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  • Protease inhibitor from Moringa oleifera with potential for use as therapeutic drug and as seafood preservative.

Protease inhibitor from Moringa oleifera with potential for use as therapeutic drug and as seafood preservative.

Saudi journal of biological sciences (2011-07-01)
B Bijina, Sreeja Chellappan, Jissa G Krishna, Soorej M Basheer, K K Elyas, Ali H Bahkali, M Chandrasekaran
ABSTRACT

Protease inhibitors are well known to have several applications in medicine and biotechnology. Several plant sources are known to return potential protease inhibitors. In this study plants belonging to different families of Leguminosae, Malvaceae, Rutaceae, Graminae and Moringaceae were screened for the protease inhibitor. Among them Moringa oleifera, belonging to the family Moringaceae, recorded high level of protease inhibitor activity after ammonium sulfate fractionation. M. oleifera, which grows throughout most of the tropics and having several industrial and medicinal uses, was selected as a source of protease inhibitor since so far no reports were made on isolation of the protease inhibitor. Among the different parts of M. oleifera tested, the crude extract isolated from the mature leaves and seeds showed the highest level of inhibition against trypsin. Among the various extraction media evaluated, the crude extract prepared in phosphate buffer showed maximum recovery of the protease inhibitor. The protease inhibitor recorded high inhibitory activity toward the serine proteases thrombin, elastase, chymotrypsin and the cysteine proteases cathepsin B and papain which have more importance in pharmaceutical industry. The protease inhibitor also showed complete inhibition of activities of the commercially available proteases of Bacillus licheniformis and Aspergillus oryzae. However, inhibitory activities toward subtilisin, esperase, pronase E and proteinase K were negligible. Further, it was found that the protease inhibitor could prevent proteolysis in a commercially valuable shrimp Penaeus monodon during storage indicating the scope for its application as a seafood preservative. This is the first report on isolation of a protease inhibitor from M. oleifera.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Thrombin from bovine plasma, lyophilized powder, ≥2,000 NIH units/mg protein (E1%/280 = 19.5)
Sigma-Aldrich
Protease from Aspergillus oryzae, ≥500 U/g