%0 Journal Article
%T Biochemical characterization of phosphatase,   -galactosidase and   -mannosidase activities of seeds of an oleaginous cucurbit: Lagenaria siceraria (Molina) Standl blocky-fruited cultivar
%A D Koffi
%A B Faule
%A J Gonnety
%A M B¨¦dikou
%A L Kouam¨¦
%A I Zoro
%A S Niamk¨¦
%J Sciences & Nature
%D 2010
%I 
%X Seeds extract of Lagenaria siceraria (Molina) Standl (blocky-fruited cultivar) was screened for enzymatic hydrolytic activities over synthetic variety and natural substrates. The best hydrolytic activities mainly consisted of phosphatase (0.68 ¡À 0.02 UI/mg), ¦Â-galactosidase (0.26 ¡À 0.03 UI/mg) and ¦Á -mannosidase (0.17 ¡À 0.02 UI/mg). Physicochemical characterization showed that these enzymatic activities were maximal at 55¡ãC in sodium acetate buffer (pHs 4.6 and 5.6). They showed pH and temperature stability and appeared to be resistant in the presence of 5 mM cations (Na+, K+, Ca2+, Ba2+ and Mg2+) concentration and 1% (w/v) detergents (cationic, non-ionic and anionic). The phosphatase activity on different phosphorylated substrates showed it ability to hydrolyze greatly para-nitrophenylphosphate (100 ¡À 2.3%) and ATP (95.3 ¡À 2.6%) and in lesser extent sodium phytate (15.2 ¡À 1.8%). As for natural substrates as lactose and the three different mannobioses linked (¦Á -1,2; ¦Á -1,3 ¦Á -1,6), that were significantly hydrolyzed by ¦Â-galactosidase and ¦Á -mannosidase activity respectively. These interesting characteristics deserved to be deeply investigated for the valorisation of Lagenaria siceraria seeds phosphatase, ¦Â -galactosidase and ¦Á -mannosidase in potential biotechnological applications.
%U http://www.ajol.info/index.php/scinat/article/view/59966