broilers that were fed different diets with different sources and concentrations of selenium. GSH-Px activity was evaluated six hours after slaughter and 120 days after frozen storage at -18 ºC. The different analytical conditions included time of pre-incubation (0, 10 and 30 minutes), reaction medium, types of substrate (H2O2 (0.72 mM, 7.2 mM, and 72 mM) and Terc-butil hydroperoxide 15 mM), and different buffer concentrations (buffer 1, potassium phosphate 50 mM pH 7.0 + EDTA 1 mM + mercaptoethanol 1 mM, and buffer 2, tris-HCl 50 mM pH 7.6 + EDTA 1 mM + mercapthanol 5 mM). The results show that the highest GSH-Px activity was observed when enzyme and substrate were in contact at 22 ºC without any pre-incubation, and that, when used at concentrations above 0.72 mM, hydrogen peroxide saturated the GSH-Px enzyme and inhibited its activity. The enzyme presented higher affinity to hydrogen peroxide when compared to terc-butil peroxide, and the addition of a buffer containing mercaptoethanol did not increase GSH-Px enzymatic activity. The activity of GSH-Px was not influenced by the source and concentration of selenium in the diet either. The obtained results allowed the determination of the best temperature of contact between the enzyme and substrate (22 ºC), the optimum concentration, and the type of substrate and buffer to be used. This information is extremely useful for future studies on GSH-Px activity in meat due to the divergence and little information found in the literature. Uma vez que estudos anteriores sobre a atividade enzimática da glutationa peroxidase (GSH-Px) divergem acerca da metodologia e dos resultados, este estudo teve por objetivo investigar a influência de diferentes condições de ensaio sobre a atividade da GSH-Px em coxas de ... |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 0101-2061 1678-457X |
| Relation: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612012000400004; https://doaj.org/toc/0101-2061; https://doaj.org/toc/1678-457X; https://doaj.org/article/fd4a9c95d15d4b4198ee254caff7e939 |
| الاتاحة: | https://doaj.org/article/fd4a9c95d15d4b4198ee254caff7e939 |
| رقم الانضمام: | edsbas.DF9DA9C6 |
| قاعدة البيانات: | BASE |
| تدمد: | 01012061 1678457X |
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