A novel laccase gene isolated from Bacillus pumilus TCCC 11568 was expressed, and the recombinant laccase (rLAC) displayed maximal activity at 80 °C and at pH 6.0 against ABTS. rLAC maintained its structural integrity at a high temperature (355 K) compared to its tertiary structure at a low temperature (325 K), except for some minor adjustments of certain loops. However, those adjustments were presumed to be responsible for the formation of a more open access aisle that facilitated the binding of ABTS in the active site, resulting in a shorter distance between the catalytic residue and the elevated binding energy. Additionally, rLAC showed good thermostability (≤70 °C) and pH stability over a wide range (3.0–10.0), and displayed high efficiency in decolorizing azo dyes that are applicable to the food industry. This work will improve our knowledge on the relationship of structure–function for thermophilic laccase, and provide a candidate for dye effluent treatment in the food industry.

No abstract