Les Inscriptions à la Bibliothèque sont ouvertes en
ligne via le site: https://biblio.enp.edu.dz
Les Réinscriptions se font à :
• La Bibliothèque Annexe pour les étudiants en
2ème Année CPST
• La Bibliothèque Centrale pour les étudiants en Spécialités
A partir de cette page vous pouvez :
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Détail de l'indexation
M006210
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Ouvrages de la bibliothèque en indexation M006210
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Etude de l'hydrolyse enzymatique de la chitine irradiée par des chitinases extraites de la biomasse marine / Maya Dziril Ep. Ouslimane
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Titre : Etude de l'hydrolyse enzymatique de la chitine irradiée par des chitinases extraites de la biomasse marine Type de document : texte imprimé Auteurs : Maya Dziril Ep. Ouslimane, Auteur ; Grib, Hocine, Directeur de thèse Editeur : [S.l.] : [s.n.] Année de publication : 2010 Importance : 107 f. Présentation : ill. Format : 30 cm. Accompagnement : 1 CD-ROM. Note générale : Mémoire de Magister : Génie de l'Environnement : Alger, Ecole Nationale Polytechnique : 2010
Bibliogr. f. 80 - 97. Annexes f. 98 - 107Langues : Français (fre) Mots-clés : Chitinase
Dépolymérisation partielle de la chitine
Oligomères et monomèresIndex. décimale : M006210 Résumé : L’objectif visé dans ce travail est l’extraction, la purification et la caractérisation de la chitinase en vue de son utilisation pour l’hydrolyse de la chitine préalablement irradiée par les rayons γ du Co-60. La production d’une chitinase brute à partir de la biomasse marine, ainsi que son utilisation dans des conditions opératoires préalablement déterminées, afin d’hydrolyser la matière chitineuse ont été atteintes. L’extrait enzymatique a été purifié par précipitation au sulfate d’ammonium (20%-90%), suivie d’un fractionnement par chromatographie d’exclusion moléculaire et enfin par ultrafiltration. Ces techniques de purification ont permis d’atteindre une activité spécifique d’environ 567 U/mg, avec un facteur de purification de 8.34. Le poids moléculaire de la chitinase a été estimé à 21 kDa. Les conditions optimales de température et de pH de la chitinase partiellement purifiée sont respectivement de 50°C et pH 4. L’enzyme reste stable sur une gamme de pH allant de 3 à 6. Pour un temps d’incubation de 1 h, l’enzyme reste stable pour une température inférieure à 50°C. Au-delà, elle perd près de 62% de son activité à 60°C et la totalité à 80°C. L’activité de la chitinase est stimulée par CuSO4 et fortement inhibée par AgNO3. L’irradiation à la dose de 210 kGy à un débit de dose de 47 Gy/min a permis une réduction jusqu'à 90% du poids moléculaire de la chitine, atteignant ainsi un PM de 11 kDa. La dépolymérisation partielle de la chitine, grâce au prétraitement par irradiation γ, a donc permis une amélioration de l’activité chitinasique. Ainsi, le couplage d’une action physique (irradiation) à l’action enzymatique nous a permis d’augmenter le taux de production des oligomères et monomères obtenus à partir de la chitine. Etude de l'hydrolyse enzymatique de la chitine irradiée par des chitinases extraites de la biomasse marine [texte imprimé] / Maya Dziril Ep. Ouslimane, Auteur ; Grib, Hocine, Directeur de thèse . - [S.l.] : [s.n.], 2010 . - 107 f. : ill. ; 30 cm. + 1 CD-ROM.
Mémoire de Magister : Génie de l'Environnement : Alger, Ecole Nationale Polytechnique : 2010
Bibliogr. f. 80 - 97. Annexes f. 98 - 107
Langues : Français (fre)
Mots-clés : Chitinase
Dépolymérisation partielle de la chitine
Oligomères et monomèresIndex. décimale : M006210 Résumé : L’objectif visé dans ce travail est l’extraction, la purification et la caractérisation de la chitinase en vue de son utilisation pour l’hydrolyse de la chitine préalablement irradiée par les rayons γ du Co-60. La production d’une chitinase brute à partir de la biomasse marine, ainsi que son utilisation dans des conditions opératoires préalablement déterminées, afin d’hydrolyser la matière chitineuse ont été atteintes. L’extrait enzymatique a été purifié par précipitation au sulfate d’ammonium (20%-90%), suivie d’un fractionnement par chromatographie d’exclusion moléculaire et enfin par ultrafiltration. Ces techniques de purification ont permis d’atteindre une activité spécifique d’environ 567 U/mg, avec un facteur de purification de 8.34. Le poids moléculaire de la chitinase a été estimé à 21 kDa. Les conditions optimales de température et de pH de la chitinase partiellement purifiée sont respectivement de 50°C et pH 4. L’enzyme reste stable sur une gamme de pH allant de 3 à 6. Pour un temps d’incubation de 1 h, l’enzyme reste stable pour une température inférieure à 50°C. Au-delà, elle perd près de 62% de son activité à 60°C et la totalité à 80°C. L’activité de la chitinase est stimulée par CuSO4 et fortement inhibée par AgNO3. L’irradiation à la dose de 210 kGy à un débit de dose de 47 Gy/min a permis une réduction jusqu'à 90% du poids moléculaire de la chitine, atteignant ainsi un PM de 11 kDa. La dépolymérisation partielle de la chitine, grâce au prétraitement par irradiation γ, a donc permis une amélioration de l’activité chitinasique. Ainsi, le couplage d’une action physique (irradiation) à l’action enzymatique nous a permis d’augmenter le taux de production des oligomères et monomères obtenus à partir de la chitine. Exemplaires
Code-barres Cote Support Localisation Section Disponibilité Spécialité Etat_Exemplaire M006210A M006210 Papier Bibliothèque centrale Mémoire de Magister Disponible M006210B M006210 Papier Bibliothèque centrale Mémoire de Magister Disponible Documents numériques
DZIRIL OUSLIMANE.Maya.pdfURL