Research database

Nowadays, Research has made significant progresses in the cancer diagnoses and treatment. Recently, it has been proved that most cancer cells are subjected to the well-known Warburg effect. In fact, even in aerobic conditions, cancer cells consume glucose to produce energy by high-rate glycolysis followed by lactic acid fermentation, during this step pyruvate is converted to lactate. The major responsible of the production of lactate is the enzyme lactate dehydrogenase (LDH) and both the aberrant expression and activation of LDH are closely correlated to most types of tumours. Because this mutated metabolic route can be considered a characteristic feature of cancerogenic cells, LDH can be looked upon as a target to test the efficiency of antitumoral drugs as inhibitors of the enzyme. Indeed, several studies demonstrate that the repression of LDH has positive effects in terms of reduction of tumour growth and proliferation. At present, the methods used to test the efficiency of new LDH inhibitors include: LDH inhibition assays and cell-based biological evaluation assays. However, these are very expensive and time-consuming techniques. Usually, the enzyme inhibition assay employs enzymes dissolved in water solution, this implies the needing of new enzyme for each assay. On the other hand, the enzyme immobilization on solid supports allows to reuse the biocatalyst with a consequent reduction of cost and time because enzymes could be employed in different type of industrial processes.