Collagenase Production from <i>Aspergillus serratalhadensis</i> URM 7866 Using Industrial By-Products: Purification and Characterization
Luiz Henrique Svintiskas Lino | Kethylen Barbara Barbosa Cardoso | Pietra Gícia Oliveira Cosmo da Silva | Raphael Luiz Andrade Silva | Maria Eduarda Luiz Coelho de Miranda | Daniel Charles dos Santos Macêdo | Ana Lúcia Figueiredo Porto | Cristina Maria de Souza Motta | Marcia Nieves Carneiro da Cunha | Thiago Pajéu Nascimento | Carolina de Albuquerque Lima Duarte | Romero Marcos Pedrosa Brandão Costa | Daniela de Araújo Viana Marques
Collagenases are enzymes with broad biotechnological applications in medicine. This study describes the production and characterization of a collagenase from <i>Aspergillus serratalhadensis</i> URM 7866, isolated from the Caatinga biome. Solid-state fermentations were conducted using wheat bran under varying conditions of pH (6, 7, 8), moisture content (50%, 60%, 70%), and substrate concentration (2.5 g, 5 g, 10 g). The optimal condition—10 g of wheat bran at pH 8 and 70% moisture—yielded the highest collagenolytic activity (177.96 U/mL) and a specific activity of 50.55 U/mg. The enzyme was purified via multiple chromatography, with pre-purification and final purification factors of 18.09 and 20.21, respectively, reaching a specific activity of 1021.86 U/mg. The enzyme showed optimal activity at 50 °C and pH 8, with stability from 20 to 40 °C and pH 7–9. PMSF caused >80% inhibition; EDTA caused ~34% inhibition. Activity increased with Na<sup>+</sup> and Ca<sup>2+</sup> and was inhibited by Zn<sup>2+</sup>. The enzyme retained full activity in anionic and non-ionic surfactants (1–10%). FTIR confirmed characteristic amide bands, and kinetic analysis revealed a Km of 1.72 mg/mL and Vmax of 6.89 mg/mL/min. These findings support its potential for alkaline and surfactant-rich industrial processes.
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