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Lipase immobilization on ionic liquid‐modified magnetic nanoparticles: Ionic liquids controlled esters hydrolysis at oil–water interface
Author(s) -
Jiang Yangyang,
Guo Chen,
Gao Hongshuai,
Xia Hansong,
Mahmood Iram,
Liu Chunzhao,
Liu Huizhou
Publication year - 2012
Publication title -
aiche journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.958
H-Index - 167
eISSN - 1547-5905
pISSN - 0001-1541
DOI - 10.1002/aic.12644
Subject(s) - lipase , ionic liquid , hydrolysis , chemistry , covalent bond , immobilized enzyme , magnetic nanoparticles , aqueous two phase system , nanoparticle , ionic bonding , aqueous solution , chemical engineering , reagent , organic chemistry , catalysis , ion , enzyme , engineering
Abstract Ester hydrolysis at oil–water interface by lipase covalently immobilized on ionic liquid‐modified magnetic nanoparticles was investigated. Magnetic supports with a diameter of 10–15 nm were synthesized by covalent binding of ionic liquids (chain length C 4 and C 8 and anions Cl − , BF 4 − , and PF 6 − ) on the surface of Fe 3 O 4 nanoparticles. Lipase was covalently immobilized on Fe 3 O 4 nanoparticles using ionic liquids as the coupling reagent. Ionic liquid‐modified magnetic nanoparticle‐grafted lipase preferentially located at the oil–water interface. It has higher catalytic activity than its native counterpart. A modified Michaelis–Menten model was used to elucidate the effect of stirring rate, aqueous–organic phase ratio, total amount of enzyme, and ester chain length. The influences of these conditions on esters hydrolysis at oil–water interface were consistent with the introduction of the ionic liquids interlayer. Ionic liquids could be used to control the oil–water interfacial characteristics during lipase catalyzed hydrolysis, and thus control the behavior of immobilized lipase. © 2011 American Institute of Chemical Engineers AIChE J, 2012