Immobilization of lipases on hydrophobic supports involves the open form of the enzyme.

@article{Manoel2015ImmobilizationOL,
  title={Immobilization of lipases on hydrophobic supports involves the open form of the enzyme.},
  author={Evelin Andrade Manoel and Jos{\'e} C S Dos Santos and Denise Maria Guimar{\~a}es Freire and Nazzoly Rueda and Roberto Fernandez-Lafuente},
  journal={Enzyme and microbial technology},
  year={2015},
  volume={71},
  pages={53-7}
}
The lipases from Thermomyces lanuginosus and Pseudomonas cepacia have been immobilized on octyl and cyanogen bromide (CNBr) agarose beads. The immobilization on octyl-agarose is slowed with increasing ionic strength, while the immobilization on CNBr is not significantly affected by the ionic strength. The inhibition of the immobilized preparations with diethyl p-nitrophenylphosphate (D-pNPP) was analyzed. The inhibition was more rapid using octyl-lipase preparations than using covalent… CONTINUE READING
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