Navegando por Autor "Falkoski, Daniel Luciano"
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Item Cellulases and hemicellulases from endophytic acremonium species and its application on sugarcane bagasse hydrolysis(Appl Biochem Biotechnol, 2011-05-02) Almeida, Maíra Nicolau de; Guimarães, Valéria Monteze; Bischoff, Kenneth M.; Falkoski, Daniel Luciano; Pereira, Olinto Liparini; Gonçalves, Dayelle S. P. O.; Rezende, Sebastião Tavares deThe aim of this work was to have cellulase activity and hemicellulase activity screenings of endophyte Acremonium species (Acremonium zeae EA0802 and Acremonium sp. EA0810). Both fungi were cultivated in submerged culture (SC) containing L -arabinose, D -xylose, oat spelt xylan, sugarcane bagasse, or corn straw as carbon source. In solid-state fermentation, it was tested as carbon source sugarcane bagasse or corn straw. The highest FPase, endoglucanase, and xylanase activities were produced by Acremonium sp. EA0810 cultivated in SC containing sugarcane bagasse as a carbon source. The highest β-glucosidase activity was produced by Acremonium sp. EA0810 cultivated in SC using D -xylose as carbon source. A. zeae EA0802 has highest α-arabinofuranosidase and α-galactosidase activities in SC using xylan as a carbon source. FPase, endoglucanase, β-glucosidase, and xylanase from Acremonium sp. EA0810 has optimum pH and temperatures of 6.0, 55 °C; 5.0, 70 °C; 4.5, 60 °C; and 6.5, 50 °C, respectively. α-Arabinofuranosidase and α-galactosidase from A. zeae EA0802 has optimum pH and temperatures of 5.0, 60 °C and 4.5, 45 °C, respectively. It was analyzed the application of Acremonium sp. EA0810 to hydrolyze sugarcane bagasse, and it was achieved 63% of conversion into reducing sugar and 42% of conversion into glucose.Item A Chrysoporthe cubensis enzyme cocktail produced from a low-cost carbon source with high biomass hydrolysis efficiency(Scientific Reports, 2017-06-20) Dutra, Thiago Rodrigues; Guimarães, Valéria Monteze; Varela, Ednilson Mascarenhas; Fialho, Lílian da Silva; Milagres, Adriane Maria Ferreira; Falkoski, Daniel Luciano; Zanuncio, José Cola; Rezende, Sebastião Tavares deLow cost and high efficiency cellulolytic cocktails can consolidate lignocellulosic ethanol technologies. Sugarcane bagasse (SCB) is a low cost agro-industrial residue, and its use as a carbon source can reduce the costs of fungi cultivation for enzyme production. Chrysoporthe cubensis grown under solid state fermentation (SSF) with wheat bran has potential to produce efficient enzymatic extracts for SCB saccharification. This fungus was grown under submersed fermentation (SmF) and SSF with in natura SCB, pretreated with acid or alkali and with others carbon sources. In natura SCB induced the highest carboxymethylcellulase (CMCase), xylanase, β-xylosidase, α-galactosidase and mannanase activities by C. cubensis under SSF. In natura and washed SCB, inducers of enzyme production under SSF, did not induce high cellulases and hemicellulases production by C. cubensis in SmF. The C. cubensis enzymatic extract produced under SSF with in natura SCB as a carbon source was more efficient for lignocelulolic biomass hydrolysis than extracts produced under SSF with wheat bran and commercial cellulolytic extract. Chrysoporthe cubensis showed high potential for cellulases and hemicellulases production, especially when grown under SSF with in natura SCB as carbon source.Item Covalent immobilization of α-Galactosidase from Penicillium griseoroseum and its application in Oligosaccharides Hydrolysis(Applied Biochemistry and Biotechnology, 2008-10-21) Falkoski, Daniel Luciano; Guimarães, Valéria Monteze; Queiroz, Marisa Vieira de; Araújo, Elza Fernandes de; Almeida, Maíra Nicolau de; Barros, Everaldo Gonçalves de; Rezende, Sebastião Tavares dePartially purified α-Galactosidase from Penicillium griseoroseum was immobilized onto modified silica using glutaraldehyde linkages. The effective activity of immobilized enzyme was 33%. Free and immobilized α-galactosidase showed optimal activity at 45 °C and pH values of 5 and 4, respectively. Immobilized α-galactosidase was more stable at higher temperatures and pH values. Immobilized α-galactosidase from P. griseoroseum maintained 100% activity after 24 h of incubation at 40 °C, while free enzyme showed only 32% activity under the same incubation conditions. Defatted soybean flour was treated with free and immobilized α-galactosidase in batch reactors. After 8 h of incubation, stachyose was completely hydrolyzed in both treatments. After 8 h of incubation, 39% and 70% of raffinose was hydrolyzed with free and immobilized α-galactosidase respectively. Immobilized α-galactosidase was reutilized eight times without any decrease in its activity.Item Effects of enzyme complex SSF (solid state fermentation) in pellet diets for Nile tilapia(Revista Brasileira de Zootecnia, 2012-05-30) Moura, Guilherme de Souza; Lanna, Eduardo Arruda Teixeira; Filer, Keith; Falkoski, Daniel Luciano; Donzele, Juarez Lopes; Oliveira, Maria Goreti de Almeida; Rezende, Sebastião Tavares deThe effects of enzyme complex SSF (solid state fermentation) on growth performance and the availability of sucrose and monosaccharides in the chyme of Nile were involved. The study included 360 fish (70g±4.43) in a completely randomized design with six dietary treatments (0, 50, 100, 150, 200 and 250 ppm of SSF) arranged in six replicates, with 10 fish per replicate. Every 15 days, one tilapia of each experimental unit was sacrificed for analyses of carbohydrate in the chyme. On day 60 of the experiment, the performance parameters were measured. There was a linear effect according to treatment for final weight and weight gain. For the other performance parameters, there were no differences. There was quadratic effect for sucrose and glucose in function of the treatment, whereas the fructose levels increased linearly. The addition of 150 ppm of the enzyme complex SSF in the feed improves the performance of Nile tilapia and increases the availability of sucrose and monosaccharides in the chyme.Item Enzimas lignocelulolíticas de fungos de podridão branca e fitopatógenos: produção, caracterização e aplicação em processos de sacarificação da biomassa(Universidade Federal de Viçosa, 2011-02-25) Falkoski, Daniel Luciano; Rezende, Sebastião Tavares de; http://lattes.cnpq.br/7062387416309293Neste trabalho, seis diferentes cepas fúngicas isoladas de plantações de eucalipto foram avaliadas quanto aos seus potenciais para produção de enzimas lignocelulolíticas visando suas aplicações em processos biotecnológicos, mais precisamente, processos de sacarificação da biomassa. Os fungos Pycnoporus sanguineus, Trametes sp. J2, Trametes sp J5, isolado J-129 (um basidiomiceto não identificado), Chrysoporthe cubensis e Cylindrocladium pteridis foram cultivados em meio líquido (ML) e meio semi- sólido (MSS) contendo farelo de trigo, sabugo de milho, polpa Kraft e celulose microcristalina (Avicel) como fonte de carbono. Após 4, 8 e 12 dias de fermentação os extratos enzimáticos produzidos foram coletados e analisados para determinação das atividades de xilanase, endoglicanases, β-glicosidases, lacases e celulase total (FPase). Pycnoporus sanguineus apresentou as maiores atividades para FPase (polpa Kraft-MSS) e lacase (farelo de trigo-ML) sugerindo que este microrganismo pode ser utilizado como um eficiente produtor de ambos os grupos de enzimas: cellulases e ligninases. Chrysoporthe cubensis propiciou as maiores atividades para endoglicanase e β-glicosidase (farelo de trigo-SSF). Sendo assim, foi demonstrado pela primeira vez que C. cubensis possui um grande potencial para produção de enzimas (principalmente celulases) para aplicação em processos de sacarificação da biomassa. As maiores atividades xilanolíticas foram encontradas em extratos produzidos pelo fitopatógeno C. pteridis, o qual foi apto a secretar quantidades incomuns de xylanase (aproximadamente 150000 U L -1 ) quando cultivado em meio semi-sólido usando farelo de trigo como substrato. Pycnoporus sanguineus e C. cubensis secretaram as maiores atividades celulolíticas e por isto os extratos enzimáticos produzidos por estes microrganismos foram caracterizados e subseqüentemente aplicados em testes de sacarificação da biomassa. Além de celulases e xilanases, P. sanguineus e C. cubensis também mostraram uma marcante capacidade para secretar atividades de α-arabinofuranosidase, α-galactosidase, β-mananase e poligalacturonase. Além disto, baixas atividades para β-xilosidase e β-manosidase também foram detectados em ambos os extratos enzimáticos. As atividades celulolíticas (endoglicanase, FPase e β-glicosidase) e xilanolíticas produzidas por P. sanguineus e C. cubensis foram caracterizadas em relação a pH e temperatura ótimos e foi observado que todas as atividades enzimáticas analisadas foram maximamente ativas quando incubadas em uma faixa de pH entre 3,5 e 4,5. Os valores de temperaturas ótimas variaram entre 50 e 60 °C. Além disto, todas as atividades enzimáticas foram altamente estáveis nas temperaturas de 40 e 50 °C tendo mantido mais de 70 % de suas atividades residuais após 48 h de incubação. Os extratos celulolíticos de P. sanguineus e C. cubensis foram aplicados em experimentos de sacarificação utilizando bagaço de cana, previamente submetido à pré-tratamento ácido ou básico, como substrato e os resultados de sacarificação foram comparados com aqueles obtidos utilizando- se uma preparação comercial de celulases. O uso de pré-tratamento ácido foi pouco eficiente na remoção da lignina junto ao bagaço de cana e como conseqüência disso observou-se um baixo rendimento de sacarificação quando este substrato foi utilizado, independentemente do extrato enzimático aplicado. Por outro lado, quando bagaço pré-tratado com base foi utilizado como substrato, elevadas taxas de hidrólise foram observadas. Considerando-se a produção de equivalentes açúcares redutores, foram observados rendimentos de sacarificação de 89,0, 60,4 e 64,0 % após 72 h de reação nos ensaios conduzidos com extrato de C. cubensis, extrato de P. sanguineus e com a preparação de celulases comercial, respectivamente. A produção de glicose também foi avaliada e, similarmente, se observou uma maior liberação deste monossacarídeo nos ensaios realizados com extrato do fungo C. cubensis (52,7 %). Para os ensaios de sacarificação utilizando extrato de P. sanguineus e celulase comercial a produção de glicose observada correspondeu a 22,6 e 36,6 % do rendimento teórico possível, respectivamente. Os resultados obtidos sugerem que as seis cepas fúngicas avaliadas neste trabalho têm grande potencial como produtoras de enzimas para aplicações em processos biotecnológicos. Os extratos celulolíticos de P. sanguineus e C. cubensis demonstraram um grande potencial para serem utilizados em processos de sacarificação da biomassa uma vez que o desempenho de hidrólise observado para estes extratos foi similar ou superior àquele observado em ensaios utilizando-se uma preparação de celulases comercial.Item Hydrolysis of galacto-oligosaccharides in soy molasses by α -galactosidases and invertase from Aspergillus terreus(Brazilian Archives of Biology and Technology, 2010-05) Reis, Angélica Pataro; Guimarães, Valéria Monteze; Ferreira, Joana Gasperazzo; Queiroz, José Humberto de; Oliveira, Maria Goreti Almeida; Falkoski, Daniel Luciano; Almeida, Maíra Nicolau de; Rezende, Sebastião Tavares deTwo α -galactosidase (P1 and P2) and one invertase present in the culture of Aspergillus terreus grown on wheat straw for 168 h at 28ºC were partially purified by gel filtration and hydrophobic interaction chromatographies. Optimum pH and temperatures for P1, P2 and invertase preparations were 4.5-5.0, 5.5 and 4.0 and 60, 55 and 65ºC, respectively. The KM app for ρ -nitrophenyl-α -D-galactopyranoside were 1.32 mM and 0.72 mM for P1 and P2, respectively, while the KM app value for invertase, using sacarose as a substrate was 15.66 mM. Enzyme preparations P1 and P2 maintained their activities after pre-incubation for 3 h at 50ºC and invertase maintained about 90% after 6 h at 55 ºC. P1 and P2 presented different inhibition sensitivities by Ag+, D-galactose, and SDS. All enzyme preparations hydrolyzed galacto-ologosaccharides present in soymolasses.Item Propriedades enzimáticas da enzima ALS de Cyperus difformis e mecanismo de resistência da espécie ao herbicida pyrazosulfuron-ethyl(Ciência Rural, 2010-12) Magro, Taísa Dal; Rezende, Sebastião Tavares de; Agostinetto, Dirceu; Vargas, Leandro; Silva, Antônio Alberto da; Falkoski, Daniel LucianoCyperus difformis L. é uma planta daninha ocorrente em lavouras de arroz irrigado, que tem apresentado dificuldade de controle devido à resistência a herbicidas inibidores da enzima ALS. Os objetivos deste trabalho foram investigar características cinéticas da enzima ALS de biótipos de C. difformis e determinar as bases bioquímicas da resistência da espécie ao herbicida pyrazosulfuron-ethyl. Para isso, foram conduzidos experimentos em laboratório do BIOAGRO/UFV. O método utilizado baseou-se na metologia utilizada por CAREY et al. (1997) e adaptada por VARGAS et al. (1999), com algumas modificações. Foram avaliadas a concentração de substrato (piruvato) que fornece velocidade inicial igual à metade da velocidade máxima de reação (K M ) e velocidade máxima de reação (V máx ), bem como a atividade da enzima ALS na presença do inibidor (pyrazosulfuron-ethyl). Diante dos resultados, pode-se observar que a resistência de C. difformis a pyrazosulfuron-ethyl é decorrente da insensibilidade da enzima ALS ao herbicida, não acarretando, porém, prejuízo aos parâmetros cinéticos K M e V máx da enzima ALS.Item Purificação e caracterização de α-galactosidases do fungo Penicillium griseoroseum para utilização na hidrólise de oligossacarídeos de rafinose em derivados de soja(Universidade Federal de Viçosa, 2007-02-28) Falkoski, Daniel Luciano; Queiroz, Marisa Vieira de; http://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4785812Z5; Oliveira, Maria Goreti de Almeida; http://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4790894D6; http://lattes.cnpq.br/7062387416309293; Barros, Everaldo Gonçalves de; http://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4781285J6; Fietto, Juliana Lopes Rangel; http://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4790238D0; Castro, Ieso de Miranda; http://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4787281A9O objetivo deste trabalho foi avaliar a eficiência das α-galactosidases purificadas do fungo Penicillium griseoroseum na hidrólise dos RO presentes no extrato desengordurado de soja. Penicillium griseoroseum foi cultivado em meio mineral, contendo galactomanana como fonte de carbono, por 120 h, a 28 oC. Após este período, o meio foi centrifugado, dialisado e utilizado como fonte de enzimas α-galactosidases. Os extratos enzimáticos foram submetidos à cromatografia de troca iônica em DEAE-Sepharose, pH 5,0. A eluição das proteínas que aderiram a resina foi feita com um gradiente de NaCl de 0 a 0,3 M, sendo detectado dois picos protéicos distintos contendo atividade α-galactosidase, sendo a enzima detectada o primeiro pico protéico eluído denominada α-Gal I e enzima eluída no segundo pico denominada α-Gal II. As frações contendo as enzimas α-Gal I e α-Gal II foram reunidas, concentradas por ultrafiltração e submetidas a uma eletroforese em gel de poliacrilamida, sob condições não desnaturantes. Ao termino das corridas eletroforéticas, os géis foram incubados em uma solução de ρ-NP-αGal (4 mg.mL-1) para determinar a localização das enzimas α-galactosidases. As regiões dos géis contendo as enzimas α-Gal I e α-Gal II, foram recortadas, maceradas e submetidas a agitação em tampão acetato de sódio, pH 5, 100 mM para extração e obtenção das enzimas purificadas. As enzimas α-Gal I e α-Gal II tiveram fatores de purificação de 155 e 53 vezes, respectivamente, com um rendimento final de 38 e 9 %, respectivamente. Atividades máximas de ambas as enzimas foram detectadas em pH 5,0 a 45oC. Os valores de meia vida da enzima α-Gal I a 40 e 45°C foram de 16 e 0,66 h respectivamente. Os valores de meia-vida da enzima α-Gal II a 40 e 45°C foram de 3,8 e 0,25 h respectivamente. Os valores da KM para ρ-NP-αGal, ο-PN-αGal, melibiose, estaquiose e rafinose para a enzima α-Gal I foram de 1,06, 1,31, 4,77, 19,99 e 28,74 mM, respectivamente, enquanto que, para a enzima α-Gal II foram de 0,80, 1,26, 5,10, 21,74 e 30,46 mM, respectivamente. As α-galactosidases apresentaram especificidade absoluta para galactose em posição α, hidrolisando os substratos sintéticos ρ-NP-αGal, ο-NP-αGal, estaquiose, rafinose, melibiose. Sulfato de cobre, sulfato de ferro e cloreto de mercúrio inativaram completamente as α-galactosidases quando presentes em concentrações iguais 1 mM no meio de reação. Os resultados dos tratamentos de extrato desengordurado de soja com as enzimas α-Gal I e α-Gal mostraram uma redução de 100% de estaquiose pós-incubação a 40 oC, por 8 h. Houve redução de 69 e 12 % da rafinose após 8 h de incubação, a 40 oC, com as enzima α-Gal I e α-Gal II, respectivamente. A enzima α-Gal I foi imobilizada em suporte insolúvel (sílica modificada) e utilizada em ensaios de hidrólise de RO contidos em extrato desengordurado de soja, sendo verificado uma redução de 100 e 70% de estaquiose e rafinose, respectivamente, após 8 h de incubação. A enzima α-Gal I foi reutilizada 8 vezes consecutivas, em ensaios de hidrólise de RO, não sendo detectada nenhuma perda de atividade enzimática. Observa-se que as α-galactosidases de P. griseoroseum foram eficientes na redução dos RO presentes em produtos derivados de soja, sendo indicadas para a utilização industrial no processamento desses açúcares.Item Purification and characterization of Aspergillus terreus α-Galactosidases and their use for hydrolysis of Soymilk Oligosaccharides(Applied Biochemistry and Biotechnology, 2011-02-18) Ferreira, Joana Gasperazzo; Reis, Angélica Pataro; Guimarães, Valéria Monteze; Falkoski, Daniel Luciano; Silva Fialho, Lílian da; Rezende, Sebastião Tavares deα-Galactosidases has the potential to hydrolyze α-1-6 linkages in raffinose family oligosaccharides (RFO). Aspergillus terreus cells cultivated on wheat bran produced three extracellular forms of α-galactosidases (E1, E2, and E3). E1 and E2 α-galactosidases presented maximal activities at pH 5, while E3 α-galactosidase was more active at pH 5.5. The E1 and E2 enzymes showed stability for 6 h at pH 4–7. Maximal activities were determined at 60, 55, and 50°C, for E1, E2, and E3 α-galactosidase, respectively. E2 α-galactosidase retained 90% of its initial activity after 70 h at 50°C. The enzymes hydrolyzed ρNPGal, melibiose, raffinose and stachyose, and E1 and E2 enzymes were able to hydrolyze guar gum and locust bean gum substrates. E1 and E3 α-galactosidases were completely inhibited by Hg2+, Ag+, and Cu2+. The treatment of RFO present in soy milk with the enzymes showed that E1 α-galactosidase reduced the stachyose content to zero after 12 h of reaction, while E2 promoted total hydrolysis of raffinose. The complete removal of the oligosaccharides in soy milk could be reached by synergistic action of both enzymesItem Purification and characterization of xylanases from the fungus Chrysoporthe cubensis for production of xylooligosaccharides and fermentable sugars(Applied Biochemistry and Biotechnology, 2016-12-24) Sousa Gomes, Kamila de; Maitan-Alfenas, Gabriela P.; Andrade, Lorena G. A. de; Falkoski, Daniel Luciano; Guimarães, Valéria Monteze; Alfenas, Acelino C.; Rezende, Sebastião Tavares deXylanases from the pathogen fungus Chrysoporthe cubensis were produced under solid state fermentation (SSF) using wheat bran as carbon source. The enzymatic extracts were submitted to ion exchange (Q Sepharose) and gel filtration chromatography methods (Sephadex S-200) for purification. The xylanases were divided into three groups: P1 showed better performance at 60 °C and pH 4.0, P2 at 55 °C and pH 3.0, and P3 at 80 °C and pH 3.0. Oat spelt xylan was the best substrate hydrolyzed by P1 and P3, while beechwood xylan was better degraded by P2. Carboxymethyl cellulose (CMC) and p-nitrophenyl-β-d-xylopyranoside (p-NPβXyl) were not hydrolyzed by any of the xylanases. The K M ’ or K M values, using oat spelt xylan as substrate, were 2.65 mg/mL for P1, 1.81 mg/mL for P2, and 1.18 mg/mL for P3. Xylobiose and xylotriose were the main xylooligosaccharides of oat spelt xylan degradation, indicating that the xylanases act as endo-β-1,4-xylanases. Xylanases also proved to be efficient for hydrolysis of sugarcane bagasse when used as supplement of a commercial cocktail due to the increase of the reducing sugar release.Item Stability of enzyme complex solid-state fermentation subjected to the processing of pelleted diet and storage time at different temperatures(Revista Brasileira de Zootecnia, 2016-09-28) Moura, Guilherme de Souza; Lanna, Eduardo Arruda Teixeira; Donzele, Juarez Lopes; Falkoski, Daniel Luciano; Rezende, Sebastião Tavares de; Oliveira, Maria Goreti de Almeida; Albino, Luiz Fernando TeixeiraThe effects of processing of pelleted diets and their storage time on the stability of the enzyme complex SSF (solid-state fermentation) were evaluated. Two diets were formulated with the same nutritional composition, differing only in the Schizochytrium sp. levels (0 g kg–1 and 50 g kg–1). The samples were collected during the following processing steps: mixing, then pelleting, and then oven. To evaluate the storage time, the diet ready after drying was considered as day 1. On this day, two samples were obtained, being one kept in a room with ambient temperature of 25 °C and another stored in freezer at –18 °C. At 15, 30, 45, and 60 days, sub-samples were taken. All samples from the processing step and storage time were sent to the laboratory and the following enzyme activities were measured: α-galactosidase, endoglucanase (carboxy-methyl-cellulase), xylanase, sucrase, amylase, lipase, and trypsin. There were no significant differences between the mixture and post-oven phase, except for the activity of α-galactosidase, lipase, and sucrase. For the storage temperature of 25 °C, no effect was observed for the activities of endoglucanase, sucrase, xylanase, amylase, and trypsin between the first (after oven) and the 60th day of the trial. As for the storage temperature of –18 °C, no difference was observed, except for the activities of endoglucanase and xylanase between the first and last day. Comparing the two types of storage (25 °C and –18 °C), there was difference only for the activity of galactosidase and trypsin at 60 days. The enzymes of the enzyme complex SSF studied remain stable during the processing of pelleted diet at 55 °C, maintaining activity for at least 60 days when stored at temperatures up to 25 °C.Item Swimming training attenuates contractile dysfunction in diabetic rat cardiomyocytes(Arquivos Brasileiros de Cardiologia, 2010-12-21) Silva, Márcia Ferreira da; Pelúzio, Maria do Carmo Gouveia; Amorim, Paulo Roberto dos Santos; Lavorato, Vitor Neiva; Santos, Natália Pereira do; Bozi, Luiz Henrique Marchesi; Penitente, Arlete Rita; Falkoski, Daniel Luciano; Berfort, Felipe Gomes; Natali, Antonio JoseExperimental diabetes promotes contractile dysfunction in cardiomyocytes, but the effects of swimming in this disorder are not known. To test the effects of a swimming training program (STP) on cardiomyocyte contractile dysfunction in rats with experimental diabetes. Wistar rats (age: 30 days; mean body weight: 84.19 g) with diabetes induced by streptozotocin (60 mg/kg body weight; glucose > 300 mg/dl) were divided into sedentary diabetic rats (SD, n = 10) and exercised diabetic rats (ED, n = 13). Animals of same age and weight served as sedentary controls (SC, n = 10) and exercised controls (EC, n = 06). Animals and ED and EC underwent a STP (05 days/week, 90 min/day) for 08 weeks. Left ventricular (LV) myocytes were isolated and electrically stimulated at 3.0 Hz at room temperature (∼ 25º C). Diabetes reduced contractile function in cardiomyocytes of animals compared to controls (i.e., lower amplitude of contraction, longer duration of contraction and relaxation). The STP attenuated the reduced amplitude of contraction (SC, 11 ± 0.2% vs ED, 11.6 ± 0.2%), time to peak contraction (SC, 319 ± 5.8 ms vs ED, 333 ± 4.8 ms) and time to 50.0% of relaxation (SC, 619 ± 22.2 ms vs ED 698 ± 18.6 ms) of cardiomyocytes of diabetic rats. Diabetes reduced the size of cardiomyocytes, however, the STP minimized the reduction of cell volume and width, without changing length. The swimming training program attenuated the contractile dysfunction of the LV myocytes of rats with experimental diabetes.Item Treatment of soy milk with Debaryomyces hansenii cells immobilised in alginate(Food Chemistry, 2009-05-15) Souza Júnior, Waldeck Campanha de; Rezende, Sebastião Tavares de; Viana, Pollyanna Amaral; Falkoski, Daniel Luciano; Reis, Angélica Pataro; Machado, Solimar Gonçalves; Barros, Everaldo Gonçalves de; Guimarães, Valéria MontezeWhole cells of Debaryomyces hansenii UFV-1 were permeabilised with ethanol and immobilised in calcium alginate hydrogel. The optimum pH and temperature for α-galactosidase activities of permeabilised free (PFC) and permeabilised immobilised cells (PIC) were 4.5 and 60 °C; and 4.0 and 70 °C, respectively. PIC α-galactosidase was more stable than that of PFC. The incubation of PIC at 60 and 70 °C promoted an increase in α-galactosidase activity. The α-galactosidase activity was maintained when PIC was used in three repeated batches. The Km values for PIC and PFC α-galactosidases, with ρNPαGal, were 0.82 mM and 0.30 mM, respectively. Soy milk treatment with PIC for 6 h at 60 °C promoted 100% hydrolysis of raffinose oligosaccharides.