Context:
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.
Relevance:
GS III: Science and Technology
Dimensions of the Article:
- What are enzymes?
- Laccase Enzyme for Dye Effluent Treatment
- Enzyme promiscuity
What are enzymes?
- Enzymes are biological molecules, typically proteins, that act as catalysts in living organisms.
- They regulate the rate at which chemical reactions occur without being consumed or permanently altered in the process.
- Enzymes are involved in various metabolic processes, including digestion, respiration, and the synthesis of complex molecules like DNA and proteins.
- They play a crucial role in maintaining the chemical balance within cells and are essential for life.
- Enzymes are highly specific in their action and are able to catalyze specific chemical reactions by binding to specific substrates, or reactant molecules.
Laccase Enzyme for Dye Effluent Treatment
The laccase enzyme, produced by certain fungi, has the ability to degrade hazardous organic dye molecules found in water bodies polluted by textile industry effluents. This characteristic, known as substrate promiscuity, has significant potential for developing enzyme-coated cassettes to treat heavily dye-polluted water.
Key points:
- Laccase is generated by certain fungi and is known for its ability to degrade various organic molecules.
- Laccase contains 4 copper atoms in two different oxidation states and degrades substrates through redox reactions, producing only water and non-virulent or less virulent oxides of carbon, nitrogen, and sulfur.
- The substrate promiscuity of laccase allows for the degradation of various organic dye molecules with varying kinetics, charge, size, and shape.
- The combination of UV/Visible spectroscopy and computer simulations has shown the potential for laccase to be used in the development of technology to treat and degrade dye effluents from textile industries.
- The substrate promiscuity of laccase offers immense biotechnological potential as a broad-spectrum degrader for industrial dye effluents.
Enzyme promiscuity
- Enzyme promiscuity refers to the ability of an enzyme to catalyze reactions other than its primary function.
- Enzymes are highly specific in their substrate binding, and they typically catalyze one or a few reactions with a high degree of selectivity.
- However, many enzymes have been found to exhibit promiscuous behavior, meaning they can also catalyze additional reactions with other substrates.
- This promiscuity can have important implications in biotechnology, as these enzymes can be repurposed for new applications beyond their original function.
-Source: The Hindu, PIB
