Aims: The objective of this work was to purify the tyrosinase from Bacillus thuringiensis subsp. kurstaki (Bt) (CCTCC AB 90010) and study its enzymatic properties. Methods and Results: A 'one-step' purification method was used in this work, which was an easy, high-yield purification method. Tyrosinase activity of this purity was measured under different conditions to study its kinetic characterizations. The optimum pH and thermal stability of this enzyme were also determined. The results revealed that the tyrosinase from Bt has distinct properties compared with those from other sources. Conclusions: A heat-inducible tyrosinase of a wild strain of Bt was identified and partially characterized. Significance and Impact of the Study: The distinct properties of Bt tyrosinase are important to the application of Bt as a biology pesticide.

Although two kinds of Liobagrus marginatoides should belong to the same species according to the taxonomy of fish morphology, the results of cytogenetic analysis showed they are two different races.