Caracterização bioquímica de amilases produzidas por Gongronella butleri, Thermoascus aurantiacus e Lichtheimia ramosa por cultivo em estado sólido

Abstract

The biocatalysts used in biotechnological processes are influenced by several factors, including: temperature, pH, reaction time, substrate and product concentration. The objective of this work was the characterization of the biochemistry of objective amylases by the filamentous fungicidal Gongronella butleri (mesophilic), Thermoascus aurantiacus (thermophilic) and Lichtheimia ramosa (mesophilic). The band amylase produced by the filamentous fungus Gongronella butleri shows activity at pH 5.0 at a temperature of 55º C, in relation to pH stability, an enzyme retained more than 78% of its original activity after being incubated for 24 hours at pH 3.0 at 10.5, in relation to its thermostability, it retained 80% of its catalytic activity after 1h at 40º C. As amylase by the filamentous agents Lichtheimia ramosa and Thermoascus aurantiacus showed optimal activity at pH 6.0 at temperatures of 60ºC. The amylase produced by L. ramosa was stable in the range of pH 3.5 to 10.5 and maintained its catalytic activity after 1 hour at 55º C, when incubated for the same period at 60º C, 75% of its original activity was recovered. The initial enzyme produced by T. aurantiacus was stable in the range of pH 4.5 and stable at a temperature of 9.5 and stable for 1 hour at a temperature of 50º C, when an enzyme was increased to 60º C, an enzyme presented only 25% of its activity. The amylase directed by G. butleri presented potential starches from distinct botanical sources (potato, mandiolisa, branches and wheat) as potential sources of treatment for T. aurantiacus and L. ramosa. The proposed results for further work, developed as different characteristics of different processes for the application of different processes.