Partial characterization of acid protease from Galactites tomentosa flowers
- Laboratiore de Biologie et Environment, Faculté des Sciences de la Nature et de la vie, Université 1 Mentouri, Constantine, Algeria.
- Laboratore de of Génetique Biochimie et Biotechnologies végétales, Faculté des Sciences de la Nature et de la vie, Université 1 Mentouri, Constantine, Algeria.
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Abstract
A plant aspartic protease from Galactites tomentosa Moench was purified 15,47 fold by salt precipitation then by size-exclusion chromatography.. The enzyme is an acid protease with optimum pH of 4. The optimal temperature for enzyme activity was 40°C and the half-life at 60°C was 21,6 min. The activity versus of the substrate concentration gave a hyperbolic curve, indicating a Michaelis kinetics. The KM calculated from Lineweaver–Burk plot is 3,47g/l when casein was used as substrate. The enzyme inhibition of 100% by pepstatin and on non-inhibition by EDTA and iodoacetamide proved it to be an aspartate protease. SDS–PAGE plus casein showed a single active zone and indicated an estimated molecular mass of 45 kDa.
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Malika Benkahoul, Meriem Benchiheub, Ines Bellil, Douadi Khelifi, Aicha Mechakra Maza (2015); Partial characterization of acid protease from Galactites tomentosa flowers , Int. J. of Adv. Res., 3 (08), 368-376, ISSN 2320-5407.
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