Abstract
A neutral proteinase (NPS) was purified from the culture broth of Saccharomonospora canescens sp. novus, strain 5, using DEAE cellulose and a POROS HQ/M 4.6×100 mm column. The stability towards thermal and chemical (guanidine hydrochloride, Gdn.HCl) denaturation of NPS was investigated by kinetic and equilibrium studies. The unfolding processes were monitored by circular dichroism and fluorescence spectroscopy. The free energy of stabilization in water was calculated to be 2.1 kcal mol −1. The thermostability was determined by the critical temperature T c from fluorescence measurements (69°C) and the melting temperature T m (70°C) from (1) measurements. Quenching with acrylamide, iodide and cesium gives information about the microenvironment of intrinsic protein fluorophores. The K sv constant for NPS is 4.6 and classifies the emitting tryptophans as ‘buried’ in the hydrophobic interior of the investigated protein.
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