2. Academic Validation
  3. Characterization of a novel protease from Aeribacillus pallidus strain VP3 with potential biotechnological interest

Characterization of a novel protease from Aeribacillus pallidus strain VP3 with potential biotechnological interest

  • Int J Biol Macromol. 2017 Jan;94(Pt A):221-232. doi: 10.1016/j.ijbiomac.2016.09.112.
Sondes Mechri 1,  Mouna Ben Elhoul Berrouina 1,  Maroua Omrane Benmrad 1,  Nadia Zaraî Jaouadi 1,  Hatem Rekik 1,  Emna Moujehed 1,  Alif Chebbi 2,  Sami Sayadi 2,  Mohamed Chamkha 2,  Samir Bejar 1,  Bassem Jaouadi 3
Affiliations

Affiliations

  • 1 Laboratory of Microbial Biotechnology and Engineering Enzymes, Centre of Biotechnology of Sfax, University of Sfax, Road of Sidi Mansour Km 6, P.O. Box 1177, Sfax 3018, Tunisia.
  • 2 Laboratory of Environmental Bioprocesses, LMI COSYS-Med, Centre of Biotechnology of Sfax, University of Sfax, Road of Sidi Mansour Km 6, P.O. Box 1177, Sfax 3018, Tunisia.
  • 3 Laboratory of Microbial Biotechnology and Engineering Enzymes, Centre of Biotechnology of Sfax, University of Sfax, Road of Sidi Mansour Km 6, P.O. Box 1177, Sfax 3018, Tunisia. Electronic address: [email protected].
PMID: 27720758 DOI: 10.1016/j.ijbiomac.2016.09.112
Abstract

The present study investigates the purification and physico-chemical characterization of an extracellular protease from the Aeribacillus pallidus strain VP3 previously isolated from a geothermal oil-field (Sfax, Tunisia). The maximum protease activity recorded after 22h of incubation at 45°C was 3000U/ml. Pure Enzyme, designated as SPVP, was obtained after ammonium sulfate fractionation (40-60%)-dialysis followed by heat-treatment (70°C for 30min) and UNO Q-6 FPLC anion-exchange chromatography. The purified Enzyme is a monomer of molecular mass about 29kDa. The sequence of the 25 NH2-terminal residues of SPVP showed a high homology with those of Bacillus proteases. The almost complete inhibition by PMSF and DIFP confirmed that SPVP is a member of serine protease family. Its optima of pH and temperature were pH 10 and 60°C, respectively. Its half-life times at 70 and 80°C were 8 and 4h, respectively. Its catalytic efficiency was higher than those of SAPCG, Alcalase Ultra 2.5L, and Thermolysin type X. SPVP exhibited excellent stability to detergents and wash performance analysis revealed that it could remove blood-stains effectively and high resistance against organic solvents. These properties make SPVP a potential candidate for applications in detergent formulations and non-aqueous peptide biocatalysis.

Keywords

Aeribacillus pallidus; Geothermal oil-field; Protease.

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