PRODUCTION AND PURIFICATION STRATEGIES FOR LACCASE

Laccase belongs to polyphenol oxidases, which is a very wide family of copper-containing atoms in the center, which serves as the catalytic site. It is biochemically a glycoprotein with molecular mass being between 50kda to 130kda and 30% carbohydrate content, in addition to this it has three types of copper atoms. It is one of the most important enzymes due to its role in the food industry. It acts as a biosensor where it can detect morphine, codeine, catecholamine, and many other enzymes. In insects, it performs the function of cuticle sclerotization. Moreover, laccase is safe for human consumption. The most important factor which has prevented laccase from being insanely famous is the cost that is associated with using a very large quantity of laccase. Laccases can be extracted from almost all kinds of white-rot fungi as well as from various other fungi species such as Pycnoporus cinnabarinus, Gloeophyllum trabeum but not in any brown-rot species except Coniophora puteana as was recently discovered. Aspergillus niger, Aspergillus oryzae and Trichoderma reesei also produce laccases due to the laccase producing genes introduced in them. Botryo sphaeria is a true laccase producing fungi, not only this, it can also be extracted from plants, bacteria such as Escherichia coli, Bacillus halodurans but not much work has been done on any other organism except fungi. Bacterial laccase is highly thermos-tolerant and functions in neutral to alkaline conditions, while fungal laccase, on the other hand, does not function at high temperature and pH.