Abstract:Laccase is a kind of polyphenol oxidase, and it has important application values in food, energy, environment industries and other fields. A mutant strain from wild Coriolopsis gallica was selected, and its morphological characteristics were very different from the wild strain. The production of laccase by the mutant was up to 303 U/mL, which was three times higher than that by the wild strain. In this article, the physiological and biochemical differences between the wild and mutant, and their genetic differences with RAPD were compared and analyzed. Twenty stable specific bands were amplified with 140 random primers, and three of them were recovered and cloned. Then comparison analysis of their sequencing results with BLASTX, NCBI database showed that the 809 bp band from primer S381 was corresponding to a hypothetical protein of Trametes versicolor. The 654 bp band from primer S225 was corresponding to 30 S ribosomal protein S4 of Oribacterium sp, and the 1027 bp band from primer S193 was corresponding to glycoside hydrolase of Dichomitus squalens. This test would provide a theoretical basis for investigating molecular mechanism of the mutant yielding high laccase, and building high yield laccase engineering stain by directed mutation.
