Mohammed Gagaoua
Institut national de la recherche agronomique
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Publication
Featured researches published by Mohammed Gagaoua.
Journal of Integrative Agriculture | 2016
Mohammed Gagaoua; E M C Terlouw; D. Micol; J-F Hocquette; Aidan P. Moloney; Karin Nuernberg; D Bauchart; Abdelghani Boudjellal; Nigel D. Scollan; R I Richardson; Brigitte Picard
Abstract The present study compared eight breeds of cattle differing in gender (heifers, bulls and steers) to determine associations between muscle characteristics and meat sensory qualities of the Longissimus thoracis muscle. Animal types differed in all the muscle characteristics and sensory qualities. Many correlations among muscle characteristics and among sensory qualities were consistent for most animal types. Isocitrate dehydrogenase (ICDH) activities allowed discrimination of muscles with respect to myosin heavy chain (MyHC)-I proportions for all animal types. Lactate dehydrogenase (LDH) and phosphofructokinase (PFK) activities were positively correlated for most animal types. Overall liking was correlated with beef flavour and abnormal flavour in all animal types and with global tenderness for all animal types except for Charolais cross breed steers. For all animal types except for Angus×Friesian heifers, beef flavour and abnormal flavour were negatively correlated. Overall liking was not correlated with juiciness. PFK, ICDH and citrate synthase (CS) activities were strongly associated with tenderness, beef flavour and overall liking when average values for all animal types were used. However, associations between muscle characteristics and sensory qualities within animal types were weak and inconsistent.
International Journal of Biological Macromolecules | 2015
Mohammed Gagaoua; Naouel Hoggas; Kahina Hafid
The present work describes for the first time an elegant non-chromatographic method, the three phase partitioning for the purification and recovery of zingibain, a milk-clotting enzyme, from Zingiber officinale rhizomes. Factors affecting partitioning efficiency such as (NH4)2SO4 saturation, crude extract to t-butanol ratio and pH on zingibain partitioning were investigated. Optimal purification parameters were 50% (NH4)2SO4 saturation with 1.0:1.0 ratio of crude extract:t-butanol at pH 7.0, which gave 14.91 purification fold with 215% recovery of zingibain. The enzyme was found to be exclusively partitioned in the aqueous phase. The enzyme showed a prominent single band on SDS-PAGE. It is a monomeric protein of 33.8 kDa and its isoelectric point is 4.38. The enzyme exhibited maximal proteolytic activity at a temperature of 60 °C and pH 7.0. It was found to be stable at 40-65 °C during 2 h. The enzyme was found to be highly stable against numerous metal ions and its activity was enhanced by Ca(2+), K(+) and Na(+). It was completely inhibited by heavy metal ions such as Cu(2+) and Hg(2+) and partially by Cd(+). Zingibain milk-clotting activity (MCA) was found to be highly stable when stored under freezing (-20 °C) for 30 days compared at 4 °C.
Foods | 2017
Amel Ait Kaki El-Hadef El-Okki; Mohammed Gagaoua; Hayat Bourekoua; Kahina Hafid; Leila Bennamoun; Shahrazed Djekrif-Dakhmouche; Mohamed El-Hadef El-Okki; Zahia Meraihi
A new thermostable α-amylase from Rhizopus oryzae FSIS4 was purified for first time and recovered in a single step using a three-phase partitioning (TPP) system. The fungal α-amylase, at a concentration of 1.936 U per kg of flour, was used in bread-making and compared to the commercial enzyme. The results showed a significant effect of the recovered α-amylase in the prepared bread and allowed us to improve the quality of the bread. The study indicated clearly that the recovered α-amylase is a potential candidate for future applications in the bread-making industry and in other food biotechnology applications.
Journal of Agricultural and Food Chemistry | 2017
Mohammed Gagaoua; Sébastien Couvreur; Guillain Le Bec; Ghislain Aminot; Brigitte Picard
This study investigated the relationships among a list of 23 protein biomarkers with CIE-L*a*b* meat color traits and ultimate pH on Longissimus thoracis (LT) and Rectus abdominis (RA) muscles of 48 protected designation of origin Maine-Anjou cows. The technological parameters were correlated with several biomarkers and were in some cases muscle-dependent. More biomarkers were related to pHu in LT than in RA muscle. Some consistencies were found, by the common correlation of pHu with MyHC-IIa and MyHC-IIx. The pHu of the LT muscle was also correlated with other cytoskeletal entities and proteins belonging to metabolism and cellular stress. In contrast to the relationships found between biomarkers and LT pHu, more proteins were related to the instrumental color coordinates in RA than in LT muscle. The regression equations were parameter- and muscle-dependent. Certain of the retained proteins explained more than one color coordinate. Hsp70-Grp75 was positive in the models of L*, a*, b*, and C* of LT and of b* in the RA muscle. Further heat shock proteins were strongly related with the meat color coordinates in both muscles. The involvement of metabolic enzymes and myofibrillar proteins in the meat color development was also verified in this experiment. This study confirmed once again the importance of numerous biological pathways in beef color.
Applied Biochemistry and Biotechnology | 2015
Mohammed Gagaoua; Kahina Hafid; Yasmine Boudida; Samira Becila; Ahmed Ouali; Brigitte Picard; Abdelghani Boudjellal; Miguel Angel Sentandreu
In living cells, after activation, protein inhibitors constitute the last step of proteases activity regulation. This review intends to provide original information about a group of bovine muscle serine proteases inhibitors belonging to the Serpin superfamily and characterized at the gene and protein level. This report is the only one and the first to provide much information on this group of proteases inhibitors of the serpin type and their potential biological functions. Amongst the eight genes identified in bovine, three serpins were purified from the muscle tissue and characterized. These are two members of the bovSERPINA3 family, i.e., bovSERPINA3-1 and A3-3, and the last one is antithrombin III (AT-III or BovSERPINC1). BovSERPINA3 family comprises at least eight protein members encoded by different genes mapped on chromosome 7q23–q26 cluster. BovSERPINA3-1 and A3-3 were shown to locate within muscle cells and are cross-class inhibitors strongly active against trypsin as well as against human initiator and effector caspases 8 and 3. They constitute a key apoptosis control in mammals. They were thus expressed in proliferating and confluent myoblasts phases where cells must be alive but not in myotubes. Antithrombin III inhibits trypsin and, in a heparin dependent manner, thrombin. AT-III and its mRNA were expressed in muscle cells and in differentiating primary myoblasts in culture.
Meat Science | 2017
Mohammed Gagaoua; E.M. Claudia Terlouw; Brigitte Picard
This study investigates relationships between 21 biomarkers and meat color traits of Longissimus thoracis muscles of young Aberdeen Angus and Limousin bulls. The relationships found allowed to propose metabolic processes underlying meat color. The color coordinates were related with several biomarkers. The relationships were in some cases breed-dependent and the variability explained in the regression models varied between 31 and 56%. The correlations between biomarkers and color parameters were sometimes opposite between breeds. The PCA using the 21 biomarkers and the instrumental color coordinates showed that these variables discriminated efficiently between the two studied breeds. Results are coherent with earlier studies on other beef breeds showing that several proteins belonging to different but partly related biological pathways involved in muscle contraction, metabolism, heat stress and apoptosis are related to beef color. The results suggest that in future, biomarkers may be used to classify meat cuts sampled early post-mortem according to their forthcoming color.
Meat Science | 2016
Mohammed Gagaoua; D. Micol; Brigitte Picard; Claudia Terlouw; Aidan P. Moloney; H. Juin; Karine Meteau; Nigel D. Scollan; Ian Richardson; Jean-François Hocquette
Eating quality of the same meat samples from different animal types cooked at two end-point cooking temperatures (55°C and 74°C) was evaluated by trained panels in France and the United Kingdom. Tenderness and juiciness scores were greater at 55°C than at 74°C, irrespective of the animal type and location of the panel. The UK panel, independently of animal type, gave greater scores for beef flavour (+7 to +24%, P<0.001) but lower scores for abnormal flavour (-10 to -17%, P<0.001) at 74°C. Abnormal flavour score by the French panel was higher at 74°C than at 55°C (+26%, P<0.001). Irrespective of the data set, tenderness was correlated with juiciness and beef flavour. Overall, this study found that cooking beef at a lower temperature increased tenderness and juiciness, irrespective of the location of the panel. In contrast, cooking beef at higher temperatures increased beef flavour and decreased abnormal flavour for the UK panelists but increased abnormal flavour for the French panel.
Biosensors Journal | 2016
Mohammed Gagaoua; Kahina Hafid
A rapid overview of the Three Phase Partitioning (TPP) system as an efficient non-chromatographic tool is given. This elegant non-chromatographic tool is able to purify numerous proteins and especially proteases in a one step protocol. TPP is able to do not only purify proteins, but also concentrate them into one of the phases and enhance their proteolytic activity. The application of TPP for the extraction and purification of plant milk-clotting enzymes and meat tenderizers agents are given. In addition, some proteases from other materials are summarized. This short communication stress showed that TPP is a simple, economical and quick method for proteases recovery from plant proteases. This elegant non-chromatographic tool may be performed in a purification process to be used successfully in food industries, namely to provide enzymes for cheese-making and meat tenderizing.
PLOS ONE | 2016
Malek Kammoun; Brigitte Picard; Thierry Astruc; Mohammed Gagaoua; Denise Aubert; Muriel Bonnet; Véronique Blanquet; Isabelle Cassar-Malek
Even though abundance of Hsp27 is the highest in skeletal muscle, the relationships between the expression of HspB1 (encoding Hsp27) and muscle characteristics are not fully understood. In this study, we have analysed the effect of Hsp27 inactivation on mouse development and phenotype. We generated a mouse strain devoid of Hsp27 protein by homologous recombination of the HspB1 gene. The HspB1-/- mouse was viable and fertile, showing neither apparent morphological nor anatomical alterations. We detected a gender dimorphism with marked effects in males, a lower body weight (P < 0.05) with no obvious changes in the growth rate, and a lower plasma lipids profile (cholesterol, HDL and triglycerides, 0.001 < P< 0.05). The muscle structure of the animals was examined by optical microscopy and transmission electron microscopy. Not any differences in the characteristics of muscle fibres (contractile and metabolic type, shape, perimeter, cross-sectional area) were detected except a trend for a higher proportion of small fibres. Different myosin heavy chains electrophoretic profiles were observed in the HspB1-/- mouse especially the presence of an additional isoform. Electron microscopy revealed ultrastructural abnormalities in the myofibrillar structure of the HspB1-/- mouse mutant mice (e.g. destructured myofibrils and higher gaps between myofibrils) especially in the m. Soleus. Combined with our previous data, these findings suggest that Hsp27 could directly impact the organization of muscle cytoskeleton at the molecular and ultrastructural levels.
Proteome | 2016
Brigitte Picard; Malek Kammoun; Mohammed Gagaoua; Christiane Barboiron; Bruno Meunier; Christophe Chambon; Isabelle Cassar-Malek
Hsp27—encoded by HspB1—is a member of the small heat shock proteins (sHsp, 12–43 kDa (kilodalton)) family. This protein is constitutively present in a wide variety of tissues and in many cell lines. The abundance of Hsp27 is highest in skeletal muscle, indicating a crucial role for muscle physiology. The protein identified as a beef tenderness biomarker was found at a crucial hub in a functional network involved in beef tenderness. The aim of this study was to analyze the proteins impacted by the targeted invalidation of HspB1 in the Tibialis anterior muscle of the mouse. Comparative proteomics using two-dimensional gel electrophoresis revealed 22 spots that were differentially abundant between HspB1-null mice and their controls that could be identified by mass spectrometry. Eighteen spots were more abundant in the muscle of the mutant mice, and four were less abundant. The proteins impacted by the absence of Hsp27 belonged mainly to calcium homeostasis (Srl and Calsq1), contraction (TnnT3), energy metabolism (Tpi1, Mdh1, PdhB, Ckm, Pygm, ApoA1) and the Hsp proteins family (HspA9). These data suggest a crucial role for these proteins in meat tenderization. The information gained by this study could also be helpful to predict the side effects of Hsp27 depletion in muscle development and pathologies linked to small Hsps.