ATIVIDADE ENZIMÁTICA DE FUNGOS PRESENTES EM CAULES DE ÁRVORES FRUTÍFERAS DO CERRADO GOIANO

Abstract

The Cerrado is considered one of the most biodiverse savannas in the world. Despite the studies that exist aimed to understand mycology, few are the works that aim to elucidate the enzymatic profile produced by filamentous fungi associated with the biome. The objective of this study was to evaluate the proteolytic and pectinolytic activities of fungal isolates from the stalk of six fruit trees: Pequi, Mangabeira, Lobeira, Muricizeiro, Monkey pepper and Marmalade. Eighteen fungal strains, in triplicate, were submitted to enzymatic assay according to the adapted methodologies of Strauss et al. (2001) and Brizzio et al. (2007), in different periods (24, 48 and 72 hours). For data treatment, a completely randomized design was used and non-parametric tests were applied, Friedman (α = 5%) (Effect of incubation periods) and Kruskal-Wallis (α = 5%) (substrate source). The fungal isolates had a higher index of pectinolytic activity at 24 and 48 hours of incubation (P<0.05). The epiphytic strains in casein medium had higher enzymatic activity index (P<0.01), about native plant, the marmalade isolates had higher enzymatic index in the respective medium, while those of the strains originated from the Lobeira, Mangabeira and Pequi showed low indices (P<0.01). All fungal isolates presented relevant enzymatic activity, in prominence, the strains of the genus Malbranchea spp. obtained a higher index of proteolytic activity (P<0.01) and pectinolytic, in conjunction with Aspergillus spp. and Aureobasidium spp. (P<0.05). Therefore, it is concluded that the fungal isolates from the Cerrado have enzymatic potential. As the genus Malbranchea spp. presented higher indices of proteolytic activity it is the most suitable for conducting future enzymatic tests aiming the application of enzymes. As for the other isolates, it is suggested the development of new researches in order to analyze optimal conditions to produce proteases and pectinases.