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A Comprehensive Study on the Activity and Deactivation of Immobilized Lecitase Ultra in Esterifications of Food Waste Streams to Monoacylglycerols
Author(s) -
Gonçalves Karen M.,
Sutili Felipe K.,
Júnior Ivaldo I.,
Flores Marcella C.,
Soter de Mariz e Miranda Leandro,
Leal Ivana C. R.,
Cordeiro Yraima,
Luque Rafael,
de Souza Rodrigo Octavio M. Alves
Publication year - 2013
Publication title -
chemsuschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.412
H-Index - 157
eISSN - 1864-564X
pISSN - 1864-5631
DOI - 10.1002/cssc.201300026
Subject(s) - chemistry , food waste , glycerol , residue (chemistry) , biocatalysis , organic chemistry , flow chemistry , chemical engineering , chromatography , catalysis , waste management , reaction mechanism , engineering
Lecitase Ultra was immobilized on Amberlites XAD2 and XAD4, through physical entrapping under conventional stirring or ultrasound irradiation, and characterized by standard techniques. The resulting immobilized biocatalysts were utilized in the valorization of an acidic food‐derived residue from a palm oil refining process to produce monoacylglycerols from isopropylidene glycerol under batch and continuous flow conditions. Results indicated that the immobilized biocatalysts could moderately convert the food waste residue (max. conversion 50–60 %), exhibiting interesting stability under continuous flow conditions.