| Literature DB >> 16642300 |
Telma Alves Garcia1, Mariângela Fontes Santiago, Cirano José Ulhoa.
Abstract
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 degrees C, and Lac II was at pH 4.2 and 50 degrees C over 5 min reaction. The Km values of enzymes toward syringaldazine were 10 microM: (Lac I) and 8 microM: (Lac II). Sodium azide inhibited Lac I (85%) and Lac II (75%) activities.Entities:
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Year: 2006 PMID： 16642300 DOI： 10.1007/s10529-006-0026-3
Source DB: PubMed Journal: Biotechnol Lett ISSN： 0141-5492 Impact factor: 2.461