Maggot kinase: A novel and cost-effective fibrinolytic enzyme from maggots

Abstract

Maggot kinase, a novel fibrinolytic enzyme source, has been isolated from fly maggots and comprehensively characterized. Using CM-52 ion exchange chromatography and affinity chromatography, we obtained a highly purified and active form of the enzyme. In particular, the fibrinolytic activity of maggot kinase, evaluated using the fibrin plate method, was found to be 8.98 ± 0.08 × 105 U/mg, demonstrating significant efficacy. Further structural analysis using mass spectrometry revealed that maggot kinase consists of a primary sequence of 226 amino acid residues with a molecular weight of 22.91 kDa. In vitro thrombolytic assays demonstrated the enzyme's remarkable ability to degrade the essential fibrinogen subunits (α, β, and γ), thereby facilitating clot lysis. Notably, our studies in a mouse model underscored the significant in vivo thrombolytic activity of maggot kinase, demonstrating its potential to inhibit thrombosis. The finding is particularly significant considering the widespread use of fly maggots in agriculture and animal husbandry due to their rapid growth cycle and minimal nutritional requirements. Our research highlights the untapped potential of fly maggots as a source for maggot kinase development for antithrombotic drug and functional food applications.