Collagenase Production from Aspergillus serratalhadensis URM 7866 Using Industrial By-Products: Purification and Characterization

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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Journal
Fermentation
Published
2025-08-20
DOI
https://doi.org/10.3390/fermentation11080478
Citations
1
Primary Topic
Enzyme Production and Characterization
Type
article
Field-Weighted Citation Impact
1.23

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article

Collagenase Production from Aspergillus serratalhadensis URM 7866 Using Industrial By-Products: Purification and Characterization

Daniel Charles dos Santos Macêdo, Daniela de Araújo Viana Marques, Ana Lúcia Figueiredo Porto, Raphael Luiz Andrade Silva et al.
1 citations
Fermentation
Enzyme Production and Characterization
1.23
article

Collagenase Production from Aspergillus serratalhadensis URM 7866 Using Industrial By-Products: Purification and Characterization

Daniel Charles dos Santos Macêdo, Daniela de Araújo Viana Marques, Ana Lúcia Figueiredo Porto, Raphael Luiz Andrade Silva, Pietra Gícia Oliveira Cosmo da Silva, Márcia Nieves Carneiro da Cunha, Thiago Pajeú Nascimento, Romero Marcos Pedrosa Brandão Costa, Luiz Henrique Svintiskas Lino, Kethylen Bárbara Barbosa Cardoso, Cristina Maria de Souza‐Motta, Maria Eduarda Luiz Coêlho de Miranda, Carolina Duarte
article en
1 citations

Abstract

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.

FermentationVol. 11(8)
Universidade Federal de Pernambuco (BR), Universidade Federal do Piauí (BR), Universidade Federal Rural de Pernambuco (BR), Universidade de Pernambuco (BR)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior, Conselho Nacional de Desenvolvimento Científico e Tecnológico, Fundação de Amparo à Ciência e Tecnologia do Estado de Pernambuco
Openalex Percentile: Top 19%
Enzyme Production and Characterization
1.23
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