title: Biochemical properties and evaluation of washing performance in commercial detergent compatibility of two collagenolytic serine peptidases secreted by Aspergillus fischeri and Penicillium citrinum.
abstract: 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 168 h with 760 U/mL, in comparison with the fungus A. fischeri, which reached a peak production at 72 h with 460 U/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°C, while the one secreted by A. fischeri had optimal activity in pH 6.5-8 and at 55-60°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°C for 1 h, 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.
authors.affiliation: a Department of Pharmaceutical Sciences, School of Pharmaceutical Sciences of Ribeirao Preto , University of Sao Paulo , Ribeirao Preto , Brazil.
authors.forename: Érika Lika
authors.initials: ÉL
authors.lastname: Ida
authors.affiliation: b Department of Biology , Institute of Biosciences, Letters and Exact Sciences, Sao Paulo State University, UNESP/IBILCE , Sao Jose do Rio Preto , Brazil.
authors.forename: Ronivaldo Rodrigues
authors.initials: RR
authors.lastname: da Silva
authors.affiliation: c Department of Biochemistry and Microbiology , Sao Paulo State University, UNESP , Rio Claro , Brazil.
authors.forename: Tássio Brito
authors.initials: TB
authors.lastname: de Oliveira
authors.affiliation: a Department of Pharmaceutical Sciences, School of Pharmaceutical Sciences of Ribeirao Preto , University of Sao Paulo , Ribeirao Preto , Brazil.
authors.forename: Tatiane Beltramini
authors.initials: TB
authors.lastname: Souto
authors.affiliation: a Department of Pharmaceutical Sciences, School of Pharmaceutical Sciences of Ribeirao Preto , University of Sao Paulo , Ribeirao Preto , Brazil.
authors.forename: Juliana Abigail
authors.initials: JA
authors.lastname: Leite
authors.affiliation: c Department of Biochemistry and Microbiology , Sao Paulo State University, UNESP , Rio Claro , Brazil.
authors.forename: André
authors.initials: A
authors.lastname: Rodrigues
authors.affiliation: a Department of Pharmaceutical Sciences, School of Pharmaceutical Sciences of Ribeirao Preto , University of Sao Paulo , Ribeirao Preto , Brazil.
authors.forename: Hamilton
authors.initials: H
authors.lastname: Cabral
mesh_terms: D001230:Aspergillus / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D017364:Collagenases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D003902:Detergents / Q000378:metabolism; D004795:Enzyme Stability; D005285:Fermentation; D006863:Hydrogen-Ion Concentration; D008670:Metals / Q000378:metabolism; D010407:Penicillium / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D057057:Serine Proteases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D013696:Temperature
chemical_list: D003902:Detergents; D008670:Metals; D057057:Serine Proteases; D017364:Collagenases
keywords: Biochemical characterization; crude enzyme extract; protease application; proteases; submerged fermentation