Abstract We will present our group results in the recombinant production of two enzymes (fructosyltransferase and invertase) that convert sucrose into value-added products and one enzyme (dextranase) used as aid to sugar production and refining. Constructed plasmids carrying several in-tandem copies of the transgene fused to a secretory signal peptide and under the transcriptional control of the constitutive glyceraldehyde 3-phosphate dehydrogenase (GAP) promoter were integrated in the Pichia pastoris genome. After fed-batch fermentations, each recombinant enzyme was recovered with purity above 85% from culture supernatants and characterized in terms of yield, posttranslational modifications, biochemical properties and catalytic performance. Fructosyltransferase converted sucrose to short-chain fructooligosaccharides (scFOS), particularly the most relevant prebiotic 1-kestose. Invertase completely hydrolyzed sucrose at elevated temperatures (60-70°C). The endo-type dextranase degraded microbial dextran and did not react on sucrose. For commercial purposes, each enzyme was recovered from the yeast culture supernatant and freeze-dried to a stable soluble powder. The recombinant P. pastoris strains developed in this study are cost-effective sources for the scaled production of three enzymes with application in the sugar and/or food industry.