Research Article 
Inducers and Inhibitors of Laccase from Penicillium
Hamed M. El-Shora, Magdy M. Youssef and Salwa A. Khalaf
Biotechnology, 2008, 7(1), 35-42.
Abstract
The objectives of the present research was to enhance laccase production by Penicillium aculeatum, P. digitatum and P. cyclopium. The effects of different inducers such as guaiacol, caffeic acid, syringaldazine and sinapinic acid were investigated. The procedure developed for laccase purification enabled us to obtain enzymic preparations purified 250, 360 and 400 fold from P. aculeatum, P. digitatum and P. cyclopium, respectively. Phenylmercuric acetate (PMA), 5,5-dithiobis (2-nitrobenzoic acid) (DTNB) and p-chloromercuribenzoate (PCMB) inhibited the activity of laccase. The inhibition by the three thiol-group reagents supports the idea that cysteinyl residues at the binding sites are important for the enzyme activity. Treatment of laccase with histidine selective reagent, diethylpyrocarbonate (DEPC) resulted in simple linear pseudo-first-order kinetics. The order of the inactivation kinetics and the protection by the substrate revealed that histidine is at the active site and taking part in the enzyme activity. The results show that desferal (desferrioxamine mesylate) is an inhibitor of laccase. The inhibitory effect was not dependent on the nature of the prosthetic group. Its use as an inhibitor of laccase, is promising since desferal seems to deactivate phenoxy radicals formed by the action phenol-oxidizing enzymes.
ASCI-ID: 11-351
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