Galacto-oligosaccharides are non-digestible carbohydrates and are recognized as important prebiotics for than stimulation of the proliferation of lactic acid bacteria and bifidobacteria in the human intestine. GOS can be produced by a transgalactosylation reaction catalysed by ?-galactosidase enzyme, and microorganisms can be used as a source of ?-galactosidase. In this work, a process for producing GOS using permeabilized cells of Kluyveromyces marxianus CCT 7082 was proposed. The effects of the concentrations of lactose and enzyme, temperature and pH were studied using a fractional design followed by a central composite rotatable design. The optimum conditions for galacto-oligosaccharides production were found to be: lactose concentration 500 g/L, enzyme concentration 10 U/mL, 45°C and pH 7.0. Under optimized conditions, the GOS concentration, yield and productivity were 83 g/L, 16.5% and 27.6 g/L.h, respectively.

The influence of some variables in the in vitro synthesis of dextran by dextransucrase from Leusconostoc mesenteroides NRRL B512F, as well as in the acidic hydrolysis of the dextran produced, were studied in order to maximize the production of clinical dextran (dextran 70 and dextran 40). The experiments were conducted using a factorial design and surface response analysis

-Enzymes have been extensively used in organic solvents to catalyze a variety of reactions of biological and industrial significance. In this work, the characteristics of free and immobilized inulinase were investigated in buffered solutions of butyl acetate. The influences of the organic solvent content on the optimal temperature and pH, the stabilities to temperature and pH and the kinetic parameters were systematically evaluated. The results showed that the organic solvent content had no effect on the optimal pH, either in the free or immobilized inulinase. For the immobilized enzyme, the optimal temperatures ranged from 55°C to 60°C, depending on the content of butyl acetate. At higher butyl acetate content, the stability of the immobilized enzyme increased for both pH and temperature. The organic solvent showed the tendency to increase the values of the kinetic parameters K m and v max for both free and immobilized inulinase.

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