Fátima Costa

In vitro synthesis of oligosaccharides by acceptor reaction of dextransucrase from Leuconostoc mesenteroides

Glucose was used as acceptor to obtain small chain oligossaccharides from sucrose using dextransucrase from Leuconostoc mesenteroides NRRL B-512F. Better conditions for the synthesis of the oligosaccharides were obtained using experimental design and response surface methodology. Yield of oligosaccharides was increased from 5% to 45% following an increase in both sucrose and glucose/sucrose concentrations, from 58 g/l to 142 g/l and from 0.02 to 0.18, respectively. Molecular weight increased from 2800 to 4500 daltons with a temperature shifting from 10°C to 30°C.

Response surface methodology applied to the enzymatic synthesis of galacto-oligosaccharides from cheese whey

In this study, a strategy was proposed for making galacto-oligossaccharides (GOS), a high valueadded product, from a byproduct of the dairy industry, cheese whey, using a commercial β-galactosidase from Kluyveromyces lactis (Lactozym® 3000L). The effects of the substrate concentration, temperature, and enzyme dosage were statistically studied and their optimum combinations were determined using response surface methodology. The increase in lactose concentration, temperature, and enzyme concentration favored a transgalactosylation reaction. The maximum values for GOS concentration (119.8 mg/mL) and yield (29.9%) in a 4 h process were obtained in the reaction system, composed of 400 mg/mL of lactose and 10 U/mL of enzyme at 40°C. Under these conditions, the lactose conversion was 68.7%. The maximum value for lactose conversion (87.8%) was observed at the same temperature and enzyme concentration, although the lactose level was 20%.

Comparative studies of the stability of free and immobilized inulinase from Kluyveromyces marxianus NRRL Y-7571 in aqueous-organic solutions

Abstract - 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. Keywords : Organic solvent; Inulinase; Stability; Kinetic parameters.

Optimization of dextran syntesis and acidic hydrolisis by surface response analysis

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.