Details

Autor(en) / Beteiligte

• Mohammd, Taghreed U.
• Farhan, Layla O.
• Dawood, Ashgan S.
• Hasan, Bushra F.

Titel

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

Ist Teil von

• Oriental journal of chemistry, 2017, Vol.33 (5), p.2676-2680

Ort / Verlag

Bhopal: Oriental Scientific Publishing Company

Erscheinungsjahr

2017

Quelle

EZB Electronic Journals Library

Beschreibungen/Notizen

• 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 .