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1. Ben Elhoul  M, Zaraî Jaouadi  N, Rekik  H, Omrane Benmrad  M, Mechri  S, Moujehed  E, Kourdali  S, El Hattab  M, Badis  A, Bejar  S, Jaouadi  B,     ( 2016 )

Biochemical and molecular characterization of new keratinoytic protease from Actinomadura viridilutea DZ50.

International journal of biological macromolecules 92 (N/A)
PMID : 27387016  :   DOI  :   10.1016/j.ijbiomac.2016.07.009    
Abstract >>
A new extracellular thermostable keratinolytic protease, designated KERDZ, was purified and characterized from a thermophilic actinomycetes Actinomadura viridilutea DZ50 isolated from Algerian fishing port. The isolate exhibited high keratinase production when grown in chicken-feather meal media (18,000U/ml) after 96-h of incubation at 45�XC. The enzyme was purified by ammonium sulfate precipitation (35-55%)-dialysis and heat treatment (30min at 75�XC) followed by UNO S-1 FPLC cation exchange chromatography and size exclusion HPLC column. The biochemical characterizations carried on include physico-chemical determination and spectroscopic analysis. The MALDI-TOF/MS analysis revealed that the purified enzyme was a monomer with a molecular mass of 19536.10-Da. The sequence of the 25 N-terminal residues of KERDZ showed high homology with those of actinomycetes keratinases. Optimal activity was achieved at pH 11 and 80�XC. KERDZ was completely inhibited by PMSF and DFP suggested its belonging to the serine keratinase family. KERDZ displayed higher levels of hydrolysis and catalytic efficiency than bacterial keratinases (KERAK-29, Actinase E, and KERAB) and subtilisins (subtilisin Carlsberg and subtilisin Novo). The kerDZ gene encoding KERDZ was isolated and its DNA sequence was determined. These properties make KERDZ a potential, promising and eco-friendly alternative to the conventional chemicals used for industrial applications.
KeywordMeSH Terms
Homology modeling

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