Resumen

SERRAT-DIAZ, Manuel; VALVERDE-NUNEZ, Tamara  y  DOMINGUEZ-FRANDIN, Zuleyka. Covalent Immobilization of a Yeast Endopolygalacturonase in Calcium Alginate. Rev Cub Quim [online]. 2014, vol.26, n.1, pp. 26-31. ISSN 2224-5421.

In this work, the covalent immobilization of a yeast endopolygalacturonase (endo-PG) in calcium alginate was examined. The carrier was activated by two different ways: glutaraldehyde addition (GA) and periodate oxidation (PO), respectively. During GA activation 5,8 mol of carbonyl groups/ mol of uronic acid residue were incorporated on the support whereas in the PO reaction only 0,13 % of vicinal glycols were oxidized. Covalent union yield and gel stability diminished when enzyme/support ratio was increased, corresponding the best results to the GA-activated alginate. The lost of enzymatic activity during immobilization was > 90 %, which is characteristic of covalent union. In all variants a high immobilized enzymatic activity was reached, around 200 U/g. It was concluded that the alginate activation, either with GA or PO, are feasible alternatives for the covalent immobilization of endo-PG on this support.

Palabras clave : endopolygalacturonase; alginate; enzyme immobilization; periodate; glutaraldehyde.

        · resumen en Español     · texto en Inglés     · Inglés ( pdf )