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@article{S_S_V_2011, title={Screening of alkalophilic thermophilic protease isolated from <em>Bacillus</em> RV.B2.90 for Industrial applications}, volume={2}, url={https://www.updatepublishing.com/journal/index.php/rib/article/view/2356}, abstractNote={Protease enzyme from Bacillus RV.B2.90 was purified, fractionated and tested for various applications. This enzyme could degrade the natural proteins like coagulated egg and blood clot. Blood and natural pigment stain (carrot, beetroot, green leaves, coffee and tea) were removed by this enzyme easily. It exhibited good compatibility with the commercial detergents such as Surf Excel, Tide, Ujala, Ariel and Rin. The keratinolytic<br />activity of the enzyme was evidenced by the complete degradation of feathers. X-ray films treated with the enzyme showed release of protein from the gelatin coating, a pre requisite for recovery of silver. Also showed better stability with surfactants and solvents, which will be advantageous as detergent formulations containing chelating agents like EDTA and in peptide synthesis. The partially purified enzyme showed direct hydrolysis of various natural proteins (BSA, casein and azocasein) applied to clean glass slides followed by denaturation by boiling. Bacillus RV.B2.90 immobilization with 3% alginate showed maximum production (2002 U/ml). In continuous production, the beads were stable over 24 hrs X 9 cycles. RV.B2.90 protease highly thermostable and alkalophilic with a variety of activities, has great potential for application in a wide range of industry.}, number={3}, journal={Research in Biotechnology}, author={S, Vijayalakshmi and S, Venkatkumar and V, Thankamani}, year={2011}, month={Jun.} }