Lipolytic isoenzymes from Euphorbia latex (original) (raw)
Related papers
Latex lipase of Euphorbia characias L.: An aspecific acylhydrolase with several isoforms
Plant Science, 2007
The objective of the present work was to contribute to the understanding of the physiological role of latex lipolytic activity in Euphorbia characias. To this end, the acid and basic lipolytic activity of E. characias latex, as well as the substrate specificity on various triacylglycerols, were measured during the plant's vegetative and reproductive stages. Both activities appeared to increase during the reproductive stage and to peak at the beginning of the vegetative stage, when new leaves and branches are formed. For the first time, the phospholipolytic and esterase activity of E. characias latex is also reported. An extraction method in aqueous medium with the zwitterionic detergent CHAPS was successfully used to extract lipolytic activity from latex. Extraction permitted the selective recovery of a single protein spot, with a molecular weight of 37 kDa, and presumably made of several acid isoforms which retained both lipolytic and phospholipolytic activity. The biochemical results suggest that lipolytic and phospholipolytic activity could depend on a single hydrolytic enzyme with several isoforms, equally expressed throughout the biological cycle of the plant. On the basis of the obtained results, we hypothesise that the E. characias latex lipase should be considered as an aspecific acylhydrolase with a combined lipase/phospholipase A activity. #
Journal of Applied Biosciences, 2017
Objective: The search for lipase with distinct features, from plant latex is of great importance for industrial applications. The catalytic properties of lipases from Ficus trichopoda and Euphorbia unispina latex were characterized. Methodology and Results: Fresh latex from Ficus trichopoda and Euphorbia unispina were collected and dried through solar. Dried latex was taken for complete proximate analysis and their activity was analysed by thin layer chromatography. The two lipases were optimally active at pH=5 and temperature of 35°C and 50°C for Ficus trichopoda and Euphorbia unispina latex, respectively. The presence of metal ions enhances the activity of Ficus trichopoda latex, while no significant enhancement was observed in the case of Euphorbia unispina latex. Both lipases were able to hydrolyze saturated esters, and showed typo-selectivity for this group. However, the lipases are weak selective for the hydrolysis of unsaturated esters, especially for 18:2 fatty acids. Conclusions and application of finding: The enzyme from Ficus trichopoda latex was able to attack specific oil to generate free fatty acids or ester as the major product. This understanding may help in devising efficient methods to produce valuable modified oils.
Journal of Applied Biosciences, 2017
Objective: The search for lipase with distinct features, from plant latex is of great importance for industrial applications. The catalytic properties of lipases from Ficus trichopoda and Euphorbia unispina latex were characterized. Methodology and Results: Fresh latex from Ficus trichopoda and Euphorbia unispina were collected and dried through solar. Dried latex was taken for complete proximate analysis and their activity was analysed by thin layer chromatography. The two lipases were optimally active at pH=5 and temperature of 35°C and 50°C for Ficus trichopoda and Euphorbia unispina latex, respectively. The presence of metal ions enhances the activity of Ficus trichopoda latex, while no significant enhancement was observed in the case of Euphorbia unispina latex. Both lipases were able to hydrolyze saturated esters, and showed typo-selectivity for this group. However, the lipases are weak selective for the hydrolysis of unsaturated esters, especially for 18:2 fatty acids. Conclusions and application of finding: The enzyme from Ficus trichopoda latex was able to attack specific oil to generate free fatty acids or ester as the major product. This understanding may help in devising efficient methods to produce valuable modified oils.
The involvement of amino acids in latex lipid synthesis in Euphorbia lathyris seedlings
Phytochemistry, 1984
The breakdown of triglycerides and proteins in the endosperm of Euphorbia luthyris was assayed in a 14 day germination period. Six days after germination, the average daily production was 2.7 pmol of amino acids. Arginine, glutamine, asparagine and glutamic acid accounted for 53 % of the total amino acids. Excised cotyledons with 1 cm hypocotyls were used for amino acid uptake and their involvement in terpenoid synthesis was studied. Glutamine and aspartate were hardly involved in apolar lipid synthesis. Leucine, isoleucine, valine and threonine were mainly incorporated into the triterpenes in the laticifers. Alanine and serine were also involved in phytosterol synthesis in the adjacent tissue. In the 14 day germination period, ca 3 y0 of the daily yield of latex triterpenes may be synthesized from a variety of amino acids.
Microorganisms
Lipases (EC 3.1.1.3) are hydrolases that catalyze triglycerides hydrolysis in free fatty acids and glycerol. Among the microorganisms that produce lipolytic enzymes, the entophytic fungi stand out. We evaluated 32 fungi of different genera, Pestalotiopsis, Aspergillus, Trichoderma, Penicillium, Fusarium, Colletotrichum, Chaetomium, Mucor, Botryodiplodia, Xylaria, Curvularia, Neocosmospora and Verticillium, isolated from Euterpe oleracea Mart. (Açaizeiro) from the Brazilian Amazon for lipase activity. The presence of lipase was evidenced by the deposition of calcium crystals. The endophytic Pestalotiopsis sp. (31) and Aspergillus sp. (24) with Pz 0.237 (++++) and 0.5 (++++), respectively, were the ones that showed the highest lipolytic activity in a solid medium. Lipase activity was rated in liquid medium, in a different range of temperatures (°C), pH and time (days). The values obtained in the production of lipase by the endophytic fungi were 94% for Pestalotiopsis sp. (31) and 93.8...
Plant latex lipase as biocatalysts for biodiesel production
African Journal of Biotechnology, 2016
Industrial-scale processes currently developed make use of chemical catalysis processes that are highly efficient but require very complex product purification steps. Enzymatic catalysis through plant lipases as biocatalysts is an alternative which, in contrast to chemical catalysis processes, appeared simple to perform, and can be done at low investment cost. Although microbial lipases have been extensively studied, little research has been focused on the use of plant lipases namely plant latex lipases. The present article outlines the most advanced knowledge concerning plant latex characterization in order to show how plant latex can be a promising alternative to catalyze transesterification for biodiesel production. This paper provides an overview regarding the main aspects of latex, such as the reactions catalyzed, physiological functions, specificities, sources and their industrial applications.
In Gel Detection of Lipase Activity in Crude Plant Extracts (Olea europaea)
BIO-PROTOCOL, 2015
Here, we provide a detailed protocol describing a SDS-PAGE based procedure to assay in gel neutral lipase activity. Total protein extracts are separated by SDS-PAGE and gels are treated with lipase substrate-α-naphthyl palmitate. This long-chain fatty acid ester is hydrolysed by lipases present in the gel. The product resulting from this reaction can be then visualized in the gel as yellowbrownish activity bands. This relatively simple and effective method of lipase assay detection can be used for crude protein extracts from different plant tissues. Materials and Reagents 16. Extraction buffer (see Recipes) 17. 12% separating gel (see Recipes) 18. 4% stacking gel (see Recipes)
Waste and Biomass Valorization, 2019
The present study investigates the biochemical characterization of an extracellular (phospho)lipase from a wood fungus Peziza sp. (medium optimization, inducer concentration and substrate specificity measurements). The strain was identified on the basis of ITS1/ITS4 primers. A 604 bp fragment was amplified by PCR and the obtained nucleotide sequence, showed 99% identity with the ITS region of isolates named as Peziza sp. Interestingly, Peziza sp. has both lipase and phospholipase activities with the same level which require both the presence of Ca 2+ and bile salts. Our result shows that the lipase hydrolyzes preferably the olive oil at 45 °C, pH 8. Whereas, the phospholipase activity was detected on pure PC at 45 °C, pH 9. Lipid extraction from dry biomass using chloroform/methanol (2/1) and quantitative measurement using electron microscope showed that intracellular triglycerides content was significantly high and reaches 20.88%. Gas chromatography analysis shows a majority of C18:1 (76, 98%) and C18:2 (9, 33%). Whereas, saturated fatty acids ranging C16-C20 represent only 11.5% of total lipids composition.
Aplica��o de lipases microbianas na obten��o de concentrados de �cidos graxos poliinsaturados
Quim Nova, 2003
Several polyunsaturated fatty acids (PUFA) belonging to the ômega 6 series, such as cis-6,9,12 γ-linolenic acid, as well as those of the ômega 3 series, such as cis-5,8,11,14,17-eicosapentaenoic acid and cis-4,7,10,13,16,19-docosahexaenoic acid are of considerable interest due to their nutritional and therapeutic properties. Methods used for the concentration of PUFA from natural sources include urea adduct formation, solvent winterization, supercritical fluid extraction and lipase-catalyzed reaction. Lipases are known to have little reactivity on PUFA and these acids can be enriched by selective hydrolysis, direct esterification of glycerol with PUFA and interesterification. Since lipase reactions are advantageous with respect to fatty acid, positional specificities and mild incubation condition, these enzymes are considered to be suitable for the production of PUFA concentrates for medical purposes.