ISSN:
1432-0614
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
,
Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
Notizen:
Summary The pH optimum of a crude preparation of lignin peroxidase was pH 3.1, whereas those of the three main isozymes of the enzyme purified from it were pH 2.2, pH 2.7 and pH 2.0. During the purification of the crude enzyme, an anionic polysaccharide containing fraction (PCF) was also separated. The latter was found to inhibit lignin peroxidase activity at pH values less than pH 3.2, thus resulting in a shift in the pH optimum of the purified isozymes back to a similar value as that obtained for the crude enzyme. Addition of divalent metal ions at 1.0 mM relieved the inhibition.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00256223
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