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Updated: May 17, 2026
Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Immobilization of lipase from grey mullet
Alberta N A Aryee1, Benjamin K Simpson
1Department of Food Science and Agricultural Chemistry, Faculty of Agricultural and Environmental Sciences, McGill University, Macdonald Campus, 21,111 Lakeshore Rd., Ste. Anne de Bellevue, QC, Canada, H9X 3V9.
Abstract:
Grey mullet (Mugil cephalus) lipase was isolated using para-aminobenzamidine agarose and immobilized on octyl Sepharose CL-4B (o-Sep). Immobilized grey mullet lipase (GMLi) had a 10 °C higher optimum temperature compared to the free enzyme and showed remarkable thermal stability. GMLi was most active within the pH range of 8.0-9.5 with an optimum at 8.5. Immobilization also enhanced the storage stability and reusability of the enzyme with minimal changes in efficiency during repeated batches. GMLi showed variable stabilities in various organic solvents. A signal in the amide I absorption region of the FTIR spectrum of GMLi was attributed to the protein layer on o-Sep. The surface morphology of o-Sep was visualized on a Zeiss stereomicroscope as globular-shaped beads.
