2006
DOI: 10.1007/s11274-006-9233-2
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Enhanced production of laccase activity by Trametes versicolor immobilized into alginate beads by the addition of different inducers

Abstract: In the present paper the effect of adding veratryl alcohol and copper sulphate on laccase activity production by Trametes versicolor immobilized into alginate beads has been investigated. Employing copper sulphate as laccase inducer or supplementing the culture medium with veratryl alcohol, led to maximum values of laccase activity. However, the highest laccase activity (around 4,000 U l -1 ) was obtained in cultures simultaneously supplemented with copper sulphate (3 mM) and veratryl alcohol (20 mM). These va… Show more

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Cited by 41 publications
(23 citation statements)
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“…pH optimums for free and immobilized laccase T. versicolor range from pH 3.0 to 5.5. In contrast to our results, immobilization mostly causes pH optimum to move about pH 0.5 higher 11,15,27,28 . Decrease in activity from pH optimum to pH 2.5 and 6.2 is similar as in articles 10,11 .…”
contrasting
confidence: 99%
“…pH optimums for free and immobilized laccase T. versicolor range from pH 3.0 to 5.5. In contrast to our results, immobilization mostly causes pH optimum to move about pH 0.5 higher 11,15,27,28 . Decrease in activity from pH optimum to pH 2.5 and 6.2 is similar as in articles 10,11 .…”
contrasting
confidence: 99%
“…Also, heterotrophic bacteria could simply use the protein laccase as substrate [48], which might be another reason for the decrease in laccase activity in the real wastewater. It is noteworthy that the compounds which are usually used in the defined WRF media to induce laccase activity, such as Cu 2+ [49], Mn 2+ [50] or veratryl alcohol [51], were not used in this study. Although only laccase was assayed as the fungal enzyme in this study, the involvement of other enzymes like MnP should not be neglected.…”
Section: Discussionmentioning
confidence: 99%
“…Finding of these structural specificities would be important to know the exact mechanism of pesticide degradation by laccase. Structural influence of xenobiotic on the extent of their degradation by laccase was mentioned by Dominguez et al (2007), particularly for PAH structures (anthracene, benzo pyrene, pbenzoquinone and phenanthrene), indicating the specificity of enzyme towards these substrates. Different laccases differ considerably in their catalytic preferences.…”
Section: Resultsmentioning
confidence: 99%