Laccase has been used for many projects over the years because of its wide range of substrate differing from lignin to other aromatic compounds. This feature makes this enzyme one of the most promising biological solutions for optimising the degradation of industrial waste. Our aim is to design a signal peptide for T. versicolor laccase enzyme and then integrate the gene that codes this signal peptide sequence in Escherichia coli. PelB will be the signal peptide that will direct the laccase enzyme to the periplasmic domain in the E. coli Shuffle strain, facilitating the formation of disulphide bonds, thus increasing its activity and stability. We also plan to use disulphate bonding isomerase (dbs) on other group to see if it is more effective than leading laccase to the periplasm. This way, we will overcome the yield problem that creates a bottleneck for industrial use.