Laccases have a huge potential in numerous environmental and industrial applications due to the ability to oxidized a wide range of substrates. Here, a novel laccase gene from the identified Bacillus velezensis TCCC 111904 was heterologously expressed in Escherichia coli. The optimal temperature and pH for oxidation by recombinant laccase (rLac) were 80 °C and 5.5, respectively, in the case of the substrate 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), and 80 °C and 7.0, respectively, in the case of 2,6-dimethoxyphenol (2,6-DMP). rLac exhibited high thermostability and pH stability over a wide range (pH 3.0, 7.0, and 9.0). Additionally, most of the metal ions did not inhibit the activity of rLac significantly. rLac showed great tolerance against high concentration of NaCl, and 50.8% of its initial activity remained in the reaction system containing 500 mM NaCl compared to the control. Moreover, rLac showed a high efficiency in decolorizing different types of dyes including azo, anthraquinonic, and triphenylmethane dyes at a high temperature (60 °C) and over an extensive pH range (pH 5.5, 7.0, and 9.0). These unique characteristics of rLac indicated that it could be a potential candidate for applications in treatment of dye effluents and other industrial processes.
Keywords: Bacillus velezensis; Decolorization; Dye effluents; Enzymatic characterization; Laccase.
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