Recently, researchers from S. N. Bose National Center for Basic Sciences (SNBNCBS), Kolkata, tested the efficacy of the laccase enzyme in degrading some standard dye molecules.


About Enzyme Laccase

  • Laccase is generated by a group of fungi that have been found capable of degrading a variety of hazardous organic dye molecules that are regularly drained into waterbodies after dying clothes in the textile industry.
  • This observed characteristic which the scientists termed substrate promiscuity can have deep implications in designing enzyme-coated cassettes for treating heavily dye-polluted water.
  • Laccase was known for its capacity to degrade various organic molecules.
  • Laccase, generated by a group of fungi, contains 4 copper atoms in two different oxidation states, and degrades substrates through redox reactions, producing only water and the simplest non-virulent or less virulent oxides of carbon, nitrogen and sulphur.  
  • Hence the scientists saw scope in using it to develop a technology to treat/degrade the dye effluents emanating from textile industries.
  • Combining UV/Visible spectroscopy and computer simulations they demonstrated that many organic dye molecules with varying kinetics and wide variation in charge, size and shape can be degraded by the enzyme laccase.
  • This substrate promiscuity of laccase offers immense biotechnological potential for a broad-spectrum degrader for industrial dye effluents.


What is enzyme promiscuity?

  • Enzyme promiscuity is defined as the capability of an enzyme to catalyze a reaction other than the reaction for which it has been specialised.
  • Although the enzyme is known for its specificity, many enzymes are reported to be promiscuous.


What are enzymes?

An enzyme is a substance that acts as a catalyst in living organisms and regulates the rate at which chemical reactions proceed without being altered in the process.