Stability lignin peroxidase

Reactivity of the Oxycomplex. The oxycomplex of lignin peroxidase does not react with veratryl alcohol, one of the lignin peroxidase substrates. Furthermore, the stability of the oxycomplex is not affected by veratryl... 

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),... 

A detailed scientific study on the properties of the five major isozymic forms of the lignin peroxidases produced in our pilot reactor has recently been published 12), Our purified enzyme in this study is composed of two isozymes having isoelectric points of 3.85 and 3.80 and molecular masses of 42 000. In this study we have characterized the enzyme s stability as an industrial product. 

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. 

Khindaria A, Yamazaki I, Aust SD (1996) Stabilization of the veratryl alcohol cation radical by lignin peroxidase. Biochemistry 35 6418-6424... 

J.H., and Lee, E.K. (2008) Functionality improvement of fungal lignin peroxidase by DNA shuffling for 2,4-dichlorophenol degradability and HjOj stability. ]. 

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]. 

Tuisel, H., R. Sinclair, J. A. Bumpus, W. Ashbaugh, B. J. Brock, and S. D. Aust. 1990. Lignin peroxidase H2 from Phanerochaete chrysosporium purification, characterization and stability to temperature and pH. Arch. Biochem. Biophys. 279 158-166. 

The further reactions of monolignols in the plant cell wall to form lignin may occur through an initial laccase or peroxidase oxidation of the monolignol giving rise to a resonance-stabilized phenoxy radical as depicted in Fig. 9.4 [10-12]. This step is followed by a coupling reaction and model experiments have shown that the first product, the... 

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