Monday, May 5, 2008
6-10

Jatropha curcas L. seed lipase study

J.S. Sousa1, E.D.C Cavalcanti1, M.L.E. Gutarra1, Donato A.G. Aranda2, and Denise M.G. Freire3. (1) Biochemistry - Chemistry Institute, Universidade Federal do Rio de Janeiro, Av. Athos da Silveira Ramos, 149 - Bloco A, Lab 541, Cidade Universitária, Rio de Janeiro, Brazil, (2) Escola de Química, Universidade Federal do Rio de Janeiro, Cidade Universitária, Centro de Tecnologia, Bloco E, Sala 207, Rio De Janeiro, 21941-909, Brazil, (3) Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil

Lipases are a group of enzymes defined as carboxylesterases able to carry out the ester bond hydrolysis in long chain acylglycerols. They generally act in the organic aqueous interface and acylglycerols are their natural substrates. Vegetable lipases, found in a great deal in nature and at a low cost, can be employed in an advantageous way for the enrichment or isolation of a fatty acid kind or class.
We investigated the catalytic lipase potential in germinated physic nut seed [acetone (AP), crude (CP) and lyophilized crude (LCP) powders] and dormant (DAP).  In this research, substrate hydrolysis rates were analyzed (vegetable oils and lipid) under several reaction conditions. The germinated seeds enzyme showed great activity in pH 8.0 at 400C. The AP hydrolyzed satisfactorily (>76%) all the evaluated substrates, except castor bean oil (23%), showing the soy oil the best result (97%), within two hours reaction. CP and LCP showed good conversion rates of soy oil (92% and 87%, respectively).
DAP did not show a significant hydrolytic activity. AP electrophoretic study showed only band in the zymogram and it did not present significant catalytic activity differences facing different chain size substrates (112U/g for tributyrin, 80U/g for trycaprylin and 100U/g for olive oil).  Preliminary results showed that the AP of physic nut lipase was able to carry out the esters synthesis, revealing the biotechnological potential of this enzyme.