Microcystins are secondary metabolites produced by some cyanobacteria, a class of cyclic heptapeptide toxins that are stable in the environment. Microcystins can create a variety of adverse health effects in humans, animals, and plants through contaminated water. Effective methods to degrade them are required. Microorganisms are considered to be a promising method to degrade microcystins due to their high efficiency, low cost, and environmental friendliness. This review focuses on perspectives on the frontiers of microcystin biodegradation. It has been reported that bacteria and fungi play an important contribution to degradation. Analysis of the biodegradation mechanism and pathway is an important part of the research. Microcystin biodegradation has been extensively studied in the existing research. This review provides an overview of (1) pollution assessment strategies and hazards of microcystins in water bodies and (2) the important contributions of various bacteria and fungi in the biodegradation of microcystins and their degradation mechanisms, including mlr gene-induced (gene cluster expressing microcystinase) degradation. The application of biodegradable technology still needs development. Further, a robust regulatory oversight is required to monitor and minimize MC contamination. This review aims to provide more references regarding the detection and removal of microcystins in aqueous environments and to promote the application of biodegradation techniques for the purification of microcystin-contaminated water.

Hepatotoxic microcystins (MCs) are produced and released by the harmful bloom-forming cyanobacteria, which severely threaten drinking water safety and human health due to their high toxicity, widespread distribution, and structural stability. The linearized microcystinase (MlrB) further hydrolyses the poisonous linearized MCs produced by the microcystinase-catalysed MCs to form tetrapeptides. Here, the purification and activity of MlrB were investigated. The results showed that the linearized products generated by 12.5 mg/L MC-LR and MC-RR were removed by purified recombinant MlrB at a protein concentration of 1 mg/L within 30 min. The high catalytic activity of MlrB can be obtained via heterologous expression and affinity purification, which lays the foundation for further studies on the properties and mechanism of MCs biodegradation enzymes.

Cyanobacterial hepatotoxins, including microcystins (MCs) and nodularins (NODs), are widely produced, distributed and extremely hazardous to human beings and the environment. However, the catalytic mechanism of microcystinase for biodegrading cyanobacterial hepatotoxins is not completely understood yet. The first microcystinase (MlrA) catalyzes the ring opening of cyclic hepatotoxins, while being further hydrolyzed by the third microcystinase (MlrC). Based on the homology modeling, we postulated that MlrC of Sphingopyxis sp. USTB-05 was a Zn²⁺-dependent metalloprotease including five active sites: Glu56, His150, Asp184, His186 and His208. Here, the active recombinant MlrC and five site-directed mutants were successfully obtained with heterologous expression and then purified for investigating the activity. The results indicated that the purified recombinant MlrC had high activity to catalyze linearized hepatotoxins. Combined with the biodegradation of linearized NOD by MlrC and its mutants, a complete enzymatic mechanism for linearized hepatotoxin biodegradation by MlrC was revealed.