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Chitooligosaccharides (COS) have a great potential to be used by pharmaceutical industry due to their many biological activities. The use of enzymes to produce them is very advantageous, however it still faces many challenges, such as discovering new strains capable to produce enzymes that are able to generate bioactive oligosaccharides. In the present study a purification protein protocol was performed to purify chitosanases produced by Bacillus toyonensis CCT 7899 for further chitosan hydrolysis. The produced chitooligosaccharides were characterized by mass spectroscopy (MS) and their antiedematogenic effect was investigated through carrageenan-induced paw edema model. The animals were treated previously to inflammation by intragastric route with COS at 30, 300 and 600 mg/kg. The purification protocol showed a good performance for the chitosanases purification using 0.20 M NaCl solution to elute it, with a 9.54-fold purification factor. The treatment with COS promoted a decrease of paw edema at all evaluated times and the AUC0–4h, proving that COS produced showed activity in acute inflammation like commercial anti-inflammatory Dexamethasone (corticosteroid). Therefore, the strategy used to purification was successfully applied and it was possible to generate bioactive oligosaccharides with potential pharmacological use. [ABSTRACT FROM AUTHOR]

The present study aimed to evaluate the lactose hydrolysis conditions from "coalho" cheese whey using β-galactosidase (β-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 β-gal was determined, and simulated environments were used to assess the preservation of the immobilized enzyme in the gastrointestinal tract. The results showed that β-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 β-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 β-galactosidase from K. lactis. [ABSTRACT FROM AUTHOR]