作者: O. A. Stepnaya , L. P. Ryazanova , V. I. Krupyanko , I. S. Kulaev
关键词: Endopeptidase 、 Lysostaphin 、 Xanthomonas campestris 、 Biochemistry 、 Extracellular 、 Streptomyces albus 、 Enzyme 、 Biology 、 Streptomyces globisporus 、 Muramidase
摘要: Interactions of a negatively charged exopolysaccharide Xanthomonas campestris IBPM 124 with its extracellular enzymes (muramidase, endopeptidase, and neutral phosphatase) also egg lysozyme, lysostaphin, muramidase Streptomyces globisporus, bacteriolytic enzyme complex albus were studied. All these positively under the conditions their maximal activity. It was shown that interaction acidic from X. changed kinetic parameters. The change either positive (increase in reaction rate) or negative (decrease depended on type substrate cleaved. Due to such interactions, secreted by into environment not only retained transported exoenzymes near-cellular space, but regulated