Lactose hydrolysis using β-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 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 maxi...

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Bibliographic Details
Published in:Preparative biochemistry & biotechnology 2021-08, Vol.51 (7), p.714-722
Main Authors: Carvalho, Catherine Teixeira de, Lima, Wildson Bernardino de Brito, de Medeiros, Fábio Gonçalves Macêdo, Dantas, Julia Maria de Medeiros, de Araújo Padilha, Carlos Eduardo, dos Santos, Everaldo Silvino, de Macêdo, Gorete Ribeiro, de Sousa Júnior, Francisco Canindé
Format: Article
Language:English
Subjects:
Alginic acid
Cheese whey
enzyme immobilization
Evaluation
Galactosidase
Gastrointestinal system
Gastrointestinal tract
Hydrolysis
Immobilization
Industrial applications
Kluyveromyces lactis
lactase
Lactose
lactose hydrolysis
pH effects
Sodium
Sodium alginate
Stability
Systems analysis
Whey
β-Galactosidase
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Summary: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.
ISSN:1082-6068
1532-2297
DOI:10.1080/10826068.2020.1853157