Properties of laccases produced by Pycnoporus sanguineus induced by 2,5-xylidine.

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.

journal_name

Biotechnol Lett

journal_title

Biotechnology letters

authors

Garcia TA,Santiago MF,Ulhoa CJ

doi

10.1007/s10529-006-0026-3

subject

Has Abstract

pub_date

2006-05-01 00:00:00

pages

633-6

issue

9

eissn

0141-5492

issn

1573-6776

journal_volume

28

pub_type

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