| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7086323 | Bioresource Technology | 2012 | 7 Pages |
Abstract
⺠A novel extracellular protease was purified and characterized kinetically. ⺠Optimum kcat/Km-value of novel protease was found at pH 7.75 and 35.5 °C. ⺠This enzyme maintained full activity at 25 °C after 30 min incubation at 10 or 60 °C. ⺠The Km-value of novel enzyme was decreased at increased [Ca2+] and/or [NaCl]. ⺠All proton inventories suggest that catalysis proceeds via a charge-relay system.
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Authors
Athanasios Foukis, Panagiota-Yiolanda Stergiou, Leonidas G. Theodorou, Maria Papagianni, Emmanuel M. Papamichael,