•Recombinant His-tagged thiazole kinase isolated, purified from genomic DNA of Plasmodium falciparum.•Monomeric enzyme with mass 34kDa, specific activity 295nmolmg−1 temperature and pH optima of 37°C and 7.5.•Km (65μM) and Vmax (36.8μmolml−1min−1) purified by FPLC on Sephacryl S100HR.•Non-competitive inhibition by Ag (79%; Ki=6.45μM).•Nanoparticles interact through Met1, Cys206 on surface of enzyme. Malaria, a mosquito-borne infectious disease, is caused by the Plasmodium genus, and remains one of the greatest health challenges worldwide. The malarial parasite possess a biosynthetic pathway for the B-group vitamin incorporating the thiamine metabolizing enzymes; humans on the other hand cannot synthesize the vitamin and require it from within their diet. The vitamin B1 biosynthetic enzyme 5-(2-hydroxyethyl)-4-methylthioazolekinase EC. 2.7.1.50 from Plasmodium (PfThzK) is particularly attractive as a biomedical target since any inhibition of this enzyme may lead to an effective treatment for malaria. In the present study, PfThzK was recombinantly produced as a 6× His fusion protein in Escherichia coli BL21(DE3) and purified using nickel affinity and size exclusion chromatography. The enzyme was monomeric with a molecular mass of 34kDa, a specific activity of 295.04nmolmin−1mg−1 and showed an optimum temperature and pH of 37°C and 7.5, respectively. The purified PfThzK was non-competitively inhibited (79%) by silver nanoparticles (2–6nm); Ki=6.45μM. A mechanism is suggested for the interaction of the silver nanoparticle with PfThzK through two sulphur bearing amino acids (Met1, Cys206) on the surface of each subunit of the enzyme.