Fibrinolytic Serine Protease Isolation from <Emphasis Type="Italic">Bacillus amyloliquefaciens</Emphasis> An6 Grown on <Emphasis Type="Italic">Mirabilis jalapa</Emphasis> Tuber Powders |
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Authors: | Rym Agrebi Noomen Hmidet Mohamed Hajji Nawrez Ktari Anissa Haddar Nahed Fakhfakh-Zouari Moncef Nasri |
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Institution: | 1.Laboratoire de Génie Enzymatique et de Microbiologie,Ecole Nationale d’Ingénieurs de Sfax,Sfax,Tunisia |
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Abstract: | In this study, Mirabilis jalapa tuber powder (MJTP) was used as a new complex organic substrate for the growth and production of fibrinolytic enzymes by
a newly isolated Bacillus amyloliquefaciens An6. Maximum protease activity (1,057 U/ml) with casein as a substrate was obtained when the strain was grown in medium containing
(grams per liter) MJTP 30, yeast extract 6, CaCl2 1, K2HPO4 0.1, and K2HPO4 0.1. The strain was also found to grow and produce extracellular proteases in a medium containing only MJTP, indicating that
it can obtain its carbon, nitrogen, and salts requirements directly from MJTP. The B. amyloliquefaciens An6 fibrinase (BAF1) was partially purified, and fibrinolytic activity was assayed in a test tube with an artificial fibrin
clot. The molecular weight of the partially purified BAF1 fibrinolytic protease was estimated to be 30 kDa by sodium dodecyl
sulfate polyacrylamide gel electrophoresis and gel filtration. The optimum temperature and pH for the caseinolytic activity
were 60 °C and 9.0, respectively. The enzyme was highly stable from pH 6.0 to 11.0 and retained 62% of its initial activity
after 1 h incubation at 50 °C. However, the enzyme was inactivated at higher temperatures. The activity of the enzyme was
totally lost in the presence of phenylmethylsulfonyl fluoride, suggesting that BAF1 is a serine protease. |
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