Stability of hydrophobic lipase derivatives immobilized on organic polymer beads

Lipase from Candida rugosa was immobilized by attaching various hydrophobic groups to the enzyme molecule and adsorbing these hydrophobic lipase derivatives on several organic polymer beads. The immobilized enzymes were more thermostable in organic solvents compared to the native and modified lipase...

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Bibliographic Details
Published in:Applied biochemistry and biotechnology 1994-09, Vol.48 (3), p.173-183
Main Authors: Basri, M. (Universiti Pertanian Malaysia, Serdang, Malaysia.), Ampon, K, Yunus, W.M.Z.W, Razak, C.N.A, Salleh, A.B
Format: Article
Language:English
Subjects:
Biological and medical sciences
Biotechnology
CANDIDA
Candida rugosa
Fundamental and applied biological sciences. Psychology
HIDROFOBICIDAD
HYDROPHOBICITE
IMMOBILISATION
Immobilization of enzymes and other molecules
Immobilization techniques
INMOVILIZACION
Methods. Procedures. Technologies
TRIACILGLICEROL LIPASA
TRIACYLGLYCEROL LIPASE
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Summary:Lipase from Candida rugosa was immobilized by attaching various hydrophobic groups to the enzyme molecule and adsorbing these hydrophobic lipase derivatives on several organic polymer beads. The immobilized enzymes were more thermostable in organic solvents compared to the native and modified lipases. Thermostability was highest with XAD2 beads, followed by XAD7 and RCOOH. Initially modifying the enzyme with hydrophobic modifiers did not have any effect on the enzyme thermostability. The best conditions for storing these enzyme preparations were at very low temperature in the lyophilized form and in a solution containing the reaction substrate. Interestingly, PEG-lipase immobilized on XAD7 beads showed increased operational stability when used in a stirred-tank reactor. The operational stability was further increased by a mild glutaraldehyde treatment of the enzyme preparation
ISSN:0273-2289
1559-0291
DOI:10.1007/BF02788740