Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditions

• Published in: Catalysis Today
• Main Authors: Arana-Peña, Sara, Rios, Nathalia S., Carballares, Diego, Gonçalves, Luciana R. B., Fernández-Lafuente, Roberto
• Other Authors: Agencia Estatal de Investigación (España), Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil), Ministerio de Ciencia e Innovación (España)
• Format: Article in Journal/Newspaper
• Language: English
• Published: Elsevier B.V. 2020
• Subjects: Interfacial activation; Lipase immobilization; Lipase modulation; Lipase specificity; Lipase stability; Biocatalysts; Candida; Enzyme activity; Isomers; Yeast; Candida antarctica; Different substrates; Hydrophobic supports; Immobilization conditions; Immobilization method; Rhizomucor miehei; Strong interaction; Enzyme immobilization; Rugosa; Antarc*; Antarctica
• Online Access: http://hdl.handle.net/10261/373216; https://doi.org/10.1016/j.cattod.2020.03.059; https://www.scopus.com/inward/record.uri?eid=2-s2.0-85083529115&doi=10.1016%2fj.cattod.2020.03.059&partnerID=40&md5=47dd1bfa1a69aa5470bfa69e9af2615a

Lipases A and B from Candida antarctica (CALA, CALB), and those from Candida rugosa (CRL) and Rhizomucor miehei (RML) have been immobilized on octyl agarose beads under 16 different conditions. The activities of the biocatalysts versus different substrates were analyzed, as well as their thermal sta...