| Autor: |
Garcia, Telma Alves, Santiago, Mariângela Fontes, Ulhoa, Cirano José |
| Předmět: |
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| Zdroj: |
Biotechnology Letters; May2006, Vol. 28 Issue 9, p633-636, 4p |
| Abstrakt: |
Two isoforms of laccase produced from the culture supernatant of Pycnoporus sanguineus were partially purified by phenyl-Sepharose chromatography. Molecular masses of the enzymes were 80 kDa (Lac I) and 68 kDa (Lac II). Optimum activity of Lac I was at pH 4.8 and 30 °C, and Lac II was at pH 4.2 and 50 °C over 5 min reaction. The Km values of enzymes toward syringaldazine were 10 μM (Lac I) and 8 μM (Lac II). Sodium azide inhibited Lac I (85%) and Lac II (75%) activities. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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