Cinthia Aparecida de Andrade Silva

Brazilian savannah fruits: Characteristics, properties, and potential applications

The Brazilian savannah is the second largest biome of the country, and it displays great biodiversity. The fruits of the native trees have peculiar characteristics and are recognized for their nutritional and therapeutic aspects. However, little is known about their technological and biotechnological potential applications. The existing information concerning these aspects has never been compiled so far. It is known that many of these fruits contain many bioactive compounds of industrial interest, such as carotenoids and phenolic constituents. Another aspect of the fruit is the high fatty acid content of some species. Pequi, bocaiuva, jatoba, baru, amburama, and buriti, for instance, are among those fruits described as being rich in fatty acids, mostly unsaturated ones. Here, we reviewed 18 species from the Brazilian savannah identified to be of interest because of high potencial for sustained medium- and short-term explorations, under the technological and biotechnological aspects, seeking the development of new products from these scarcely studied raw materials.

Biochemical characterization and evaluation of invertases produced from Saccharomyces cerevisiae CAT-1 and Rhodotorula mucilaginosa for the production of fructooligosaccharides

Abstract Invertases are used for several purposes; one among these is the production of fructooligosaccharides. The aim of this study was to biochemically characterize invertase from industrial Saccharomyces cerevisiae CAT-1 and Rhodotorula mucilaginosa isolated from Cerrado soil. The optimum pH and temperature were 4.0 and 70 °C for Rhodotorula mucilaginosa invertase and 4.5 and 50 °C for Saccharomyces cerevisiae invertase. The pH and thermal stability from 3.0 to 10.5 and 75 °C for R. mucilaginosa invertase, respectively. The pH and thermal stability for S. cerevisiae CAT-1 invertase from 3.0 to 7.0, and 50 °C, respectively. Both enzymes showed good catalytic activity with 10% of ethanol in reaction mixture. The hydrolysis by invertases occurs predominantly when sucrose concentrations are ≤5%. On the other hand, the increase in the concentration of sucrose to levels above 10% results in the highest transferase activity, reaching about 13.3 g/L of nystose by S. cerevisiae invertase and 12.6 g/L by R. mucilaginosa invertase. The results demonstrate the high structural stability of the enzyme produced by R. mucilaginosa, which is an extremely interesting feature that would enable the application of this enzyme in industrial processes.