Abstract
Individual serine proteinases were isolated from various microbial sources using affinity chromatography, and characterized. It is suggested that microbial serine proteinase might be classified as follows: 1. Subtilisin family, including subfamilies of a) secretory subtilisins (B. subtilis, B. amyloliquefaciens, B. licheniformis, B. thuringiensis), b) intracellular serine proteinases from the same strains, c) SH- containing serine proteinases (Thermoactinomyces vulgaris); 2. Chymotrypsin-like serine proteinases found only in actinomycetes (Str. griseus). Intracellular serine proteinase from B. amyloliquefaciens efficiently splits peptide and denatured protein substrates, but can perform only limited hydrolysis of native proteins thus differing from homologous secretory subtilisins. It is suggested that this feature is of functional importance in the regulation of the enzyme action on proteins within the cell.
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