Peptide synthesis catalysed by a haloalkaliphilic serine protease from the archaeon Natrialba magadii (Nep).

摘要: Aims:  Haloarchaeal proteases function optimally in high salt (low water activity); thus, they offer an advantage over the nonhalophilic counterparts as biocatalysts for protease-catalysed peptide synthesis. The haloalkaliphilic archaeon Natrialba magadii secretes a solvent-tolerant protease, Nep (Natrialba extracellular protease). In this work, ability of to catalyse synthesis was examined. Methods and Results:  tripeptide Ac-Phe-Gly-Phe-NH2 synthesized using Ac-Phe-OEt Gly-Phe-NH2 substrates building blocks presence Nep, 30% (v/v) dimethyl sulfoxide (DMSO) 1·5 or 0·5 mol l−1 NaCl. Purification identification product achieved by RP-HPLC ESI-MS, respectively. native well recombinant enzyme produced Haloferax volcanii (HvNep) similarly effective catalysts model with yields up 60% without secondary hydrolysis product. HvNep catalysed various tripeptides preference those having aromatic amino acids P1 site. Conclusion:  is able under different concentrations DMSO. Significance Impact Study:  catalytic property combined overproduction protease Hfx. volcanii anticipates potential applicability haloarchaeal biotechnology.