Prospecção de leveduras para a produção de biocombustíveis: estudo dos gêneros Aureobasidium e Meyerozyma

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Micropartículas de goma gelana revestidas com filmes de amido resistente/pectina como estratégia para administração oral de insulina

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

Avaliação do processo de hidrólise enzimática para obtenção de açúcares a partir de gengibre (Zingiber officinale)

Ginger is a starchy tubers prized for their chemical components. In the production of any kinds of beverages has been added to the extract of ginger. However, in view of the high starch content, a possibility of further development of the agribusiness sector this would be the hydrolysis tuberous rhizomes disqualified for export in order to obtain hydrolysates that would be used in the preparation of fermented beverages. This work aimed to evaluate the production of sugar from rhizomes of ginger. Two α-amylase enzymes were tested in the stage of liquefaction (Liquozyme Supra (T1) and Termamyl 2X (T2)), as well as the effect of time of action of amyloglucosidase (AMG 300L). The hydrolysates were analyzed in liquid chromatography (HPLC) and was also carried out the mass balance of the processes. The results showed higher hydrolysis of starch in the treatment that used Liquozyme Supra in liquefaction. The action time of 18 hours of AMG 300L hydrolyzate which gave an 98% of its chemical components was glucose.

Vicilinas de sementes de leguminosas selvagens:purificação, caracterização, efeito de deletério e mecanismo de ação para bruquídeos e para fungos fitopatogênicos

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