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Comparative study of the hydrolysis of different oils by lipase‐immobilized membranes
Author(s) -
Gupta S.,
Ingole P.,
Singh K.,
Bhattacharya A.
Publication year - 2011
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.35400
Subject(s) - castor oil , lipase , hydrolysis , chemistry , membrane , ricinoleic acid , glutaraldehyde , polysulfone , chromatography , nuclear chemistry , organic chemistry , biochemistry , enzyme
Lipase immobilization on asymmetric polysulfone (PS) membranes was done by physical adsorption and covalent coupling techniques. The glutaraldehyde (Glu) crosslink showed maximum immobilization (1.53 mg/cm 2 ) on the hydrazine (Hz)‐modified membrane surface. Lipase immobilization on the membrane was proved by different analytical tools (viz., X‐ray diffraction, scanning electron microscopy). The hydrolase‐immobilized enzyme marked its hydrolyzing ability to different oils (olive, palm, and castor oils). The hydrolysis yield (U/mg) for the different immobilized membranes was in the following order: Olive oil > Palm oil > Castor oil. The PS–Hz–Glu–lipase membrane showed maximum hydrolyzing ability for olive oil (62.37 U/mg) and minimum hydrolyzing ability for castor oil (38.11 U/mg). The low aptitude for the hydrolysis of castor oil was explained by the presence of ricinoleic acid in the main composition. The lowest affinity toward castor oil (Michaelis–Menten constant = 18.86 m M ) also featured the same. The order of maximum reaction rate for the same membrane was as follows: Olive oil (64.5) > Palm oil (62.5) > Castor oil (41.6). The immobilized lipase on PS–Hz–Glu suffered only a 12.5% deterioration for olive oil after five cycles. © 2011 Wiley Periodicals, Inc. J Appl Polym Sci, 2012