Biochemical properties and evaluation of washing performance in commercial detergent compatibility of two collagenolytic serine peptidases secreted byAspergillus fischeriandPenicillium citrinum
| Autor: | Andre Rodrigues, Hamilton Cabral, Tatiane Beltramini Souto, Tássio Brito de Oliveira, Érika Lika Ida, Juliana Abigail Leite, Ronivaldo Rodrigues da Silva |
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| Přispěvatelé: | Universidade de São Paulo (USP), Universidade Estadual Paulista (Unesp) |
| Rok vydání: | 2016 |
| Předmět: |
0106 biological sciences
0301 basic medicine Proteases Detergents submerged fermentation Fungus 01 natural sciences Biochemistry protease application Serine 03 medical and health sciences chemistry.chemical_compound 010608 biotechnology Enzyme Stability parasitic diseases Organic matter Secretion Collagenases Penicillium citrinum Bioprocess chemistry.chemical_classification ENZIMAS PROTEOLÍTICAS biology Biochemical characterization Aspergillus fischeri Penicillium Temperature General Medicine Hydrogen-Ion Concentration biology.organism_classification Aspergillus 030104 developmental biology chemistry Metals Fermentation proteases Serine Proteases crude enzyme extract Biotechnology |
| Zdroj: | Scopus Repositório Institucional da UNESP Universidade Estadual Paulista (UNESP) instacron:UNESP Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP |
| ISSN: | 1532-2297 1082-6068 |
| DOI: | 10.1080/10826068.2016.1224247 |
| Popis: | Made available in DSpace on 2018-12-11T17:07:43Z (GMT). No. of bitstreams: 0 Previous issue date: 2017-03-16 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. Department of Pharmaceutical Sciences School of Pharmaceutical Sciences of Ribeirao Preto University of Sao Paulo Department of Biology Institute of Biosciences Letters and Exact Sciences Sao Paulo State University UNESP/IBILCE Department of Biochemistry and Microbiology Sao Paulo State University UNESP Department of Biology Institute of Biosciences Letters and Exact Sciences Sao Paulo State University UNESP/IBILCE Department of Biochemistry and Microbiology Sao Paulo State University UNESP |
| Databáze: | OpenAIRE |
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