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Research Article


A Protease Isolated from the Latex of Plumeria rubra Linn (Apocynaceae) 1: Purification and Characterization

Indranil Chanda1*, Sanat Kumar Basu2, Sadhan Kumar Dutta3 and Smriti Rekha Chanda Das1

1Girijananda Chowdhury Institute of Pharmaceutical Science, Guwahati, Assam-781017, 2Department of Pharmaceutical Technology, Jadavpur University, Kolkata, West Bengal-700032, 3A College of Pharmacy, Bengal School of Technology, Hooghly, West Bengal- 712102, India.

For correspondence: E-mail: ichanda@sify.com  Tel: +91-9957179226

Received:  12 May 2011                                                Revised accepted: 15 October, 2011

Tropical Journal of Pharmaceutical Research, December 2011; 10(6): 705-711

http://dx.doi.org/10.4314/tjpr.v10i6.2  

Abstract

 

Purpose: To isolate, purify and characterize protease from the latex of the plant.

Methods: Protease was isolated from the latex of Plumeria rubra Linn using acetone precipitation method and purified by a sequence of DEAE cellulose column chromatography, followed by two successive column purification in Sephadex G-50 and Sephadex G-200. The molecular weight of the purified protease was determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The protease was given a trivial name, Plumerin-R.

Results: Plumerin-R showed a single protein band on SDS-PAGE and molecular weight was approximately 81.85 kDa. It remained active over a broad range of temperature but had optimum activity at 55 °C and pH 7.0 when casein was used as substrate. Activation of the protease by a thiol-activating agent indicated the presence of sulfhydryl as an essential group for its activity.

Conclusion: A protease from the latex of Plumeria rubra Linn was purified to homogeneity by a simple purification procedure and then characterized.

 

Keywords: Protease, Plumerin-R, Sulfhydryl, Purification; Characterization

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