Covalent Immobilization of a Yeast Endopolygalacturonase in Calcium Alginate

Authors

  • Dr. C. Manuel Serrat-Díaz Centro de Estudios de Biotecnología Industrial, Facultad de Ciencias Naturales, Universidad de Oriente, Santiago de Cuba
  • MSc. Tamara Valverde-Núñez Centro de Estudios de Biotecnología Industrial, Facultad de Ciencias Naturales, Universidad de Oriente, Santiago de Cuba
  • MSc. Zuleyka Domínguez-Frandín Centro de Estudios de Biotecnología Industrial, Facultad de Ciencias Naturales, Universidad de Oriente, Santiago de Cuba

Abstract

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.

Keywords: endopolygalacturonase, alginate, enzyme immobilization, periodate, glutaraldehyde.

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Published

2015-11-02

How to Cite

Serrat-Díaz, D. C. M., Valverde-Núñez, M. T., & Domínguez-Frandín, M. Z. (2015). Covalent Immobilization of a Yeast Endopolygalacturonase in Calcium Alginate. Revista Cubana De Química, 26(1), 26–31. Retrieved from https://cubanaquimica.uo.edu.cu/index.php/cq/article/view/306

Issue

Vol. 26 No. 1 (2014)

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Artículos

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