| Autor: | A. Yonetsu, Teizi Urakami, Y. Oda, Kenzo Tonomura |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
chemistry.chemical_classification
Proteases Environmental Engineering Protease Materials science Polymers and Plastics biology medicine.medical_treatment Proteinase K Lactic acid chemistry.chemical_compound Hydrolysis Enzyme chemistry Biochemistry Keratin Materials Chemistry medicine biology.protein Specific activity |
| Zdroj: | Journal of Polymers and the Environment. 8:29-32 |
| ISSN: | 1566-2543 |
| Popis: | Fifty-six commercially available proteases were tested for polylactide-degrading activity. Little or no activity was found in acid and neutral proteases, while some alkaline proteases formed appreciable amounts of lactic acid from polylactide. These polylactide-degrading proteases were derived from Bacillus species and had catalytic activity even under neutral, as well as alkaline, conditions. Savinase (Novo Nordisk) degraded polylactide the fastest among the enzymes tested and its specific activity corresponded to about one-half of proteinase K. Polylactide-degrading activity was not always present in the enzymes that affected keratin, while polylactide-degrading proteases commonly hydrolyzed keratin. A significant correlation was observed between degrading activities of polylactide and keratin in alkaline proteases. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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