+44 330 818 7254Goldbeck R, Andrade CCP, Ramos MM, Pereira GAG, Maugeri Filho F
Explorations of biodiversity in the search for new biocatalysts by selecting microorganisms from nature represents a method for discovering new enzymes which may permit the development of bio-catalysis on an industrial scale. In face this, the objective of the present study was to identify and characterize cellulases produced by Acremonium strictum AAJ6 isolated from samples collected from different Brazilian biomes. The microorganism was cultivated in medium containing microcrystalline cellulose (Avicel), at temperature of 30°C and 150 rpm agitation for 240 h. After induction of enzymes, four specific activities were evaluated: endoglucanase (CMCase), total activity (filter paper activity), cellobiase and b-glucosidase. The optimal temperature and pH of the enzymes were determined using the central composite rotational design (CCRD). For the identification of cellulases produced by Acremonium strictum, the purified protein was subjected to trypsin digestion and analyzed by liquid chromatography coupled with mass spectrometry (LC-MS/MS). The peptides identified in the mass spectrometry were searched against the CAZy database and two potential cellulolytic enzymes were identified: endoglucanase Cel74a and β-glucosidase. This work shows not only studies of enzymatic characterization, but also the importance of the biodiversity exploitation for the identification of new microorganisms and new enzymes with potential application biotechnological
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