100 resultados para Rhizopus Arrhizus
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Tesis (Maestría en Ciencias con Especialidad en Alimentos) UANL
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The improvement of the enzymatic performance of Aspergillus terreus and Rhizopus oryzae in enantioselective bioreductions by using glycerol as a co-solvent has been studied. In the most of the bioreductions, glycerol has demonstrated its potential for improved conversions (up to >99%) and enantioselectivities (up to >99%) when compared to reactions in aqueous or other aqueous-organic media (THF, diethyl ether, toluene, DMSO and acetonitrile). Moreover, high isolated yields of the desired chiral alcohols have been obtained on a preparative scale showing the great potential of this green solvent in biocatalysis. (C) 2009 Elsevier Ltd. All rights reserved.
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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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A strain of Rhizopus sp. screened among more than 800 filamentous fungi showed great ability to produce a thermostable alpha-amylase by solid state fermentation. The best production was obtained with a bran moisture content of 40% when the enzyme activity reached 60 EU/g. of medium. During the purification procedures, a column of DEAE-Sephadex A-50 separated the enzyme in two fractions and the larger (85% of the total activity) showed optimum pH in a range from 4.0 to 5.6. Optimum temperature was found at 60-65 degrees C and in this range no loss of activity was observed after 60 min. of treatment in pH 5,0. Its K-m and V-m are, respectively, of 5.0 mg/ml of starch and 10,01 uMol of reducing sugar/min./mg. of protein. Its molecular weight was calculated in 64.000 by gel filtration in Sephadex G-200. The dextrinization power of the enzyme was observed preferentialy on substrates compound by chains with higher ramifications, that is: amylopectin > starch > amylose. Other aspects of the enzyme pattern action are also discussed.
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This paper discusses the inducer effect of corn soluble starch and the individual components (amylose and amylopectin) from corn and potatoes starch for alpha-amylase production by a strain of Rhizopus sp. The following decreasing order in the enzyme production was obtained: corn amylose > potatoes amylose > corn amylopectin > potatoes amylopectin > starch > maltose, coinciding with the ability of the enzyme to release reducing units, except the soluble starch that was more softly hydrolysed. However, when the enzyme action was measured by the iodine binding method, an inverse order of enzyme activity was obtained, that is: amylopectins > starch > amylosis. The results suggest that: a) branched structures in substrate affect the enzyme production; b) corn amylose and corn amylopectin are better inducers than their respectives homologous from potatoes; c) cc-amylase from Rhizopus sp has different action patterns on substrates with straight or branched chains: from the former, it removes only reducing units with lower molecular weight (G1-G3); from the latter it also removes oligosaccharides with higher molecular weight (G5-G6).
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Rhizopus microsporus var. rhizopodiformis produced high levels of alpha-amylase and glucoamylase under solid state fermentation, with several agricultural residues, such as wheat bran, cassava flour, sugar cane bagasse, rice straw, corncob and crushed corncob as carbon sources. These materials were humidified with distilled water, tap water, or saline solutions-Segato Rizzatti (SR), Khanna or Vogel. The best substrate for amylase production was wheat bran with SR saline solution (1:2 v/v). Amylolytic activity was still improved (14.3%) with a mixture of wheat bran, corncob, starch and SR saline solution (1:1:0.3:4.6 w/w/w/v). The optimized culture conditions were initial pH 5, at 45 degrees C during 6 days and relative humidity around 76%. The crude extract exhibited temperature and pH optima around 65 degrees C and 4-5, respectively. Amylase activity was fully stable for 1 h at temperatures up to 75 degrees C, and at pH values between 2.5 and 7.5.
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Some factors influencing the growth and production of extracellular lipase by Rhizopus oligosporus were studied. Highest yields of enzyme were obtained when Tweens were the carbon source. Soybean meal extract supported good growth and enzyme production. Carbohydrates, vegetable oils, proteins or amino acids did not stimulate lipase production. The fungus grew well with carbohydrate- or protein-supplemented media but not with oils, unless emulsified with a non-metabolizable gum. The production of biomass in static cultures was maximum at 35-40°C after 4 d at pH 5.5. The yield of lipase was maximum at 25°C after 3 d at pH 6.5. Shaking cultures enhanced growth but decreased lipase production.
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Amylases from Rhizopus oryzae and Rhizopus microsporus var. oligosporus were obtained using agro-industrial wastes as substrates in submerged batch cultures. The enzymatic complex was partially characterised for use in the production of glucose syrup. Type II wheat flour proved better than cassava bagasse as sole carbon source for amylase production. The optimum fermentation condition for both microorganisms was 96 hours at 30°C and the amylase thus produced was used for starch hydrolysis. The product of the enzymatic hydrolysis indicated that the enzyme obtained was glucoamylase, only glucose as final product was attained for both microorganisms. R. oligosporus was of greater interest than R. oryzae for amylase production, taking into account enzyme activity, cultivation time, thermal stability and pH range. Glucose syrup was produced using concentrated enzyme and 100 g L-1 starch in a 4 hours reaction at 50°C. The bioprocess studied can contribute to fungus glucoamylase production and application. © 2013 Institute of Chemistry, Slovak Academy of Sciences.
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Pós-graduação em Biotecnologia - IQ
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Amilases e proteases constituem um dos principais grupos de enzimas industriais pelo seu amplo espectro de aplicações biotecnológicas. Elas podem ser obtidas a partir de fontes microbianas e com altos rendimentos por processos de fermentação em estado sólido (FES). Conhecer as características bioquímicas das enzimas é fundamental para adequação aos processos industriais. O objetivo do trabalho foi determinar a melhor temperatura para atividade das enzimas amilase e protease de Rhizopus oligosporus obtidas por fermentação em estado sólido utilizando farelo de trigo como substrato. Os melhores valores para atividade amilolítica e proteolítica foram obtidos nas temperaturas de 55 - 65 °C e de 50 - 60 °C, respectivamente. Estes resultados sugerem que as enzimas estudadas podem ser utilizadas em processos que empregam elevadas temperaturas.
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)