Modification of phospholipids with lipases and phospholipases

Annikka Mustranta, Pirkko Forssell, Anna-Marja Aura, Tapani Suortti, Kaisa Poutanen

    Research output: Contribution to journalArticleScientificpeer-review

    20 Citations (Scopus)


    Different commercial lipases and phosphoiipases were studied in the hydrolysis and transesterification of synthetic phosphatidylcholine and soybean lecithin. Wide variations in the lipase and phospholipase activities and in the protein contents of the preparations were observed. The substrate specificity varied between different enzymes. A high degree of hydrolysis of synthetic and soybean phospholipids was achieved with both types of enzymes.
    Enzymes immobilized on Celite were used in the transesterification of dimyristoyl phosphatidylcholine and oleic acid. The conversions were carried out both without solvent and in the presence of toluene. The amount of modified phosphatidylcholine was measured using HPLC. The highest amount of modified phosphatidylcholine was obtained in solvent-free transesterification. The best results were obtained with Aspergillus niyer lipase.
    Original languageEnglish
    Pages (from-to)181 - 194
    JournalBiocatalysis and Biotransformation
    Issue number1-4
    Publication statusPublished - 1994
    MoE publication typeA1 Journal article-refereed


    • modification
    • phospholipids
    • phospholilipases
    • lipases


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