Sequencing and Characterization of Laci gene of Ganoderma lucidum [manuscript]
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Date
2017
Authors
Jennifer T. Casabar
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Abstract
Laccases are multicopper enzymes belonging to the group of blue oxidases that has been known due to its potential functions in detoxification, wine stabilization, paper processing, textile dye bleaching, pulp bleaching, detergents and enzmatic conversion of chemical intermediates. These lacases can completely mineralized by white-rot fungi like G. lucidum. In this study, new sets of primers were designed from the converved regions of the nucleotide sequences of lacases gene from different Ganoderma species using Primer3. The LACI gene obtained from the mycelia of G. lucidum collected from CTMRD was successfully isolated with a 550 bp long of nucleotide sequence. The amplified partial LACI gene had 79% similarity to G. lucidum laccase with an accession number of DQ914869.1 and found to had 85% similarity to G. weberianum laccase with an accession number of KF384100.1. The percentage homology of the obtained sequence to other fungal laccases ranged from 60% to 85%. In the nucleotide percentage identify matrix done with Clustal 2.1, there was 57.73% homology of lacases between GL_LACI and G. lucidum (DQ914869.1) and particularly it has approximately 255 polymorphisms within the amplified region. On the other hand, there was 56.35% homology between the laccases of GL_LACI and G. weberianum (KF384100.1) and GL_LACI had-295 polymorphisms as compared to G. weberianum. LAC1 gene obtained from G. lucidum is distant relative to other laccases isolated and supported the idea that G. lucidum is distant relative to other laccases isolated and supported the idea that G. lucidum has a complex structure that made it unique among other Ganoderma species.