Lactose hydrolysis using ß-galactosidase from Kluyveromyces lactis immobilized with sodium alginate for potential industrial applications.

The present study aimed to evaluate the lactose hydrolysis conditions from "coalho" cheese whey using ß-galactosidase (ß-gal) produced by Kluyveromyces lactis immobilized with sodium alginate. Three sodium alginate-based immobilization systems were evaluated (0.5, 0.7, and 1% w/v) for maximizing the immobilization yield (Y), efficiency (EM), and recovered activity (ar). The lactose hydrolysis capacity of the immobilized form of ß-gal was determined, and simulated environments were used to assess the preservation of the immobilized enzyme in the gastrointestinal tract. The results showed that ß-gal immobilization with 1% (w/v) sodium alginate presented the best results (EM of 66%, Y of 41%, and ar of 65%). The immobilization system maintained the highest pH stability in the range between 5.0 and 7.0, with the highest relative activity obtained under pH 5 conditions. The temperature stability was also favored by immobilization at 50 °C for 30 min was obtained a relative activity of 180.0 ± 1.37%. In 6 h, the immobilized ß-gal was able to hydrolyze 46% of the initial lactose content. For the gastrointestinal simulations, around 40% of the activity was preserved after 2 h. Overall, the results described here are promising for the industrial applications of ß-galactosidase from K. lactis.

Potential of "coalho" cheese whey as lactose source for ß-galactosidase and ethanol co-production by Kluyveromyces spp. yeasts.

The present study evaluated the co-production of ß-galactosidase and ethanol by Kluyveromyces marxianus ATCC 36907 and Kluyveromyces lactis NRRL Y-8279 using as carbon source the lactose found on "coalho" cheese whey. Cheese whey was subjected to partial deproteinization, and physicochemical parameters were assessed. Cultivations were carried out in an shaker to evaluate two carbon/nitrogen (C:N) ratios. The best C:N ratio (1.5:1) was carried to 1.5-L bioreactor cultivation in order to increase co-production yields. The stability of ß-galactosidase was assessed against different temperatures and pH, and in the presence of metal ions. Concerning the co-production of ß-galactosidase and ethanol, K. lactis proved to be more efficient in both the C:N ratios, reaching 21.09 U·mL-1 of activity and 7.10 g·L-1 of ethanol in 16 h. This study describes the development of a viable and value-adding biotechnological process using a regional cheese by-product from Northeast Brazil for co-production of biomolecules of industrial interest.

Efficient stabilisation of curcumin microencapsulated into yeast cells via osmoporation.

This study proposes the investigation of curcumin encapsulation into Saccharomyces cerevisiae cells through osmoporation as an efficient way of increasing curcumin stability. The influence of three process parameters (cell, ethanol and curcumin concentrations) on the encapsulation process was evaluated, and the obtained biocapsules were characterised for physical and photochemical stabilisation. Results showed that encapsulation efficiency was favoured by the increase of cells/curcumin ratio and ethanol concentration up to 60%. Differential scanning calorimetry (DSC) curves revealed that yeast encapsulation delayed the curcumin melting point up to 207 °C. Encapsulated curcumin retained over 80% of antioxidant activity after thermal treatment (150 °C) and over 70% after a 50-day exposure to artificial light. Photochemical stability of yeast-encapsulated curcumin was increased by 5.7-fold, and half-life time reached 181 days under illumination conditions. Overall, osmoporation-produced yeast biocapsules confirmed the versatility of osmoporation as an encapsulation technique and successfully improved curcumin stability.