In the era of green revolution, awareness of the need to find sustainable alternatives to traditional industrial processes, chemicals and materials grows greater every day. Nearly every industrial process uses catalysts that are harmful to the environment, nondegradable and require very harsh reaction conditions. On the other hand, biocatalysts are mostly enzymes, molecules evolved in a physiological environment that are fully biodegradable and survive in mild reaction conditions where they show the greatest activity and efficiency. Biocatalysis follows almost every green chemistry principle and the potential that biocatalysts have regarding replacing traditional chemical processes, making them more environmentally friendly, grows exponentially with the development of innovations and technological advancements especially in areas of enzymatic and genetic engineering. MenD is the designation for the enzyme 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) synthase, which is important in the synthesis of menaquinone, has potential antibiotic properties in anti-tuberculosis medicines, catalyses reactions that give 1,4-functionalized products and is the only known enzyme that catalyses the addition of ThDP on β-carbon of a secondary substrate. Purification of protein sample containing MenD, mass concentration of γ=41,67 mg/mL, was performed in this work. The sample was purified by affinity chromatography on ÄKTAprime plus via HisTrap™ excel chromatography column. These chromatography columns enable the capture and purification of histidine labelled proteins by immobilized metal affinity chromatography. The success of the purification was determined using electrophoresis, which tested the presence of MenD in purified fractions.