Abstract
A novel procedure was developed to intercalate enzymes into dispersed phyllosilicates that were cross-linked with silicate polymers formed by the hydrolysis of tetramethyl orthosilicate (TMOS). Lipoxygenase (LOX) intercalated into cross-linked phyllosilicates exhibited high enzymatic activity. The enzyme-phyllosilicate composite prepared by this procedure had an improved pore network. Alkylamines were used to occupy the charge sites of the phyllosilicate, which increased the hydrophobicity of the phyllosilicate and reduced charge-charge interaction between LOX and the phyllosilicate. The amount of macropores and the enzymatic activity of the lipoxygenase-phyllosilicate composites increased with an increase in the ratio of trimethylammonium (TMA)-phyllosilicate to cross-linking reagent TMOS. LOX intercalatively immobilized into phyllosilicates displayed good storage stability and reusability at ambient temperature.
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Shen, S., Hsu, AF., Foglia, T.A. et al. Effectiveness of cross-linked phyllosilicates for intercalative immobilization of soybean lipoxygenase. Appl Biochem Biotechnol 69, 79–90 (1998). https://doi.org/10.1007/BF02919390
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DOI: https://doi.org/10.1007/BF02919390