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Production and partial characterization of extracellular proteinases from <Emphasis Type="Italic">Streptomyces malaysiensis</Emphasis>, isolated from a Brazilian cerrado soil
Authors:Email author" target="_blank">Rodrigo?P?NascimentoEmail author  Claudia?M?d’Avila-Levy  Rodrigo?F?Souza  Marta?H?Branquinha  Elba?P?S?Bon  Nei?Pereira-Jr  Rosalie?R?R?Coelho
Institution:(1) Dep. Microbiologia Geral, Instituto de Microbiologia Prof. Paulo de Góes, CCS, Universidade Federal do Rio de Janeiro (UFRJ), CEP, 21941-590 Rio de Janeiro, Brazil;(2) Dep. Bioquímica, Instituto de Química, CT, UFRJ, Brazil;(3) Escola de Química, CT, UFRJ, Brazil
Abstract:Streptomyces malaysiensis AMT-3, isolated from a Brazilian cerrado soil, showed proteolytic activities detected by gelatin–sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The optimum proteinase production was obtained when using 2.5% wheat bran and 0.1% yeast extract in the culture medium, after 5 days incubation at 30°C. The enzymatic complex degraded gelatin optimally at pH 7.0, and under these conditions eight proteolytic bands (four serine-proteinases and four metaloproteinases), ranging from 20 to 212 kDa, were detected on the culture supernatant filtrates. In addition, a 35-kDa proteinase was thermostable at 60°C for 120 min. These results point out to the applicability of gelatin zymograms in the characterization of crude enzymatic complexes. According to our results, this enzymatic complex could be used for biotechnological applications.
Keywords:Streptomyces malaysiensis            Thermostable proteinase  Enzyme characterization  Wheat bran
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