Tuning Almond Lipase Features by Using Different Immobilization Supports

Cherni, Oumaima and Carballares, Diego and Siar, El Hocine and Abellanas-Perez, Pedro and de Andrades, Diandra and Rocha-Martin, Javier and Bahri, Sellema and Fernandez-Lafuente, Roberto (2024) Tuning Almond Lipase Features by Using Different Immobilization Supports. Catalysts, 14 (2). p. 115. ISSN 2073-4344

[thumbnail of catalysts-14-00115.pdf] Text
catalysts-14-00115.pdf - Published Version

Download (389kB)


The lipase from Prunus dulcis almonds has been immobilized for the first time. For this purpose, two different supports, an octadecyl methacrylate particulate support, and aminated agarose (monoaminoethyl-N-aminoethyl) have been utilized. Both immobilized biocatalysts show improved enzyme stability, but great changes in enzyme specificity were detected. The enzyme immobilized via ion exchange maintained its activity intact versus p-nitrophenyl butyrate, while the enzyme immobilized on the hydrophobic support fully lost its activity versus this substrate, which was confirmed to be due to substrate adsorption on the support. However, this biocatalyst was much more active versus triacetin (more than 10-fold), R- or S- methyl mandelate at pH 7. At pH 9, a strong effect of using phosphate or bicarbonate as reaction buffers was detected. Using bicarbonate, the interfacially immobilized enzyme presented no activity versus R-isomer, but it was very active versus the S-isomer and triacetin. Using a phosphate buffer during the reaction, all compounds were recognized as substrates. The enzyme immobilized via ion exchange was significantly more active using phosphate; in fact, using bicarbonate, the enzyme was inactive versus both methyl mandelate isomers. This paper shows for the first time a great interaction between the effects of the immobilization protocol and buffer used during reaction on the enantiospecificity of lipases.

Item Type: Article
Subjects: Eurolib Press > Multidisciplinary
Depositing User: Managing Editor
Date Deposited: 01 Feb 2024 05:52
Last Modified: 01 Feb 2024 05:52
URI: http://info.submit4journal.com/id/eprint/3423

Actions (login required)

View Item
View Item