To investigate the effects of surface property of mesoporous supports on the lipase immobilization and the performance of immobilized lipase, the mesoporous molecular sieve SBA-15 is functionalized with three organic moieties, dimethyl (DM), diisopropyl (DIP), and diisobutyl (DIB), respectively, by post-synthesis grafting and one-pot synthesis methods. Porcine pancreas lipase (PPL) is immobilized on SBA-15 supports through hydrogen bonding and hydrophobic interaction. The hydrophobic adsorption involves no active sites of PPL, and neither hyper-activation nor total inactivation occurs. The study on the intrinsic stability of PPL, including thermal stability, pH stability, and storage stability, indicates that the entrapment in mesoporous supports, and especially in organic-functionalized supports, makes PPL more resistant to temperature increment but more sensitive to pH change. The reusability investigation shows that the organic modification of mesoporous surface inhibits the enzyme leaching to some extent, resulting in a better operational stability. © 2009 American Institute of Chemical Engineers AIChE J, 2010
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