Purification and characterization of a subtilisin-like proteinases secreted in the stationary growth phase of Bacillus amyloliquefaciens H2 |
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Authors: | N. P. Balaban L. A. Malikova A. M. Mardanova G. N. Rudenskaya M. R. Sharipova |
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Affiliation: | (1) Biological and Soil Science Faculty, Kazan State University, ul. Kremlevskaya 18, 420008 Kazan, Russia;(2) Chemical Faculty, Lomonosov Moscow State University, 119899 Moscow, Russia |
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Abstract: | Proteinases secreted during the early and late stationary phases have been isolated from the culture liquid of Bacillus amyloliquefaciens H2 using CM-cellulose ion-exchange chromatography with subsequent FPLC on a Mono S column. Considering the character of hydrolysis of specific chromogenic substrates and the type of inhibition, these enzymes were identified as subtilisin-like proteinases. The molecular weight of both proteinases is 29 kD. The proteolytic activity of the proteinases secreted during the early and late stationary phases towards the synthetic substrate Z-Ala-Ala-Leu-pNA was maximal at pH 8.5 and 9.0, respectively. The maximal activity of both proteinases was observed at 37 degrees C, and the proteins were stable within the pH range of 7.2-9.5. The subtilisin-like proteinases from B. amyloliquefaciens were shown to catalyze synthesis of peptide bonds. |
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Keywords: | subtilisin-like proteinases Bacillus amyloliquefaciens purification properties |
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