AI Article Synopsis
- Alkaline serine protease was isolated from a thermophilic, alkaliphilic strain using ammonium sulphate precipitation and ion exchange chromatography, achieving a purification level of 16.5-fold with an activity of 6900 U/mg.
- The enzyme displayed optimal activity against casein at pH 8.0 and 80 °C, and remained stable in these conditions for up to 2 hours.
- Calcium and manganese ions enhanced its activity, while various metals like zinc and mercury decreased it; also, PMSF inhibited the enzyme, but 2-mercaptoethanol doubled its activity, and it was stable in common surfactants and detergents.
Article Abstract
Alkaline serine protease was purified to homogeneity from culture supernatant of a thermophilic, alkaliphilic sp. by 80% ammonium sulphate precipitation followed by CM-cellulose and DEAE-cellulose ion exchange column chromatography. The enzyme was purified up to 16.5-fold with 6900 U/mg activity. The protease exhibited maximum activity towards casein at pH 8.0 and at 80 °C. The enzyme was stable at pH 8.0 and 80 °C temperature up to 2 h. The Ca and Mn enhanced the proteolytic activity up to 44% and 36% as compared to control, respectively. However, Zn, K, Ba , Co , Hg and Cu significantly reduced the enzyme activity. PMSF (phenyl methyl sulphonyl fluoride) completely inhibited the protease activity, whereas the activity of protease was stimulated up to two folds in the presence of 5 mM 2-mercaptoethanol. The enzyme was also stable in surfactant (Tween-80) and other commercial detergents (SDS, Triton X-100).
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6299798 | PMC |
| http://dx.doi.org/10.1016/j.jgeb.2015.01.002 | DOI Listing |
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