Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto

About: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto is a based out in . It is known for research contribution in the topics: Population & Catalysis. The organization has 2143 authors who have published 3674 publications receiving 71071 citations. The organization is also known as: FFCLRP & FFCLRP-USP.

Diversidade de formigas (Hymenoptera: Formicidae) em Seara, oeste de Santa Catarina

Abstract: The richness of the ant litter fauna in a county of the west of Santa Catarina state was studied using the Winkler sifting methods. Six sites were studied and 110 leaf litter samples collected. The similarity of the ant litter fauna between the sites was calculated using 10 samples of each site. Seven subfamilies, 40 genera and 92 ant species were identified in the six areas. The most rich genera were Pheidole (12 species) and Brachymyrmex (10), Solenopsis (9), Hypoponera and Strumigenys (5 each). The similarity values between pairs sites can be considered moderately high and not was showed a significant correlation of the similarity indices and the distance between the sites.

Thermostable invertases from Paecylomyces variotii produced under submerged and solid-state fermentation using agroindustrial residues

Abstract: The filamentous fungus Paecylomices variotii was able to produce high levels of cell extract and extracellular invertases when grown under submerged fermentation (SbmF) and solid-state fermentation, using agroindustrial products or residues as substrates, mainly soy bran and wheat bran, at 40°C for 72 h and 96 h, respectively. Addition of glucose or fructose (≥1%; w/v) in SbmF inhibited enzyme production, while the addition of 1% (w/v) peptone as organic nitrogen source enhanced the production by 3.7-fold. However, 1% (w/v) (NH4)2HPO4 inhibited enzyme production around 80%. The extracellular form was purified until electrophoretic homogeneity (10.5-fold with 33% recovery) by DEAE-Fractogel and Sephacryl S-200 chromatography. The enzyme is a monomer with molecular mass of 102 kDa estimated by SDS–PAGE with carbohydrate content of 53.6%. Optima of temperature and pH for both, extracellular and cell extract invertases, were 60°C and 4.0–4.5, respectively. Both invertases were stable for 1 h at 60°C with half-lives of 10 min at 70°C. Mg2+, Ba2+ and Mn2+ activated both extracellular and cell extract invertases from P. variotii. The kinetic parameters Km and Vmax for the purified extracellular enzyme corresponded to 2.5 mM and 481 U/mg prot−1, respectively.