473 resultados para Manioc bran
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O objetivo deste trabalho foi detectar traços de farinha de carne e ossos bovinos, em ovos de poedeiras alimentadas com dietas comerciais com inclusão de ingredientes vegetais alternativos e leveduras. A detecção foi feita pela técnica dos isótopos estáveis do carbono e do nitrogênio. Foram utilizadas 384 poedeiras, distribuídas aleatoriamente em oito tratamentos. Os tratamentos consistiram de uma dieta-controle - à base de milho e farelo de soja - e sete dietas com inclusão de farinha de carne e ossos bovinos, acrescidas ou não de outros ingredientes (farelo de trigo, quirera de arroz, farelo de algodão, glúten de milho, levedura de cana e levedura de cerveja). No 35º dia, foram tomados aleatoriamente 24 ovos por tratamento: 12 para análise de ovo e 12 para análise de gema e albúmen, em separado. Após análise isotópica de carbono e nitrogênio, os resultados foram submetidos à análise multivariada de variância. As médias dos pares isotópicos dos ovos, gema e albúmen, em todos os tratamentos, diferiram daquelas do tratamento-controle. A técnica dos isótopos estáveis permite detectar, nos ovos, gema e albúmen, a farinha de carne e ossos bovinos utilizada na dieta de poedeiras, mesmo com a inclusão de outros ingredientes vegetais e leveduras.
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Este trabalho teve por objetivo avaliar o efeito dos níveis 40, 55 e 70% de concentrado associados a um volumoso de baixa qualidade sobre o consumo e ganho de peso de 16 novilhos mestiços, castrados, com 10 meses de idade e peso vivo inicial médio de 312kg, em delineamento inteiramente ao acaso, com três repetições, durante 63 dias. O volumoso usado foi a aveia (Avena strigosa), tratada com uréia e o concentrado era constituído de milho, farelo de arroz, farelo de soja e minerais. Todas as dietas foram ajustadas para conter 12% de proteína bruta. Houve resposta positiva e linear à proporção de concentrado na dieta, para as variáveis ganho de peso diário e consumo de matéria seca expresso em kg/animal/dia, em percentagem do peso vivo e em g por kg de peso metabólico em função da proporção de concentrado na dieta. Houve resposta linear negativa para conversão alimentar. O consumo de matéria seca e o ganho de peso diário aumentaram na medida em que se elevou a proporção de concentrado na dieta. O volumoso de baixa qualidade empregado possivelmente limitou o consumo e conseqüentemente o aporte de nutrientes.
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Basidyomycete Lentinula edodes has its related enzymatic activity mainly on the agribusiness waste kind used as a substrate. The objective of this work was to verify the activity of oxidative enzymes lacase (Lac), lignina peroxidase (LiP) and manganese peroxidase (MnP) of three L. edodes strains, in stationary system, cultivated the 25 degrees C, in the absence of light, in substrates wtih 20% of bran of rice, 1% of CaCO(3) and 79% of rice husk (CA), eucalyptus sawdust (SE), cassava bagasse (BM) and sugarcane bagasse (BC), adjusted to 60% of humidity. The Lac and MnP activities were bigger in eucalyptus sawdust (SE) and sugarcane bagasse (BC). The UP activity was not induced for tested substrates. The rice husk (CA) and cassava bagasse (BM) Substrates, although are not adequate to produce Lac or MnP, can be used as additives to increase the porosity, air availability and easy metabolism polysaccharides.
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Cyclodextrin glycosyltransferase (CGTase) is an enzyme that produces cyclodextrins from starch by an intramolecular transglycosylation reaction. Cyclodextrins have been shown to have a number of applications in the food, cosmetic, pharmaceutical, and chemical industries. In the current study, the production of CGTase by Paenibacillus campinasensis strain H69-3 was examined in submerged and solid-state fermentations. P. campinasensis strain H69-3 was isolated from the soil, which grows at 45 C, and is a Gram-variable bacterium. Different substrate sources such as wheat bran, soybean bran, soybean extract, cassava solid residue, cassava starch, corn starch, and other combinations were used in the enzyme production. CGTase activity was highest in submerged fermentations with the greatest production observed at 48-72 h. The physical and chemical properties of CGTase were determined from the crude enzyme produced from submerged fermentations. The optimum temperature was found to be 70-75 degrees C, and the activity was stable at 55 degrees C for 1 h. The enzyme displayed two optimum pH values, 5.5 and 9.0 and was found to be stable between a pH of 4.5 and 11.0.
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Rhizopus stolonifer was cultivated in wheat bran to produce a cellulase-free alkaline xylanase. The purified enzyme obtained after molecular exclusion chromatography in Sephacryl S-200 HR showed optimum temperature as 45 degrees C and hydrolysis pHs optima as pH 6.0 and 9.0. Xylanase presented higher Vmax at pH 9.0 (0.87 mu mol/mg protein) than at pH 6.0 and minor Km at pH 6.0 (7.42 mg/mL)than at pH 9.0.
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An Aspergillus giganteus strain was isolated as an excellent producer of xylanase associated with low levels of cellulase. Optimal xylanase production was obtained in liquid VOGEL medium containing xylan as carbon source, pH 6.5 to 7.0, at 25degreesC and. under shaking at 120 rpm during 84h. Among the several carbon sources tested, higher xylanase production was verified in xylan, xylose, sugar-cane bagasse, wheat bran and corn cob cultures, respectively. Optimal conditions for activity determination were 50degreesC and pH 6.0. The xylanolytic complex of A. giganteus showed low thermal stability with T-50 of 2 h, 13 min and I min when it was incubated at 40, 50 and 60degreesC, respectively, and high stability from pH 4.5 to 10.5, with the best interval between 7.0 to 7.5. This broad range of stability in alkali pH indicates a potential applicability in some industrial processes, which require such condition. Xylanolytic activity of A. giganteus was totally inhibited by Hg+2, Cu+2 and SDS at 10 mm. The analysis of the products from the oat spelts xylan hydrolysis through thin-layer chromatography indicated endoxylanase activity, lack of debranching enzymes and P-xylosidase activity in assay conditions.
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A strain of Aspergillus versicolor produces a xylanolytic complex containing two components, the minor component being designated xylanase II. The highest production of xylanase II was observed in cultures grown for 5 days in 1% wheat bran as carbon source, at pH 6.5. Xylanase II was purified 28-fold by DEAE-Sephadex and HPLC GF-5 10 gel filtration. Xylanase II was a monomeric glycoprotein, exhibiting a molecular mass of 32 kDa with 14.1% of carbohydrate content. Optimal pH and temperature values for the enzyme activity were about 6.0-7.0 and 55 degreesC, respectively. Xylanase II thermoinactivation at 50degreesC showed a biphasic curve. The ions Hg2+, Cu2+ and the detergent SDS were strong inhibitors, while Mn2+ ions and dithiothreitol were stimulators of the enzyme activity. The enzyme was specific for xylans, showing higher specific activity on birchwood xylan. The Michaelis-Menten constant (K-m) for birchwood xylan was estimated to be 2.3 mg ml(-1) while maximal velocity (V-max) was 233.1 mumol mg(-1) min(-1) of protein. The hydrolysis of oat spell xylan released only xylooligosaccharides. Published by Elsevier Ltd.
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The xylanolytic system of Aspergillus versicolor is controlled by induction and carbon catabolite repression. Carboxymethylcellulose and wheat bran were the best inducers of xylanolytic activity. When the fungus was grown for 5 days on VOGEL's liquid medium with wheat bran, the optimal pH and temperature for xylanase production were 6.5 and 30 degrees C, respectively. Optimal conditions for the xylanolytic activity assay were at pH 6.0 and 55 degrees C. The half-life at 60 degrees C of the crude enzyme was 6.5 and 21 minutes, in the absence or presence of substrate, respectively.Xylan is the main hemicellulosic component of plant biomass being present in appreciable quantities in agricultural and several agroindustrial wastes. From the products of xylan enzymatic hydrolysis it is possible to obtain cell protein, fuels and other chemicals. Xylanases combined with cellulase could have applications in food processing. Cellulase-free xylanases can be also utilized for preparation of cellulose pulps and liberation of textile fibres (WOODWARD 1984; BIELY 1985, WONG et al. 1988). In view of the potential applications of xylanases, a study of these enzymes from various sources and their multiplicity is desirable.Among xylanolytic microorganisms, filamentous fungi have been more extensively studied and the genus Aspergillus has been shown to be an efficient producer of xylanases. Preliminary observations from our laboratory have demonstrated that a strain of Aspergillus versicolor, isolated from Brazilian soil, produced high xylanase and low cellulase levels, which is an interesting characteristic for some industrial applications. In this report we describe the production and some properties of xylanase obtained from this fungus.
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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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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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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The objective of this research was to investigate xylanase production by filamentous fungi (Trichoderma viride) to determine the best cultivation conditions in the process, aiming toward optimization of enzyme production. The best temperature, as well as the best carbon source, for biomass production was determined through an automated turbidimetric method (Bioscreen-C). The enzyme activity of this fungus was separately evaluated in two solid substrates (wheat and soybean bran) and in Vogel medium, pure and by adding other carbon sources. Temperature effects, cultivation time, and spore concentrations were also tested. The best temperature and carbon source for enzyme and biomass production was 25 C and sorbitol, respectively. Maximum xylanase activity was achieved when the fungus was cultivated in wheat bran along with sorbitol (1%, w/v), using a spore concentration of 2 x 10(6) spores. mL(-1), pH 5.0, for 144 h cultivation. The study demonstrated not only the importance of the nature of the substrate in obtaining a system resistant to catabolic repression, but also the importance of the culture conditions for biosynthesis of this enzyme. T. viride showed a high potential for xylanase production under the conditions presented in these assays.
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)