Extração de esterase de fígado suíno (PLE)

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

A comparative study of protein and enzymatic activity in venoms of some common wasps (Hymenoptera: Vespidae) from São Paulo State

The Hymenoptera Aculeata venoms, with few exceptions, have been poorly studied and characterized. Nevertheless, they have raised increasing interest due to their medical importance, since accidents with these insects are fairly frequent in Brazil and may cause severe allergic reactions. The objectives of the present work were the quantitative characterization of the main allergenic enzymes present in the venom of the species Polybia paulista, Polybia ignobilis, Polistes simillimus, and Agelaia pallipes pallipes through biochemical assays for the determination of total protein content, as well as the level of the enzymatic activity of phospholipase, hyaluronidase, acid phosphatase and esterase. These results, in addition to providing biochemical knowledge about the venom of the species in question, also supply studies that allow phylogenetic inferences among them.

Characterization of esterase patterns in hepatopancreas of three species of Macrobrachium (Palaemonidae)

The genus Macrobrachium (Bate, 1868) belongs to the Palaemonidae family. These species are commonly found in lakes, floodplains and rivers in tropical and subtropical regions of South America. The Macrobrachium genus encompasses nearly 210 species of ecological and economic importance. In this study, three species of Macrobrachium (M acrobrachium jelskii, M acrobrachium amazonicum and M acrobrachium brasiliense) were studied in order to characterize the esterase patterns in the hepatopancreas, which were still unknown. Esterases are enzymes which catalyze the hydrolysis of esters. In the hepatopancreas, these enzymes play important roles in several metabolic processes involved in some functions of this organ, such as detoxification and digestion. Twelve esterase bands (EST1 to EST12) were detected in these species, and a comparison among them showed no qualitative differences in interspecific bands, or between males and females. Inhibitors were used to classify the esterase bands. The results indicated seven acetylesterases, two carboxylesterases, one arylesterase, and one cholinesterase. The EST11 band was not detected in these procedures because of its lower frequency. Statistical analyses showed no variability among the species, in either interspecific or intraspecific assays. These results support the hypothesis of a high evolutionary conservation of esterases in the hepatopancreas of these crustaceans. The data enabled us to assess the genetic structure of these species through the use of esterasic enzymes. It also contributes to our knowledge about the biology of these poorly studied species. Knowledge on the genetic structure of populations and species are essential when defining priorities for their management and conservation. © 2012 Elsevier Ltd.

Biomass-to-bio-products application of feruloyl esterase from Aspergillus clavatus

The structural polysaccharides contained in plant cell walls have been pointed to as a promising renewable alternative to petroleum and natural gas. Ferulic acid is a ubiquitous component of plant polysaccharides, which is found in either monomeric or dimeric forms and is covalently linked to arabinosyl residues. Ferulic acid has several commercial applications in food and pharmaceutical industries. The study herein introduces a novel feruloyl esterase from Aspergillus clavatus (AcFAE). Along with a comprehensive functional and biophysical characterization, the low-resolution structure of this enzyme was also determined by small-angle X-ray scattering. In addition, we described the production of phenolic compounds with antioxidant capacity from wheat arabinoxylan and sugarcane bagasse using AcFAE. The ability to specifically cleave ester linkages in hemicellulose is useful in several biotechnological applications, including improved accessibility to lignocellulosic enzymes for biofuel production. © 2012 Springer-Verlag Berlin Heidelberg.

Adaptabilidade diferencial das variantes moleculares slow e fast da esterase-5 de Drosophila mulleri

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Isolamento de fungos termofílicos produtores de celulases, xilanases e ferruloil esterase para bioconversão de bagaço de cana de açúcar em açúcares fermentescíveis

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Activity of some isoenzymatic systems in stored coffee grains

Considering the worldwide consumption of coffee, it is natural that throughout the history many people have dedicated the research to markers that contribute somehow on gauging its quality. This research aimed to evaluate the biochemical performance of arabica coffee during storage. Coffee in beans (natural) and in parchment (pulped) dried in concrete terrace and in dryer with heated air were packed in jute bags and stored in not controlled environmental conditions. Enzymatic activities of superoxide dismutase, catalase, peroxidase, polyphenoloxidase, esterase and lipoxygenase in coffee grains were evaluated at zero, three, six, nine and twelve months by means of electrophoresis. Independently of the drying method, the activity of isoenzymatic complexes highlighted deteriorative processes in stored grains of coffee. The treatments 60/40º C and 60º C used to reduce the water content imposed a greater stress condition, accelerated metabolism of natural coffee in the storage with decreased activity of defense mechanisms due to latent damage in these grains. Natural coffees are more sensible to high drying temperatures and its quality reduces faster than pulped coffee in the storage.

Endophytic fungi producing of esterases: evaluation in vitro of the enzymatic activity using pH indicator

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)