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Moncef Nasri - One of the best experts on this subject based on the ideXlab platform.

  • Recovery and physicochemical properties of smooth hound (Mustelus Mustelus) skin gelatin
    LWT - Food Science and Technology, 2012
    Co-Authors: Ali Bougatef, Rafik Balti, Assaâd Sila, Rim Nasri, Ghada Graiaa, Moncef Nasri
    Abstract:

    Gelatin was extracted from the skin of smooth hound after pre-treatment with acetic and citric acids. The addition of smooth hound crud acid protease (SHCAP) at a level of 15 Units/g alkaline treated skin resulted in an increase yields of gelatin. The hydroxyproline yields of gelatins extracted for 24 h with acetic acid and with SHCAP were 17.34% and 56.82%, respectively. While the serine content recorded for the smooth hound skin gelatin (SHSG) extracted with SHCAP was higher than that of halal bovine gelatin (HBG) (36 versus 29 residues per 1000 residues), hydroxyproline and proline (202 residues per 1000 residues) contents were slightly lower (219 residues per 1000 residues). The gel strength of the gelatin gel from SHSG (211 g) was lower than that of HBG (259 g) (p < 0.05). Compared to HBG (p < 0.05), SHSG was noted to exhibit lower emulsifying, foaming, and fat-binding properties but similar emulsifying stability. SDS-PAGE revealed that SHSG showed high band intensity for the major protein components, especially α- and β-components, which was comparable to that of standard calf skin collagen type I. In conclusion gelatin extracted from smooth hound skin has good quality and can be used in the food industries.

  • evidence of in vivo satietogen effect and control of food intake of smooth hound Mustelus Mustelus muscle protein hydrolysate in rats
    Journal of Functional Foods, 2010
    Co-Authors: Ali Bougatef, Rozenn Ravallec, Naima Nedjararroume, Ahmed Barkia, Didier Guillochon, Moncef Nasri
    Abstract:

    Abstract Protein hydrolysates are of a significant interest, due to their potential application as a source of bioactive peptides in nutraceutical and pharmaceutical domains. The present study was focused on the effect of protein hydrolysate from smooth hound (Mustelus Mustelus) (SHPH) in the regulation of components of the food intake control such as satiety. SHPH was produced by intestinal digestive proteases from the same species. The amino acid analysis by GC/MS showed that the hydrolysate was rich in leucine, alanine, glycine, threonine, serine, lysine and glutamate. The molecular weights of peptides in SHPH were estimated by ESI-MS to be between 200 and 2500 Da. Biological in vivo capacities of SHPH in rats were evaluated by determination of the CCK-like peptides and insulin content using a clinical human radioimmunoassay. The food intake and the body weight of rats were measured during the period of treatment. Rats treated with SHPH showed a significant decrease in body weight at the end of treatment, as well as a decrease of food intake. Our findings revealed a possible mechanism of the beneficial effects of SHPH in appetite regulation, and this might be important to prevent the risk of a number of medical conditions including type II diabetes.

  • antioxidant and free radical scavenging activities of smooth hound Mustelus Mustelus muscle protein hydrolysates obtained by gastrointestinal proteases
    Food Chemistry, 2009
    Co-Authors: Ali Bougatef, Rafik Balti, Mohamed Hajji, Imen Lassoued, Yosra Trikiellouz, Moncef Nasri
    Abstract:

    Abstract We have investigated the antioxidative activity of five hydrolysates from smooth hound ( Mustelus Mustelus ) meat obtained by various gastrointestinal proteases: crude enzyme extract, low molecular weight (LMW) alkaline protease and trypsin-like protease from M. Mustelus intestine, pepsin from M. Mustelus stomach, and bovine trypsin. The antioxidant activities of the different smooth hound protein hydrolysates (SHPHs) were evaluated using various in vitro antioxidant assays, such as 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical-scavenging activity, reducing power, total antioxidant capacity, lipid peroxidation inhibition in rat liver homogenate and β-carotene bleaching assay. The five hydrolysates showed different degrees of hydrolysis and varying degrees of antioxidant activity. The hydrolysate produced by the LMW protease generally showed a greater antioxidative activity as indicated by all the methods considered. The IC 50 values (the concentration of antioxidant substance removing 50% of DPPH radical) for DPPH and lipid peroxidation were found to be 0.6 ± 0.01 and 1.1 ± 0.06 mg/ml, respectively. Moreover, LMW protease hydrolysate exhibited notable reducing power and strong total antioxidant capacity. The protein hydrolysate produced by the LMW protease was then fractionated by size exclusion chromatography on a Sephadex G-25 into three major fractions ( F 1 – F 3 ). Fraction F 3 , with molecular weight lower than 3500 Da, was found to display a high antioxidant activity than F 1 (12,200 Da) and F 2 (molecular weights between 6500 and 12,200 Da). The amino acid analysis by GC/MS showed that F 3 was rich in histidine, methionine, tyrosine, leucine, Isoleucine, glycine, and arginine.

  • pepsinogen and pepsin from the stomach of smooth hound Mustelus Mustelus purification characterization and amino acid terminal sequences
    Food Chemistry, 2008
    Co-Authors: Ali Bougatef, Rafik Balti, Saida Ben Zaied, Nabil Souissi, Moncef Nasri
    Abstract:

    Abstract Pepsinogen from the stomach of smooth hound ( Mustelus Mustelus ) was purified to homogeneity by 20–70% ammonium sulphate precipitation, Sephadex G-100 gel filtration and DEAE-cellulose anion exchange chromatography with a 9.4-fold increase in specific activity and 38.36% recovery. Upon activation at pH 2.0, M. Mustelus pepsinogen was converted to active form in one-step pathway. Molecular weights of the purified pepsinogen and the active pepsin were estimated to be 40,000 and 35,000 Da using SDS-PAGE and gel filtration, respectively. The optimum pH and temperature for the pepsin activity were pH 2.0 and 40 °C, respectively, using haemoglobin as a substrate. Activity was completely inhibited by Pepstatin A but not by phenylmethylsulphonyl fluoride, a serine-protease inhibitor and ethylenediaminetetraacetic acid, a metalloenzyme inhibitor. The N-terminal amino acid sequences of the first 15 amino acids of the activation segment of the pepsinogen and the first 20 amino acids of the active pepsin were LLRVPLRKGKSTLDV and ATEPLSNYLDSSYFGDISIG, respectively. M. Mustelus pepsinogen, which showed high homology to rat C pepsinogen, had Thr-Leu-Asp sequence at amino acid positions 12–14 not found in all pepsinogen sequences. A remarkable substitution was found in the activation segment of M. Mustelus pepsinogen: the Arg-13 conserved in all gastric proteinases, whose sequences are known, is replaced by Leu-13.

Ali Bougatef - One of the best experts on this subject based on the ideXlab platform.

  • Valorisation of smooth hound (Mustelus Mustelus) waste biomass through recovery of functional, antioxidative and antihypertensive bioactive peptides
    Environmental Science and Pollution Research, 2016
    Co-Authors: Nadhem Sayari, Rafik Balti, Assaâd Sila, Anissa Haddar, Semia Ellouz-chaabouni, Ali Bougatef
    Abstract:

    Concerns over the environmental and waste disposal problems created by the large amounts of by-products generated from fish processing industries are increasing worldwide. The bioconversion of those marine waste by-products through the enzymatic hydrolysis of their protein content offers the possibility for the development of bioactive peptides for use in various biotechnological applications. The present study aimed to investigate and evaluate the biological and functional properties of smooth hound ( Mustelus Mustelus ) protein hydrolysates (SHPHs) obtained by treatment with intestinal and gastric enzyme preparations from M. Mustelus viscera and porcine pancreatin. The results revealed that the SHPHs exhibited different degrees of hydrolysis and antioxidant activity. The hydrolysate produced by the intestinal crude extract presented the highest rate of antioxidative activity, showing an IC_50 value of 1.47 ± 0.07 mg/mL in 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging assays. The alkaline protease extract from the intestine of M. Mustelus produced hydrolysate with the highest angiotensin I-converting enzyme (ACE) inhibitory activity (82 ± 1.52 % at 2 mg/mL). All the protein hydrolysates showed excellent solubility and interfacial properties that were governed by pH. The major amino acids detected in SHPHs were glutamic acid/glutamine, aspartic acid/asparagine, histidine and arginine, followed by methionine, phenylalanine, serine, valine and leucine. Overall, the results indicated that smooth hound by-products can be used to generate high value-added products, thus offering a valuable source of bioactive peptides for application in wide range of biotechnological and functional food applications.

  • Recovery and physicochemical properties of smooth hound (Mustelus Mustelus) skin gelatin
    LWT - Food Science and Technology, 2012
    Co-Authors: Ali Bougatef, Rafik Balti, Assaâd Sila, Rim Nasri, Ghada Graiaa, Moncef Nasri
    Abstract:

    Gelatin was extracted from the skin of smooth hound after pre-treatment with acetic and citric acids. The addition of smooth hound crud acid protease (SHCAP) at a level of 15 Units/g alkaline treated skin resulted in an increase yields of gelatin. The hydroxyproline yields of gelatins extracted for 24 h with acetic acid and with SHCAP were 17.34% and 56.82%, respectively. While the serine content recorded for the smooth hound skin gelatin (SHSG) extracted with SHCAP was higher than that of halal bovine gelatin (HBG) (36 versus 29 residues per 1000 residues), hydroxyproline and proline (202 residues per 1000 residues) contents were slightly lower (219 residues per 1000 residues). The gel strength of the gelatin gel from SHSG (211 g) was lower than that of HBG (259 g) (p < 0.05). Compared to HBG (p < 0.05), SHSG was noted to exhibit lower emulsifying, foaming, and fat-binding properties but similar emulsifying stability. SDS-PAGE revealed that SHSG showed high band intensity for the major protein components, especially α- and β-components, which was comparable to that of standard calf skin collagen type I. In conclusion gelatin extracted from smooth hound skin has good quality and can be used in the food industries.

  • evidence of in vivo satietogen effect and control of food intake of smooth hound Mustelus Mustelus muscle protein hydrolysate in rats
    Journal of Functional Foods, 2010
    Co-Authors: Ali Bougatef, Rozenn Ravallec, Naima Nedjararroume, Ahmed Barkia, Didier Guillochon, Moncef Nasri
    Abstract:

    Abstract Protein hydrolysates are of a significant interest, due to their potential application as a source of bioactive peptides in nutraceutical and pharmaceutical domains. The present study was focused on the effect of protein hydrolysate from smooth hound (Mustelus Mustelus) (SHPH) in the regulation of components of the food intake control such as satiety. SHPH was produced by intestinal digestive proteases from the same species. The amino acid analysis by GC/MS showed that the hydrolysate was rich in leucine, alanine, glycine, threonine, serine, lysine and glutamate. The molecular weights of peptides in SHPH were estimated by ESI-MS to be between 200 and 2500 Da. Biological in vivo capacities of SHPH in rats were evaluated by determination of the CCK-like peptides and insulin content using a clinical human radioimmunoassay. The food intake and the body weight of rats were measured during the period of treatment. Rats treated with SHPH showed a significant decrease in body weight at the end of treatment, as well as a decrease of food intake. Our findings revealed a possible mechanism of the beneficial effects of SHPH in appetite regulation, and this might be important to prevent the risk of a number of medical conditions including type II diabetes.

  • antioxidant and free radical scavenging activities of smooth hound Mustelus Mustelus muscle protein hydrolysates obtained by gastrointestinal proteases
    Food Chemistry, 2009
    Co-Authors: Ali Bougatef, Rafik Balti, Mohamed Hajji, Imen Lassoued, Yosra Trikiellouz, Moncef Nasri
    Abstract:

    Abstract We have investigated the antioxidative activity of five hydrolysates from smooth hound ( Mustelus Mustelus ) meat obtained by various gastrointestinal proteases: crude enzyme extract, low molecular weight (LMW) alkaline protease and trypsin-like protease from M. Mustelus intestine, pepsin from M. Mustelus stomach, and bovine trypsin. The antioxidant activities of the different smooth hound protein hydrolysates (SHPHs) were evaluated using various in vitro antioxidant assays, such as 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical-scavenging activity, reducing power, total antioxidant capacity, lipid peroxidation inhibition in rat liver homogenate and β-carotene bleaching assay. The five hydrolysates showed different degrees of hydrolysis and varying degrees of antioxidant activity. The hydrolysate produced by the LMW protease generally showed a greater antioxidative activity as indicated by all the methods considered. The IC 50 values (the concentration of antioxidant substance removing 50% of DPPH radical) for DPPH and lipid peroxidation were found to be 0.6 ± 0.01 and 1.1 ± 0.06 mg/ml, respectively. Moreover, LMW protease hydrolysate exhibited notable reducing power and strong total antioxidant capacity. The protein hydrolysate produced by the LMW protease was then fractionated by size exclusion chromatography on a Sephadex G-25 into three major fractions ( F 1 – F 3 ). Fraction F 3 , with molecular weight lower than 3500 Da, was found to display a high antioxidant activity than F 1 (12,200 Da) and F 2 (molecular weights between 6500 and 12,200 Da). The amino acid analysis by GC/MS showed that F 3 was rich in histidine, methionine, tyrosine, leucine, Isoleucine, glycine, and arginine.

  • pepsinogen and pepsin from the stomach of smooth hound Mustelus Mustelus purification characterization and amino acid terminal sequences
    Food Chemistry, 2008
    Co-Authors: Ali Bougatef, Rafik Balti, Saida Ben Zaied, Nabil Souissi, Moncef Nasri
    Abstract:

    Abstract Pepsinogen from the stomach of smooth hound ( Mustelus Mustelus ) was purified to homogeneity by 20–70% ammonium sulphate precipitation, Sephadex G-100 gel filtration and DEAE-cellulose anion exchange chromatography with a 9.4-fold increase in specific activity and 38.36% recovery. Upon activation at pH 2.0, M. Mustelus pepsinogen was converted to active form in one-step pathway. Molecular weights of the purified pepsinogen and the active pepsin were estimated to be 40,000 and 35,000 Da using SDS-PAGE and gel filtration, respectively. The optimum pH and temperature for the pepsin activity were pH 2.0 and 40 °C, respectively, using haemoglobin as a substrate. Activity was completely inhibited by Pepstatin A but not by phenylmethylsulphonyl fluoride, a serine-protease inhibitor and ethylenediaminetetraacetic acid, a metalloenzyme inhibitor. The N-terminal amino acid sequences of the first 15 amino acids of the activation segment of the pepsinogen and the first 20 amino acids of the active pepsin were LLRVPLRKGKSTLDV and ATEPLSNYLDSSYFGDISIG, respectively. M. Mustelus pepsinogen, which showed high homology to rat C pepsinogen, had Thr-Leu-Asp sequence at amino acid positions 12–14 not found in all pepsinogen sequences. A remarkable substitution was found in the activation segment of M. Mustelus pepsinogen: the Arg-13 conserved in all gastric proteinases, whose sequences are known, is replaced by Leu-13.

Simo N Maduna - One of the best experts on this subject based on the ideXlab platform.

Edward D. Farrell - One of the best experts on this subject based on the ideXlab platform.

  • historical biogeography of smoothhound sharks genus Mustelus of southern africa reveals multiple dispersal events from the northern hemisphere
    Systematics and Biodiversity, 2020
    Co-Authors: Simo N Maduna, Edward D. Farrell, Jessica J. Boomer, Sabine P Wintner, Ilaria A M Marino, Carlotta Mazzoldi, Lorenzo Zane, Kelvin L Hull, Ana Verissimo, Mikhail V Chesalin
    Abstract:

    Members of the smoothhound shark genus Mustelus display a widespread distribution pattern across ocean basins with a high degree of sub-regional endemism. The patterns and processes that resulted i...

  • new molecular tools for the identification of 2 endangered smooth hound sharks Mustelus Mustelus and Mustelus punctulatus
    Journal of Heredity, 2015
    Co-Authors: Ilaria A M Marino, Edward D. Farrell, Emilio Riginella, Alessia Cariani, Fausto Tinti, Carlotta Mazzoldi, Lorenzo Zane
    Abstract:

    The smooth-hounds represent a significant proportion of the elasmobranch catch in the Adriatic basin of the Mediterranean Sea, where the common (Mustelus Mustelus) and blackspotted (Mustelus punctulatus) smooth-hounds co-occur. The 2 species share several morphological and morphometric characters that lead to frequent misidentification. In order to provide information useful for their species identification, we performed a morphological identification of several Mustelus specimens to select individuals unambiguously attributed to 1 of the 2 species, and assayed these with 3 new molecular tests. First, we developed and validated a mitochondrial DNA assay based on species-specific amplification of the cytochrome c oxidase subunit 1 (COI). Second, a fragment analysis of 15 microsatellites cross-amplified from several triakid species was performed to identify diagnostic loci. Finally, a length difference was identified in the internal transcribed spacer 2 (ITS2) region and a diagnostic test based on its amplification was established. All the samples classified morphologically as M. Mustelus and M. punctulatus showed a species-specific profile using all the 3 molecular tests. In addition, cross-amplification of microsatellites allowed identification of 9 highly polymorphic loci that will be useful for the study of the mating system and population differentiation of the 2 species.

  • age and growth estimates for the starry smoothhound Mustelus asterias in the northeast atlantic ocean
    Ices Journal of Marine Science, 2010
    Co-Authors: Edward D. Farrell, Stefano Mariani, Maurice Clarke
    Abstract:

    This is a pre-copy-editing, author-produced PDF of an article accepted for publication in ICES Journal of Marine Science following peer review. The definitive publisher-authenticated version Farrell, E. D., Mariani, S., and Clarke, M. W. 2010. Age and growth estimates for the starry smoothhound (Mustelus asterias) in the Northeast Atlantic Ocean. – ICES Journal of Marine Science, 67: 931–939 is available online at: http://icesjms.oxfordjournals.org/content/67/5/931

  • A simple genetic identification method for Northeast Atlantic smoothhound sharks (Mustelus spp.)
    Ices Journal of Marine Science, 2009
    Co-Authors: Edward D. Farrell, Maurice Clarke, Stefano Mariani
    Abstract:

    Farrell, E. D., Clarke, M. W., and Mariani, S. 2009. A simple genetic identification method for Northeast Atlantic smoothhound sharks (Mustelus spp.). - ICES Journal of Marine Science, 66: 561-565.Considerable ambiguity exists in the identification of the commercially valuable smoothhound sharks (Mustelus spp.) in the Northeast (NE) Atlantic. The lack of a clear and accurate method of identification prevents the collation of reliable species-specific landings and survey data for these fish and hinders the accurate delineation of the distribution ranges of species and stock boundaries, making it impossible to apply sound species-specific conservation and management strategies. This paper reports on the development of a multiplex PCR reaction that utilizes a set of mtDNA primers for the identification of Mustelus asterias, Mustelus Mustelus, and Galeorhinus galeus. The high throughput method allows for the rapid and cost-effective identification of large numbers of samples; its application to 431 fish collected between 2006 and 2008 also raises important questions regarding the biogeography of the genus Mustelus in the NE Atlantic.

A Bestervan Der E Merwe - One of the best experts on this subject based on the ideXlab platform.