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Porcine pancreatic lipase immobilized on polysiloxane–polyvinyl alcohol hybrid matrix: catalytic properties and feasibility to mediate synthesis of surfactants and biodiesel
Author(s) -
Paula Ariela V,
Urioste Daniele,
Santos Julio C,
de Castro Heizir F
Publication year - 2007
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.1669
Subject(s) - lipase , lauric acid , chemistry , biodiesel , oleic acid , organic chemistry , polyvinyl alcohol , catalysis , fatty acid , glycerol , ethanol , alcohol , thermal stability , biodiesel production , transesterification , biochemistry , enzyme
Abstract Polysiloxane–polyvinyl alcohol hybrid matrix was prepared by a sol–gel technique and its capacity to bind porcine pancreatic lipase investigated. The loading of 250 units g −1 support was shown to be effective, resulting in an immobilized lipase with high catalytic activity. Both free and immobilized lipases were characterized by determining the activity profile as a function of pH, temperature, substrate concentration and thermal stability. Application of the immobilized lipase in non‐conventional biocatalysis for the synthesis of surfactants and biodiesel was also analyzed. Production of sugar fatty acid esters was found to be dependent on the carbohydrate and the highest molar conversion (50% in 3–4 h of reaction) was achieved for substrates containing fructose and lauric or oleic acids. Biodiesel synthesis from babassu oil and ethanol, propanol or butanol was feasible and regardless of the kind of alcohols, results revealed that the immobilized PPL could efficiently convert triglycerides to fatty acid alkyl esters attaining yields varying from 75 to 95%. Copyright © 2007 Society of Chemical Industry