106 resultados para feruloyl esterase

em Repositório Institucional UNESP - Universidade Estadual Paulista "Julio de Mesquita Filho"


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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.

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

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Four population samples of Haematobia irritans (horn flies), collected from farms and subjected, or not, to insecticide control, were: analysed as to esterase bands by polyacrylamide gel electrophoresis. Eight esterase bands were detected in this species, a low number when compared with flies of other genera. The reduced number of esterase variants of H. irritans is attributed to their parasitic behaviour and blood-dependence for food. Unlike other fly species whose esterase bands exhibit affinity to both alpha- and beta-naphthyl acetates, the esterases in H. irritans seem to be of a single kind, all preferentially hydrolysing a-naphthyl. The four populations were very similar as to esterase bands. In relation to the frequencies of patterns resulting from combining bands, Nova Alianca and Birigui were more alike than the other two populations. Inhibitors were used in an attempt to classify five of the esterase bands. The results indicate one acetylcholinesterase, two acetylesterases and two carboxylesterases.

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

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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Esterases are a group of enzymes that are reportedly associated with acaricide resistance in Riphicephallus (Boophilus) microplus. A comparative analysis was made of the esterase patterns in malathion and deltamethrin-sensitive, tolerant and resistant tick groups, using non-denaturing polyacrylamide gel electrophoresis. Electrophoretical profiles revealed four bands of esterase activity against alpha-naphthyl acetate; which were dubbed EST-1 to EST-4. The EST-3 and EST-4 were detected in all strains and were classified as carboxylesterases (CaEs). The EST-2, classified as an acetylcholinesterase (AChE), was detected in all groups, but its staining intensity increased from susceptible to resistant groups, indicating an altered production according to the degree of resistance. EST-1, which was also classified as an AChE, was detected exclusively in tolerant and resistant groups to both acaricides, but displayed greater activity in the malathion-resistant group. These data suggest that these AChEs may represent an important detoxification strategy developed to overcome the effects of acaricides. (C) 2008 Elsevier B.V. All rights reserved.

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

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

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The esterase patterns of sixteen strains from four species in the saltans subgroup were analyzed using polyacrylamide gel electrophoresis. Thirty-four esterase bands were detected. By using alpha and beta naphthyl acetates as substrates, they were classified in 18 alpha-esterases (they hydrolyse the alpha-naphtyl substrate), 15 beta-esterases (they hydrolyse the beta-naphtyl substrate) and 1 alpha/beta-esterase (it hydrolyses the alpha and beta-naphtyl substrates). Among the alpha-esterases, three were detected exclusively in males. Malathion, Eserine and pCMB were used as inhibitors in order to characterize biochemically the esterases. The results indicated the presence of cholinesterases, carboxylesterases and acetylesterases. The degree of mobility of the bands in the gels, their specificity to alpha and beta naphthyl acetates and the results of the inhibition tests allowed us to recognize tentatively nine genetic loci. Phylogenetic relationships among species inferred on the basis of the esterase patterns by PAUP 4.0 b8, with neighbor-joining search and a bootstrap analysis showed that, although the four species are closely related, D. septentriosaltans, D. saltans and D. austrosaltans are closer to each other than to D. prosaltans. These results showed to be consistent with phylogenetic relationships previously inferred from inversion polymorphism.

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Several fitness components in strains of Drosophila mulleri carrying the slow or the fast alleles for the major beta esterase (esterase-4) found in this species, as well as in heterozygous flies in which the slow or fast alleles came from one of the parents, were evaluated. Twelve components were analysed including longevity of both virgins and mated males and females, productivity, viability, including the egg-larva, egg-pupa, egg-imago and pupa-imago periods. These parameters were used to estimate the total fitness for each genotype. The best score was reached by individuals having the Est-4(S)/Est-4(S) genotype (scored at 1.000), followed by a fitness value of 0.892 presented by the Est-4(F)/Est-4(S) genotype (with the fast allele from maternal origin), 0.863 for the Est-4(F)/Est-4(F) and 0.842 for the Est-4(S)/Est-4(F) genotypes (with Est-4(F) maternal origin). These results suggested a higher relative adaptability of the Est-4(S)/Est-4(S) genotype followed by the Est-4(F)/Est-4(S) hybrid that possessed the allele Est-4(S) of maternal origin, which was incompatible with predictions of neutral polymorphism.

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Ten strains of two species in the Drosophila buzzatii cluster (D. serido and D. seriema) were examined as to esterase patterns using polyacrylamide gel electrophoresis. The migration rate of esterases, and their substrate specificity to alpha and beta naphthyl acetates, were analysed. Other esterase features such as inhibition behaviour, presence in males and females and location in the head, thorax or abdomen of flies, were also examined. The present data,together with results obtained by others for eight strains of D. koepferae, D. serido, D. seriema and D. buzzatii, show that 69 bands have been detected in the eighteen strains studied. This total number of bands was used for comparison of strains and species by similarity index, analysis of dependence and cluster analysis. The comparisons confirmed the existence of a high degree of similarity among D. seriema strains and among D. koepferae strains, but indicated differentiation among the D. serido strains. Two strains (D69R2 and D69R5) which differed from the others of the latter species, showed closer affinities with D. buzzatii, which indicates the need for further work on those strains classified as D. serido.