U.S. flag

An official website of the United States government

Dot gov

Official websites use .gov
A .gov website belongs to an official government organization in the United States.


Secure .gov websites use HTTPS
A lock ( ) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.


Main content area

In situ immobilization of Candida antarctica B lipase in polyurethane foam support

Nadia Ligianara D. Nyari, Ilizandra A. Fernandes, Cindy E. Bustamante-Vargas, Clarisse Steffens, Débora de Oliveira, Jamile Zeni, Elisandra Rigo, Rogério M. Dallago
Journal of molecular catalysis 2016 v.124 pp. 52-61
Pseudozyma antarctica, carboxylic ester hydrolases, catalysts, catalytic activity, enzyme activity, enzyme stability, foams, food industry, oleic acid, polyols, polyurethanes, propionates, refrigeration, temperature
Candida antarctica B (CALB) lipase was immobilized using polyurethane (PU) foam as support by confinement method. This can be a promising technique due to the low cost of the support, simple procedure of immobilization and the possibility of using the derivative as catalyst for the food industry reactions. CALB immobilization on PU was performed using 6mL polyol and 4mL isocyanate (60–40%, v/v), with 1mL of enzymatic solution (0.8g enzyme in 5mL distilled water). The immobilization process resulted in a 535% increase in activity for the enzymatic derivative. The enzyme was stable for 360 days at room (10–25°C) and low (2–8°C) temperatures, for 300 days at 40 and 60°C and for 150 days at 80°C in wet ambient conditions. The synthesis of geranyl propionate and ethyl oleate catalyzed by the immobilized derivative presented conversions of around 97 and 83%, respectively. The immobilized CALB in PU was reused consecutively different behavior occurred which stored in dry ambient conditions at different temperatures (room: 10–25°C, refrigeration: 2–8°C and 40°C) resisted 30 cycles, for both forms of storage, keeping more than 87, 95 and 83% of its activity, respectively.