La lipase est une enzyme contenue dans certaines sécrétions des organes de la digestion tels que le pancréas ou l’intestin, et dans le sang. La lipase transforme les graisses alimentaires en acides gras et alcool (ce que l’on appelle la lipolyse).
Le dithiothreitol (DTT) est le nom usuel d’une petite molécule redox également connue sous le nom de réactif de Cleland ou DTT, en abrégé.
Nous publions cette information pour insister très modestement, sans aucune ambition scientifique, sur le champ presque infini des recherches des alternatives aux phytosanitaires pour contrôler ce ravageur.
08:00 EDT 13th September 2017 | BioPortfolio
Home » Topics » Mergers & Acquisitions » Research » Lipase Activity in the Larval Midgut of Rhynchophorus palmarum: Biochemical Characterization and the Effects of Reducing Agents.
Summary of « Lipase Activity in the Larval Midgut of Rhynchophorus palmarum: Biochemical Characterization and the Effects of Reducing Agents. »
Lipases have key roles in insect lipid acquisition, storage, and mobilization and are also fundamental to many physiological processes in insects. Lipids are an important component of insect diets, where they are hydrolyzed in the midgut lumen, absorbed, and used for the synthesis of complex lipids. The South American palm weevil Rhynchophorus palmarum is one of the most important pests on commercial palm plantations. However, there are few studies about lipid digestion for this insect. In this work, we have described the biochemical characterization of the lipase activity in the posterior midgut of the R. palmarum palm weevil. Lipase activity was highest between the temperatures of 37 °C and 45 °C and at pH 6.5. Lipase activity was also sensitive to variations in salt and calcium concentrations. Lipases have been described structurally as enzymes with the Ser-His-Asp Catalytic Triad, containing an active serine. The serine protease inhibitor PMSF (phenylmethane sulfonyl fluoride) inhibited the lipases from R. palmarum, demonstrating the importance of a serine residue for this activity. The ability of the lipases to hydrolyze p-Nitrophenyl esters with different chain lengths has revealed the activities of a broad range of substrates. The lipase activities of R. palmarum increased in the presence of reduced glutathione (GSH) and dithiothreitol (DTT), while in the presence of oxidized glutathione (GSSG), activities were drastically reduced. To our knowledge, this study has provided the first information about lipase activity in the R. palmarum palm weevil.