An efficient enzymatic way catalyzed by an enzyme from D-Threonine Aldolase family was developed for D-serine production at industrial scale. This process was applied to the synthesis of two valuable ketoses, L-erythrulose and D-fructose, within cascade enzymatic concept involving both other enzymes. Indeed, D-serine was used as a substrate of D-amino acid oxidase for the in situ generation of the corresponding ketoacid, hydroxypyruvate, a key donor substrate of Transketolase. This enzyme catalyzed the irreversible transfer of the ketol group from hydroxypyruvate to an aldehyde acceptor to form a (3S)-ketose by stereoselective carbon-carbon bond formation. The compatibility of all enzymes and substrates allowed to develop a three step enzymatic process avoiding the purification of intermediates. This strategy was validated with two TK aldehyde substrates to finally obtain the corresponding (3S)-ketoses with a high control of the stereoselectivity and excellent aldehyde conversion rates.