Tuning almond lipase features by the buffer used during immobilization: The apparent biocatalysts stability depends on the immobilization and inactivation buffers and the substrate utilized-Reference-Cited by-同舟云学术

Tuning almond lipase features by the buffer used during immobilization: The apparent biocatalysts stability depends on the immobilization and inactivation buffers and the substrate utilized

Published:2024-08 Issue: Volume:391 Page:72-80
ISSN:0168-1656
Container-title:Journal of Biotechnology
language:en
Short-container-title:Journal of Biotechnology

Author:

Cherni Oumaima,Carballares Diego,Siar El Hocine,Abellanas-Perez Pedro,de Andrades Diandra,de Moraes Polizeli Maria de Lourdes Teixeira,Rocha-Martin Javier,Bahri Sellema,Fernandez-Lafuente Roberto

Funder

Agencia Estatal de Investigación

FAPESP

Ministerio de Ciencia e Innovación

Enseignement Supérieur et de la Recherche Scientifique

Universidad de Alicante

Publisher

Elsevier BV

Reference92 articles.

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2. Glutaraldehyde modification of lipases immobilized on octyl agarose beads: roles of the support enzyme loading and chemical amination of the enzyme on the final enzyme features;Abellanas-Perez;Int J. Biol. Macromol.,2023

3. The nature of the buffer alters the effects of the chemical modification on the stability of immobilized lipases;Abellanas-Perez;Process Biochem.,2023

4. Efficient production of bioactive structured lipids by fast acidolysis catalyzed by Yarrowia lipolytica lipase, free and immobilized in chitosan-alginate beads, in solvent-free medium;Akil;Int J. Biol. Macromol.,2020

5. Effects of enzyme loading and immobilization conditions on the catalytic features of lipase from Pseudomonas fluorescens immobilized on octyl-agarose beads;Arana-Peña;Front Bioeng. Biotechnol.,2020