Biochemical properties and evaluation of washing performance in commercial detergent compatibility of two collagenolytic serine peptidases secreted by Aspergillus fischeri and Penicillium citrinum

Autor(es)

Ida, Erika Lika ; da Silva, Ronivaldo Rodrigues ; de Oliveira, Tassio Brito ; Souto, Tatiane Beltramini ; Leite, Juliana Abigail ; Rodrigues, Andre ; Cabral, Hamilton

• Tipo de documento: Artigo Científico
• Fonte: PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY; v. 47, n. 3, p. 282-290, 2017.
• Citações Web of Science: 5

Resumo

Filamentous fungi secrete diverse peptidases with different biochemical properties, which is of considerable importance for application in various commercial sectors. In this study, we describe the isolation of two fungal species collected from the soil of decayed organic matter: Aspergillus fischeri and Penicillium citrinum. In a submerged bioprocess, we observed better peptidase production with the fungus P. citrinum, which reached a peak production at 168h with 760U/mL, in comparison with the fungus A. fischeri, which reached a peak production at 72h with 460U/mL. In both situations, the fermentative medium contained 0.5% crushed feathers as a source of nitrogen. On performing biochemical characterization, we detected two alkaline serine peptidases: The one secreted by P. citrinum had optimal activity at pH 7.0 and at 45 degrees C, while the one secreted by A. fischeri had optimal activity in pH 6.5-8 and at 55-60 degrees C. Metallic ions were effective in modulating these peptidases; in particular, Cu2+ promoted negative modulation of both peptidases. The peptidases were stable and functional under conditions of nonionic surfactants, temperatures up to 45 degrees C for 1h, and incubation over a wide pH range. In addition, it was observed that both peptidases had the capacity to hydrolyze collagen and performed well in removing an egg protein stain when supplemented into a commercial powder detergent; this was especially true for the peptidase from P. citrinum. (AU)

• Processo FAPESP: 11/06986-0 - Determinação da especificidade de peptidases isoladas de fungos usando peptídeos FRET como substratos
• Beneficiário: Hamilton Cabral
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 12/24703-8 - Análises proteômicas de fungos filamentosos meso e termofílicos expostos aos fatores físico e químico
• Beneficiário: Hamilton Cabral
• Modalidade de apoio: Auxílio à Pesquisa - Regular