Jornal de Pesquisa e Desenvolvimento
Acesso livre

Abstrato

Purification and Characterization of a Protease from Green Seeded Chickpea (Cicer arientum)

Tooba Naz Shamsi, Priyankar Sen and Sadaf Fatima

Background: Proteases are ubiquitous in nature and are found to play a major role in biological functions like digestion of food, control of blood clotting, apoptosis and interaction of signalling receptors in animals.

Method: The protease was purified by soaking of sample, homogenization, ammonium sulphate precipitation and Ion-exchange chromatography on DEAE-cellulose column. Activity of protease was determined using Nα- benzoyl-DL-arginine-p-nitroanilide (BAPNA) as chromogenic substrate. The biochemical characterization was done for temperature stability, pH profile and effect of various inhibitors on enzymatic activity.

Results: We have purified a trypsin like protease of ~23 kDa from Cicer arientum, green chickpea seeds. The protease shows appreciable stability in wide range of pH and temperature.

Conclusion: To the best of our knowledge, it is first report on purification of protease with trypsin-like properties, from this source.