Abstract

L-tryptophan is the only protein amino acid (AA) with an indole ring; through biotransformation in live creatures, it either helps to retain this chemical group in cells and tissues or breaks it down by producing a variety of bioactive chemicals in both scenarios. Studies on the biology of Trp emphasise the pleiotropic impact of its tiny derivatives on homeostasis mechanisms. In addition to protein turnover, the production of the neurotransmitter and hormone serotonin (5-HT), the pineal gland hormone melatonin (MLT), and the trace amine tryptamine is covered by the pathways of Trp indole derivatives in humans. Instead, the "kynurenine shunt," which results in cell-response adapters such L-kynurenine, kynurenic, and quinolinic acids, or the coenzyme nicotinamide adenine dinucleotide (NAD+), is defined by the breakdown of the Trp indole ring. One of the most promising approaches to cleaning up polluted surroundings with powerful, very effective bacteria is bioremediation. The very poisonous heterocyclic molecule nicotine and other tobacco alkaloids can be broken down by microbes using particular enzymes and metabolic pathways. These nicotinophilic bacteria use nicotine as their only supply of carbon, nitrogen, and energy following the metabolic conversion. The demethylation pathway in fungi, the pyridine pathway in Gram-positive bacteria, the pyrrolidine pathway, and variants of the pyridine and pyrrolidine pathways in Gram-negative bacteria are just a few of the identified nicotine breakdown pathways. In this review, we covered the biotechnological uses of nicotine intermediate metabolites as well as the enzymes and microorganisms that break down nicotine.