A liquid-phase-blocking concanavalin A enzyme-linked immunosorbent assay for the detection of antibodies against Newcastle disease virus in serum of free-ranging pigeons

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Aspergillus niger beta-Glucosidase Has a Cellulase-like Tadpole Molecular Shape INSIGHTS INTO GLYCOSIDE HYDROLASE FAMILY 3 (GH3) beta-GLUCOSIDASE STRUCTURE AND FUNCTION

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

Cyclodextrin Production by Bacillus lehensis Isolated from Cassava Starch: Characterisation of a Novel Enzyme

The properties of a previously unknown enzyme, denominated cyclodextrin glycosyltransferase, produced from Bacillus lehensis, were evaluated using affinity chromatography for protein purification. Enzyme characteristics (optimum pH and temperature; pH and temperature stability), the influence of substances on the enzyme activity, enzyme kinetics, and cyclodextrin production were analysed. Cyclodextrin glycosyltransferase was purified up to 320.74-fold by affinity chromatography using beta-cyclodextrin as the binder and it exhibited 8.71% activity recovery. This enzyme is a monomer with a molecular weight of 81.27 kDa, as estimated by SDS-PAGE. Optimum temperature and pH for cydodextrin glycosyltransferase were 55 degrees C and 8.0, respectively. The Michaelis-Menten constant was 8.62 g/l during maximum velocity of 0.858 g/l.h.

Citrus pulp and enzyme complex for growing and finishing pigs

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

Produção e imobilização de celulases em matriz de agarose com diferentes ativações químicas

Pós-graduação em Biotecnologia - IQ

Deconstructing the DGAT1 enzyme: Binding sites and substrate interactions

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

Evaluation of Three Enzyme Immunoassays for Diagnosis of Clostridium difficile-Associated Diarrhea in Foals

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

ENDO-OLIGOPEPTIDASE-A, A PUTATIVE ENKEPHALIN-GENERATING ENZYME, IN THE VERTEBRATE RETINA

Endo-oligopeptidase A, EC 3.4.22.19, converts small enkephalin-containing peptides into the corresponding enkephalins in vitro. We investigated the presence of endooligopeptidase A in the retina and its possible colocalization with enkephalins in retinal neurons. The specific activity of endo-oligopeptidase A found in pigeon retinae (30.3 +/- 7.3 mU/mg, mean +/- standard deviation) was four times higher than in rabbit retinae (7.0 +/- 1.1 mU/mg). The enzyme activity was not modified by EDTA, but it was enhanced by dithiothreitol and inhibited by zinc and 5,5'-dithiobis(2-nitrobenzoic acid). Immunohistochemical experiments with a purified antiserum against rabbit endo-oligopeptidase A revealed labeled neurons in both the inner nuclear layer and the ganglion cell layer of pigeon and rabbit retinae. Double-labeling immunofluorescence experiments demonstrated that about 90% of neurons containing endo-oligopeptidase A-like immunoreactivity also contained [Leu5]-enkephalin-like immunoreactivity. These colocalization results may represent an important step toward the demonstration of the possible involvement of endo-oligopeptidase A in enkephalin generation in vivo.

SAXS Studies of the Endoglucanase Cel12A from Gloeophyllum trabeum Show Its Monomeric Structure and Reveal the Influence of Temperature on the Structural Stability of the Enzyme

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

Fibrolytic enzyme production of Myceliophthora thermophila M.7.7. using inexpensive carbon sources and mineral nutrients

This study investigated the effect of inexpensive carbon and nitrogen sources on enzyme production by Myceliophthora thermophila M.7.7 in solid-state fermentation. Three kinds of lignocellulosic waste (corn straw, sugarcane bagasse and sugarcane straw) and six nitrogen sources (urea, calcium nitrate, analytical ammonium sulphate, yeast extract, agricultural fertilizer NPK 20-05-20 and fertilizing grade ammonium sulphate) were tested. Some physical-chermical parameters of the fermentation, such as temperature, initial pH and moisture content of the substrate on enzyme production, were evoluated. The maximum activities of xylanase (446.9 U/ml) endoglucanase (94.7 U/ml) and beta-glucosidase (2.8 U/ml) were observed in a mixture of corn straw and wheat bran (1:1 w/w) as the carbon source using fertilizer grade ammonium sulphate as the nitrogen source. This production occurred for an incubation period of 96 h, at 40°C, with initial moisture content of 70% and pH 5.0. These results have significant interest since they could be used for the future production of enzymes in a low-cost industrial process.

Angiotensin converting enzyme polymorphism in type 2 diabetes mellitus

This study was undertaken to assess the frequency of angiotensin converting enzyme (ACE) insertion/deletion (I/D) polymorphism in patients with type 2 diabetes mellitus. A total of 162 patients with type 2 diabetes and 160 individuals without this disease were analyzed. From the diabetes group, 81 patients with cardiovascular risk (according to American Diabetes Association parameters) were selected to form another subgroup. For polymorphism identification, two polymerase chain reactions were performed: one reaction to identify all genotypes and a second one to confirm the presence of the I allele. The observed genotype frequencies were as follows: diabetes group I/I (19.1%), I/D (52.5%), D/D (28.4%); control group I/I (12.5%), I/D (55.6%), D/D (31.9%); and diabetes with cardiovascular risk group I/I (16.0%), I/ D (59.3%), D/D (24.7%). No statistically significant difference was observed between the allelic and genotypic frequencies in the analyzed groups. Previous studies reported an association between the D allele and type 2 diabetes in Caucasian and East Asian populations. However, in mixed populations, such as those found in Brazil, such an association was not found. This fact does not discard the need for more studies on the frequencies of this polymorphism in the Brazilian population and the associations with risk factors, which can compromise the quality of life of diabetes patients

Estabilização de enzimas: uma abordagem

Enzyme stabilization is one critic point in basic and applied enzymology. The increasing interest in applying enzymes in industrial processes has fostered the search for biocatalysts with new properties or extreme stability. Enzyme stabilization can be achieved by different methods: isolating enzyme variants from organisms living in appropriate extreme environments (extremozymes), by protein engineering, chemical modification, use of additives, immobilization. This brief review aims to give a better understanding of those methods employed for enzyme stabilization.

The effect of biomass immobilization support material and bed porosity on hydrogen production in an upflow anaerobic packed-bed bioreactor

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