Fermentation, Vol. 11, Pages 478: Collagenase Production from Aspergillus serratalhadensis URM 7866 Using Industrial By-Products: Purification and Characterization

Fermentation doi: 10.3390/fermentation11080478

Authors:
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 Aspergillus serratalhadensis 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+ and Ca2+ and was inhibited by Zn2+. 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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