Accéder directement au contenu Accéder directement à la navigation
Article dans une revue

Purification and characterization of a 33 kDa extracellular proteinase from Microsporum cookei

Abstract :

ObjectiveAn extracellular proteinase synthesized by the geophilic dermatophyte Microsporum cookei has been purified and characterized. Material and methods The soil isolate of M. cookei was cultivated in modified Czapek-Dox liquid medium containing 0.1% bacteriological peptone and 1% glucose as the nitrogen and carbon sources. Purification of the proteinase was accomplished by (NH4)2SO4 precipitation, followed by ion-exchange chromatography. Results Analysis of the enzyme by SDS-PAGE revealed a single polypeptide chain with an apparent molecular mass of 33 kDa. A keratinolytic activity was evidenced for the enzyme by the keratin azure test. The inhibition profile and the good activity of the enzyme towards the synthetic substrate N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide suggested that it belongs to the subtilisin group of serine proteinases. Conclusion The keratinolytic properties of M. cookei suggest that this fungus may be an alternative for the recycling of industrial keratinic wastes.

Type de document :
Article dans une revue
Liste complète des métadonnées

https://hal.univ-angers.fr/hal-03134639
Contributeur : Okina Université d'Angers <>
Soumis le : lundi 8 février 2021 - 14:27:08
Dernière modification le : jeudi 29 avril 2021 - 11:24:05

Identifiants

Collections

Citation

Hossein Moallaei, F. Zaini, S. Rezaei, Jean-Philippe Bouchara, Gérald Larcher. Purification and characterization of a 33 kDa extracellular proteinase from Microsporum cookei. Journal of Medical Mycology / Journal de Mycologie Médicale, Elsevier Masson, 2011, 21 (4), pp.241 - 247. ⟨10.1016/j.mycmed.2011.09.004⟩. ⟨hal-03134639⟩

Partager

Métriques

Consultations de la notice

32