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Updated: Dec 11, 2025

Functional Cloning Using a Xenopus Oocyte Expression System
Published on: January 30, 2016
[Cloning, Expression, and Characterization of Novel Laccase Enzyme from Native Bacillus subtilis Strain OH67]
O Hajipour1,2, N Mercan Dogan1, S Dincer3
1Department of Biology, Faculty of Science and Arts, Pamukkale University, Denizli, 20160 Turkey.
Abstract:
Bacterial laccases are very stable at high temperature and high pH values, and have many biotechnological and industrial applications. Here we describe how we cloned, expressed and purified the laccase from Bacillus subtilis (B. subtilis). The enzyme molecular weight has been determined as 34 kDa in SDS-PAGE analysis. The activity of the recombinant enzyme has been proved by guaiacol oxidation. The KM and Vmax values of the enzyme were at 1.1077 mM and at 19.3 μmol/min/mg, respectively. The recombinant laccase was effective in the decolorization of Turquoise blue HF6, Remazol red 106, Remazol brilliant orange 3R, and Brilliant blue, thus, possessing the characteristics necessary for its possible application in textile and environmental industries.

