Aquaculture by-product: a source of proteolytic enzymes for detergent additives
| Autor: | Chirleanny Maciel Mendes, Tatiana Souza Porto, Marília A. Brito, Maria G. Carneiro-da-Cunha, Ana M. A. Caneiro-Leão, Ana Lúcia Figueiredo Porto, Luiz B. Carvalho, Ranilson de Souza Bezerra |
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| Rok vydání: | 2009 |
| Předmět: |
Chromatography
biology Chemistry General Chemical Engineering Sodium Proteolytic enzymes Substrate (chemistry) chemistry.chemical_element General Chemistry Biochemistry Industrial and Manufacturing Engineering Enzyme assay chemistry.chemical_compound Hydrolysis Casein Materials Chemistry biology.protein Hydrogen peroxide Laundry detergent |
| Zdroj: | Chemical Papers. 63 |
| ISSN: | 1336-9075 |
| DOI: | 10.2478/s11696-009-0081-z |
| Popis: | Intestine proteases of Nile tilapia (Oreochromis niloticus) were partially purified by heat treatment (purification factor of 3.5, enzyme activity remained almost constant) to reach the maximum activity and stability within an alkaline pH range of 7.2–11.0. The optimum temperature and stability over a 120 min period were found to be at 55°C and at 35–45°C, respectively. The proteases’ activity was not affected by a 1 vol. % saponin surfactant, inactivated by 0.01 g mL−1 sodium dodecylsulphate after 120 min, and it remained stable for 30 min in a 5 vol. % and 10 vol. % hydrogen peroxide solutions. The proteases were slightly activated by Ca2+, Mg2+, and K+ and the substrate most effectively hydrolysed was casein (40.0 U mg−1). A 24 full factorial design used to evaluated the influence of independent variables showed that the enzyme extract, detergent concentration and the incubation time had a significant influence on the enzymatic activity. The best conditions to be used concerning detergent additive were found with 0.3 mg mL−1 of protein and 3.0 mg mL−1 of detergent for 30 min in the presence of Astrus® detergent. |
| Databáze: | OpenAIRE |
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