2Chemical Faculty, Lomonosov Moscow State University, 119992 Moscow, Russia; fax: (495) 939-3188; E-mail: firstname.lastname@example.org
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Received February 13, 2008; Revision received February 27, 2008
Biochemical properties of Bacillus intermedius subtilisin-like proteinase (AprBi) secreted by a B. subtilis recombinant strain in the early and late stationary phases of growth have been determined. Protein structure was analyzed and its stability estimated. It was noted that the enzyme corresponding to different phases of bacterial growth retains activity in the presence of reducing and oxidizing agents (C2H5OH and H2O2). Different effects of bivalent metal ions on activity of two proteinase fractions were found. Calcium ions more efficiently activate proteinase secreted in the late stationary phase. Unlike the first enzyme fraction, the second forms catalytically active dimers.
KEY WORDS: subtilisin-like proteinase, AprBi, dimers