Abstract

Leucine Aminopeptidase from Arachis hypogaea L. Seeds Partial Purification and Characterization

Taghreed U. Mohammd¹Layla O. Farhan²Ashgan S. Dawood² and Bushra F. Hasan²

DOI : http://dx.doi.org/10.13005/ojc/330567

Abstract:

Leucine aminopeptidases (LAP; EC 3.4.11.1) constitute a diverse set of exopeptidases that catalyze the hydrolysis of leucine residues from the amino-terminal of protein or peptide substrates , (LAP) are present in animals, plants, and microbes . In this study, leucine aminopeptidase was purified Partial from Arachis hypogaea seeds by using gel filtration chromatography Sephadex G-100. The enzyme was purified 3.965 fold with a recovery of 29.4%. Its pH and temperature optimum were(8.7) and (37˚C), respectively. The results show novel properties of LAP from Arachis hypogaeaL. or peanut. The Km value for LAP (77 mM) , with Vmax (1538 mmole min ^-1). We recommend a separate isoenzyme of the enzyme (LAP)from Arachishypogaeaon L. peanut seeds and study the kinetic qualities of each of them .

Keywords:

Leucine amionpeptidase (LAP); Arachis hypoaea L. seeds; Purification

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