Abstract: A fructose-1,6-bisphosphate aldolase with obtained from Staphylococcus carnosus is disclosed. The aldolase has considerably improved stability as compared to aldolase from rabbit muscle, having an inactivation rate of 0.77%/d at 25.degree. C. as compared with 59.3%/d for rabbit muscle aldolase. The aldolase is obtained by culturing Staphylococcus carnosus cells, mechanically disrupting the cell mass, and then working up the product by fractional ammonium sulfate precipitation, pH fractionation and ion exchange chromatography to provide F-1,6-BP aldolase with a specific activity of 25 U/mg in 21% yield. Particularly high yields are obtained by the aqueous 2-phase extraction and obtaining the enzyme from the upper phase by anion exchange chromatography. The aldolase is suitable for synthesis of carbohydrates and derivatives thereof by enzymatic reaction of aldehydes with DHAP.