Process for preparing sphingolipids of the general formula I by reacting a first component, a lysosphingolipid of the general formula II with a second component, an acyl group donor of the acyl group R 1 CO, where R 1 represents a linear or branched alkyl chain having 2 to 55 carbon atoms that optionally contains one or more multiple bonds and/or aromatic or heteroaromatic rings, is optionally interrupted by oxygen atoms or ester or amide functionalities and is optionally substituted by at least one further group selected from alkyl, hydroxyl, keto or amine groups, R 2 represents H, phosphocholine, serine, ethanolamine or a sugar, preferably sugar or H, more preferably H, and X represents CH=CH, CH 2 -CH 2 or CH 2 -HCOH, preferably CH 2 -CH 2, characterized in that the first and second components, based on the overall reaction mixture, account for a total of at least 70% by weight, preferably 90% by weight, especially 95% by weight, and not more than 600 propyl laurate units of at least one carboxylic ester hydrolase from the E.C. 3.1.1 enzyme class per gram of first component are used in the entire reaction mixture, where one propyl laurate unit is defined as the amount of enzyme that synthesizes one μmol of propyl laurate per minute from 1-propanol and lauric acid, and characterized in that the carboxylic ester hydrolase is selected from the group comprising the lipase from Thermomyces lanuginosus with accession number 059952, lipases A and B with accession number P41365 from Candida antarctica and the lipase from Mucor miehei with accession number P19515, the lipase from Humicola sp. with accession number O59952, the lipase from Rhizomucor javanicus with accession number S32492, the lipase from Rhizopus oryzae with accession number P61872, the lipases from Candida rugosa with accession number P20261, P32946, P32947, P3294 and P32949, the lipase from Rhizopus niveus with accession number P61871, the lipase from Penicillium camemberti with accession number P25234, the lipases from Aspergillus niger with accession number ABG73613, ABG73614 and ABG37906, and the lipase from Penicillium cyclopium with accession number P61869, and their respective at least 60%, preferably at least 80%, more preferably at least 90%, especially preferably at least 95%, 98% or 99%, homologues at the amino acid level, where the accession numbers correspond to the NCBI ProteinBank database entries as at 01.01.2017. R 1 represents a linear or branched alkyl chain having 2 to 55 carbon atoms that optionally contains one or more multiple bonds and/or aromatic or heteroaromatic rings, is optionally interrupted by oxygen atoms or ester or amide functionalities and is optionally substituted by at least one further group selected from alkyl, hydroxyl, keto or amine groups, R 2 represents H, phosphocholine, serine, ethanolamine or a sugar, preferably sugar or H, more preferably H, and X represents CH=CH, CH 2 -CH 2 or CH 2 -HCOH, preferably CH 2 -CH 2, the first and second components, based on the overall reaction mixture, account for a total of at least 70% by weight, preferably 90% by weight, especially 95% by weight, and not more than 600 propyl laurate units of at least one carboxylic ester hydrolase from the E.C. 3.1.1 enzyme class per gram of first component are used in the entire reaction mixture, where one propyl laurate unit is defined as the amount of enzyme that synthesizes one μmol of propyl laurate per minute from 1-propanol and lauric acid, and characterized in that the carboxylic ester hydrolase is selected from the group comprising the lipase from Thermomyces lanuginosus with accession number 059952, lipases A and B with accession number P41365 from Candida antarctica and the lipase from Mucor miehei with accession number P19515, the lipase from Humicola sp. with accession number O59952, the lipase from Rhizomucor javanicus with accession number S32492, the lipase from Rhizopus oryzae with accession number P61872, the lipases from Candida rugosa with accession number P20261, P32946, P32947, P3294 and P32949, the lipase from Rhizopus niveus with accession number P61871, the lipase from Penicillium camemberti with accession number P25234, the lipases from Aspergillus niger with accession number ABG73613, ABG73614 and ABG37906, and the lipase from Penicillium cyclopium with accession number P61869, and their respective at least 60%, preferably at least 80%, more preferably at least 90%, especially preferably at least 95%, 98% or 99%, homologues at the amino acid level, where the accession numbers correspond to the NCBI ProteinBank database entries as at 01.01.2017.