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Factors influencing the activity and thermostability of immobilized porcine pancreatic lipase
Author(s) -
Kéry Vladimír,
Haplová Jana,
Tihlárik Karol,
Schmidt Štefan
Publication year - 1990
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.280480209
Subject(s) - lipase , thermostability , chemistry , covalent bond , adsorption , immobilized enzyme , cellulose , hydrophobic effect , substrate (aquarium) , olive oil , triacylglycerol lipase , chromatography , organic chemistry , enzyme , food science , biology , ecology
Lipase from porcine pancreas was immobilized on cellulose beads having various degrees of hydrophobicity, by covalent linking and by hydrophobic adsorption. Lipolytic activity was measured in heterogeneous organicaqueous systems of various hydrophobicities using olive oil as a substrate. The main factors influencing lipase activity were hydrophobicity of the reaction mixture and of the carrier. Carriers with increased hydrophobicity enhanced lipase activity more than less hydrophobic ones. Lipase immobilized covalently on cellulose beads was less active than that adsorbed onto tritylcellulose but was considerably more thermostable.