Amino acid supplementation improves the production of extracellular peptidases by aspergillus section flavi and their ionic immobilization

Bioprocess studies have been highlighted due to the importance of physiological processes and industrial applications of enzymes. The potential of peptidase production from Aspergillus section Flavi using different amino acids as a supplemental nitrogen source was investigated. A production profile revealed that amino acids had positive effects on peptidase production when compared to the control without amino acids. Optimal production (100 U/mL) was obtained with Arginine amino acid in 96 h of fermentation. Extracellular peptidase from Aspergillus section Flavi was identified in submerged bioprocesses by in situ activity. Biochemical studies revealed that the maximum activities of the enzyme extract were obtained at pH 6.5 and a temperature of 55°C. The inhibition by EDTA and PMSF suggests the presence of more than one peptidase while the Ni2+ and Cu2+ had a negative influence on the enzyme activity. When the crude extract was reversibly immobilized on ionic supports, DEAE-Agarose and MANAE-Agarose the derivative showed different profiles of thermal and pH stabilities. Hence, this study revealed the basic properties and biochemical characteristics that allowed the production improvement of this class of enzyme. Moreover, with known properties stabilization and immobilization process is required to further explore its biotechnological capacities.

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Bibliographic Details
Main Authors: Gonsales da Rosa-Garzon, Nathalia, Rodrigues Siqueira, Ana Claudia, Hirano, Viviane Naomi, Rodrigues, André, Pessela, Benevides C., Cabral, Hamilton
Other Authors: Fundação de Amparo à Pesquisa do Estado de São Paulo
Format: artículo biblioteca
Language:English
Published: Instituto de Tecnologia do Paraná 2020
Subjects:Filamentous fungi, Protease, Immobilization, Submerged bioprocess, MANAE-agarose,
Online Access:http://hdl.handle.net/10261/219991
http://dx.doi.org/10.13039/501100003593
http://dx.doi.org/10.13039/501100002322
http://dx.doi.org/10.13039/501100001807
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