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    Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions

    , Article Process Biochemistry ; Volume 95 , August , 2020 , Pages 288-296 Kornecki, J. F ; Carballares, D ; Morellon Sterling, R ; Siar, E. H ; Kashefi, S ; Chafiaa, M ; Arana Peña, S ; Rios, N. S ; Gonçalves, L. R. B ; Fernandez Lafuente, R ; Sharif University of Technology
    Elsevier Ltd  2020
    Abstract
    A destabilizing effect at pH 7 of sodium phosphate on several lipases immobilized via interfacial activation is shown in this work. This paper investigates if this destabilizing effect is extended to other inactivation conditions, immobilization protocols or even other immobilized enzymes (ficin, trypsin, β-galactosidase, β-glucosidase, laccase, glucose oxidase and catalase). As lipases, those from Candida antarctica (A and B), Candida rugosa and Rhizomucor miehei have been used. Results confirm the very negative effect of 100 mM sodium phosphate at pH 7.0 for the stability of all studied lipases immobilized on octyl agarose, while using glutaraldehyde-support the effect is smaller (still...