35 resultados para Amilases


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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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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

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Dissertação de mestrado, Tecnologia dos Alimentos, Instituto Superior de Engenharia, Universidade do Algarve, 2014

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Globulins fractions of legume seeds of Crotalaria pallida, Erytrina veluntina and Enterolobium contortisiliquum were isolated and submitted to assays against serine, cysteine and aspartic proteinases, as also amylase present in midgut of C. maculatus and Z. subfasciatus. Hemagglutination assays indicated presence of a lectin in E. veluntina globulin fractions. This lectin had affinity to human erythrocytes type A, B and O. Vicilins were purified by chromatography on Sephacryl S-300 followed of a chromatography on Sephacryl S-200, which was calibrated using protein markers. Vicilins from C. pallida (CpV) and E. veluntina (EvV) seeds had a molecular mass of 124.6 kDa and E. contortisiliquum a molecular mass of 151kDa. Eletrophoresis in presence of SDS showed that CpV was constituted by four subunities with apparent molecular mass of 66, 63, 57 and 45 kDa, EvV with three subunities with apparent molecular mass of 45kDa and EcV four subunities, two with 37.1 kDa and two with 25.8 kDa. Non denaturantig eletrophoresis displayed single bands with high homogeneity, where CpV had lower acidic behavior. All vicilins are glycoproteins with carbohydrate contents at 1 to1.5%. Bioassays were done to detect deleterious effects of vicilins against C. maculatus and Z. subfasciatus larvae. CpV, EvV and EcV exhibited a WD50 of 0.28, 0.19 and 1.03%; LD50 0.2, 0.26, and 1.11% respectively to C. maculatus. The dose responses of CpV, EvV and EcV to Z. subfasciatus were: WD50 of 0.12, 0.14, 0.65% and LD50 of 0.09, 0.1, and 0.43% respectively. The mechanism of action of these proteins to bruchids should be based on their properties of bind to chitin present in mid gut of larvae associated with the low digestibility of vicilin. In assays against phytopatogenous fungus, only EcV was capable of inhibit F. solani growth at concentrations of 10 and 20 µg and its action mechanism should be also based in the affinity of EcV to chitin present in the fungi wall

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Seed germination and seedling establishment are critical processes for commercial plantation and depend directly on reserve mobilization as a source of cellular fuels and biosynthetic precursors. In this way, we investigated the coordination among reserve mobilization, metabolite partitioning, and mobilizing enzyme activities in Moringa oleifera Lam (moringa) an oil-seeded species employed in biofuel production. Seeds were germinated under controlled conditions and seedlings were grown hydroponically at a greenhouse. Samples were harvested at 0, 4, 8, 10, 12, 16, and 20 days after imbibition (DAI). The contents of dry mass (DM), neutral lipids (NL), soluble proteins (SP), starch, total soluble sugars (TSS), non-reducing sugars (NRS), and total free amino acids (TFAA) as the activity of isocitrate lyase (ICL), acid proteases, and amylases were determined. The mobilization of storage proteins was initiated during seed germination whereas the mobilization of storage lipids and starch was triggered throughout seedling establishment although all reserves have been depleted until 20 DAI. The partitioning of DM and metabolites to the roots and the shoots was uneven during seedling establishment. Low shoot/root ratio on the basis of DM could be related to the natural occurrence of moringa in drought climates. In the roots, TSS, NRS, and TFAA were accumulated from 12 to 16 DAI and then were consumed until the end of the experiment. In the shoots, TSS and TFAA were consumed in parallel with NRS accumulation from 12 to 20 DAI. The activity of ICL, acid proteases, and amylases was coordinated with the mobilization of lipids, proteins and starch respectively. Thus, we propose that the patterns of reserve mobilization and metabolite partitioning verified in moringa seem distinct from those found to other tree species and may be involved in metabolic strategies to enable environment colonization

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Neste trabalho objetivou-se avaliar a concentração de pectinase (Pectinex Ultra SP-L) no processo de hidrólise-sacarificação do farelo de mandioca para produção de etanol. Foram avaliadas quatro concentrações da enzima pectinase com enzima complemetar as amilases e o tratamento com apenas as amilases. Realizou-se a caracterização do hidrolisado e resíduo fibroso resultantes do processo, e os resultados obtidos demonstraram que a concentração mínima de pectinase para um bom rendimento do processo foi 8Kg enzima/t fibras, com. 89,4% do amido hidrolisado. Quanto ao resíduo fibroso, este apresenta potencialidade de aproveitamento com base para produtos dietéticos ricos em fibras.

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Uma possibilidade de incremento na cadeia produtiva do gengibre seria o uso de rizomas desclassificados para comercialização in natura, ou mesmo o resíduo da extração de óleos, como matérias-primas para a obtenção de bebidas destiladas. O amido não é diretamente fermentável, necessitando de uma hidrólise prévia de suas cadeias para a obtenção de glicose. Neste trabalho, objetivou-se avaliar o efeito das concentrações de amilases sobre o perfil de açúcares e rendimento no processo de hidrólise-sacarificação de gengibre. O processo seguiu o delineamento central composto rotacional para dois fatores, totalizando 11 tratamentos. Os resultados obtidos mostram o efeito das concentrações da α-amilase (Termamyl 2X) e da amiloglucosidase (AMG 300L) sobre o teor de glicose do hidrolisado e efeito da concentração de amiloglucosidase sobre o teor de dextrina. Os maiores rendimentos de hidrólise da suspensão de gengibre foram obtidos nas condições de elevada concentração de -amilase e amiloglucosidase.

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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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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)