Isolation and characterization of a surfactant-stable protease from halophilic bacteria Chromohalobacter Japonicus BK-AB18
The protease from Chromohalobacter japonicus BK-AB18 was produced by growing bacteria in a LB medium containing 5% casein and 5% NaCl. The crude protease was partially purified by three levels of ammonium sulfate concentration (ranges of 0–70%, 70–75% and 75–80%) and the highest specific activity...
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| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Penerbit Universiti Kebangsaan Malaysia
2020
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| Online Access: | http://journalarticle.ukm.my/16022/1/49_02_06.pdf http://journalarticle.ukm.my/16022/ http://www.mabjournal.com/index.php?option=com_content&view=article&id=1003&catid=59:current-view&Itemid=56 |
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| Summary: | The protease from Chromohalobacter japonicus BK-AB18 was produced by growing bacteria in a LB medium containing
5% casein and 5% NaCl. The crude protease was partially purified by three levels of ammonium sulfate concentration (ranges
of 0–70%, 70–75% and 75–80%) and the highest specific activity was exhibited in the range of 75–80%. The enzyme has a
relative molecular weight of 65 kDa. The protease in this fraction had the highest activity in the following optimum conditions:
7.5% NaCl, a pH of 9.0 and a temperature of 45°C. The activity of the enzyme at the optimum pH and temperature was
enhanced by the addition of a Ca2+ ion, but its activity was significantly inhibited by EDTA, hence this enzyme is included as
metalloenzyme. Interestingly, the protease activity increased when exposed to a concentration of 0.01% and 0.05% SDS, and
was relatively stable in this solution up to a concentration of 10%. It is thus demonstrated that C. japonicus BK-AB18 is a
potential source to produce extracellular protease that can be applied in the surfactant/detergent industry. |
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