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Behaviour of a recombinant cabbage ( Brassica oleracea ) phospholipase D immobilized on CNBr‐activated and antibody supports
Author(s) -
Younus Hina,
Rajcani Julius,
UlbrichHofmann Renate,
Saleemuddin Mohammed
Publication year - 2004
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1042/ba20030171
Subject(s) - thermostability , sepharose , chemistry , pld2 , enzyme , affinity chromatography , biochemistry , brassica oleracea , recombinant dna , immobilized enzyme , chromatography , biology , phosphatidylcholine , botany , phospholipid , membrane , gene
Recombinant cabbage ( Brassica oleracea ) PLD2 (phospholipase D2) immobilized covalently on CNBr‐activated Sepharose expressed low activity (≈10%), while that immobilized by binding on to anti‐PLD2 IgG–Sepharose was more active (≈38%). Coupling of PLD2 to CNBr‐activated Sepharose resulted in significant improvement in storage stability without affecting its thermostability, as compared with the soluble enzyme. Binding of PLD2 to the antibody support, however, rendered the enzyme remarkably labile to high temperatures and storage.