Serine Protease Inhibitors as Good Predictors of Meat Tenderness: Which Are They and What Are Their Functions?
| Autor: | Mohammed Gagaoua, Carlos Hernan Herrera-Mendez, Yasmine Boudida, Abdelghani Boudjellal, Miguel Angel Sentandreu, Ahmed Ouali, Brigitte Picard, Samira Becila |
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| Přispěvatelé: | Institut de la Nutrition de l'Alimentation et des Technologies Agro-Alimentaire (INATAA), Unité Mixte de Recherche sur les Herbivores - UMR 1213 (UMRH), Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Universidad de Guanajuato, Consejo Superior de Investigaciones Científicas [Madrid] (CSIC), Qualité des Produits Animaux (QuaPA), Institut National de la Recherche Agronomique (INRA) |
| Rok vydání: | 2014 |
| Předmět: |
0301 basic medicine
Models Molecular Proteases Meat Serine Proteinase Inhibitors Protein Conformation medicine.medical_treatment Biology Industrial and Manufacturing Engineering Serine 03 medical and health sciences Meat tenderness Thrombin [SDV.IDA]Life Sciences [q-bio]/Food engineering medicine Food Quality Animals Muscle Skeletal chemistry.chemical_classification Protease serpins apoptosis General Medicine Trypsin serine protease inhibitors cell differentiation 030104 developmental biology Enzyme chemistry Biochemistry caspases bovine muscle MASP1 Food Science medicine.drug |
| Zdroj: | Critical Reviews in Food Science and Nutrition Critical Reviews in Food Science and Nutrition, Taylor & Francis, 2016, 56 (6), pp.957-972. ⟨10.1080/10408398.2012.741630⟩ |
| ISSN: | 1549-7852 1040-8398 |
| DOI: | 10.1080/10408398.2012.741630⟩ |
| Popis: | International audience; Since years, serine proteases and their inhibitors were an enigma to meat scientists. They were indeed considered to be extracellular and to play no role in postmortem muscle proteolysis. In the 1990's, we observed that protease inhibitors levels in muscles are a better predictor of meat tenderness than their target enzymes. From a practical point of view, we therefore choose to look for serine protease inhibitors rather than their target enzymes, i.e. serine proteases and the purpose of this report was to overview the findings obtained. Fractionation of a muscle crude extract by gel filtration revealed three major trypsin inhibitory fractions designed as F1 (Mr:50-70kDa), F2 (Mr:40-60kDa) and F3 (Mr:10-15kD) which were analyzed separately. Besides antithrombin III, an heparin dependent thrombin inhibitor, F1 and F2 comprised a large set of closely related trypsin inhibitors encoded by at least 8 genes bovSERPINA3-1 to A3-8 and able to inhibit also strongly initiator and effector caspases. They all belong to the serpin superfamily, known to form covalent complexes with their target enzymes, were located within muscle cells and found in all tissues and fluids examined irrespective of the animal species. Potential biological functions in living and postmortem muscle were proposed for all of them. In contrast to F1 and F2 which have been more extensively investigated only preliminary findings were provided for F3. Taken together, these results tend to ascertain the onset of apoptosis in postmortem muscle. However, the exact mechanisms driving the cell towards apoptosis and how apoptosis, an energy dependent process, can be completed postmortem remain still unclear. |
| Databáze: | OpenAIRE |
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