Lignin peroxidase stability effects

Effect of Veratiyl Alcohol. At pH 5.0 the purified lignin peroxidase was not inactivated under the conditions tested. At pH 3.0 the enzyme lost its activity when incubated at 20°C for 38 days, and the presence of veratryl alcohol could not stabilize it. 100 mM veratryl alcohol even inactivated the enzyme to some extent. Ionic strength did not significantly affect the activities. The effect of veratryl alcohol was the same when unfractionated enzyme was used. This time the ionic strength in the activity assay mixture affected the activities, probably because one enzyme in the unfractionated preparation is sensitive to high ionic strength 12),... 

Aitken and Irvine 17) have recently reported on the stability characteristics of lignin peroxidases. They also have shown that the enzyme was most stable at pH 4.5, although higher pH values were not tested. The stability was dependent on protein concentration and veratryl alcohol had a stabilizing effect. The latter result was contrary to our experience. 

Water/TX-100/[C mim][PF ] microemulsions were used as reaction media in enzymatic reactions. The catalytic activities of alcohol dehydrogenase in this ternary system were determined, and it was found to be greatly improved as compared with those in pure [Bmim][PF ] [62].The same system was used in order to analyze the effect on the catalytic activity of lignin peroxidase and laccase [63]. The catalytic behavior and stability of lipases from Candida rugosa, Chromobacterium viscosum, and Thermomyces lanuginosa in these microemulsions were investigated and compared to other microheterogeneous media used so far for enzyme-catalyzed reactions [64]. 

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