Ligninolytic fungal laccases and their biotechnological applications.
Lignin is amorphous in nature, lacks stereoregularity, and is not susceptible to hydrolytic attack. Despite its resistant nature, it is however degraded by various microorganisms, particularly, white-rot fungi. Such fungi are capable of extracellular production of lignin peroxidase, manganese peroxidase, and laccase, the three major enzymes associated with ligninolysis. Though all white-rot fungi do not produce all the three enzymes, laccase occupies an important place in ligninolysis. Laccase belongs to a diverse group of enzymes called oxidoreductases and is also known as benzenediol: oxygen oxidoreductase. They have low substrate specificity. The copper-containing enzyme laccase has been detected in a variety of organisms such as bacteria, fungi, plants, and insects. Mostly, these are extracellular proteins, although intracellular laccases have also been detected in some fungi and insects. Fungal laccases are believed to play a variety of roles, such as, morphogenesis, pathogenesis, and lignin degradation. As an oxidase, laccase is used in many agricultural, industrial, and medicinal applications. Current investigations are focused on laccase-based biooxidation, biotransformation, biosensor, and enzymatic synthesis of organic compounds. By enhancing laccase production using different physiochemical parameters, better understanding of the mechanism for the reactions of interest, and optimizing the catalytic activity of laccase, it can be used in a better way in diverse fields of biotechnology.
Singh Arora
Daljit
D
Department of Microbiology, Microbial Technology Laboratory, Guru Nanak Dev University, Amritsar, 143005, Punjab, India. daljit_02@yahoo.co.in
Kumar Sharma
Rakesh
R
D055162:Biocatalysis; D001709:Biotechnology; D057075:Enzyme Assays; D005658:Fungi / Q000201:enzymology*; D042845:Laccase / Q000378:metabolism*; D008031:Lignin / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D008031:Lignin; D042845:Laccase