Quantatitive assessment of enzyme immobilization capacity in porous silicon

Immobilized enzyme systems are important in a broad range of applications, from biological sensing to the industrial-scale biocatalytic synthesis of chiral products. We demonstrate the ability to systematically vary and quantitatively assess the immobilization capacity of porous silicon thin films for the enzyme glutathione-S-transferase in a manner predicted by a simple geometric model of the porous silicon matrix. We find that the immobilization capacity quantatitively correlates with systematic changes in the device thickness. These results are significant since, despite the wide range over which porous silicon morphology and surface area can be varied, few attempts have been made to systematically characterize surface binding capacity. Our findings suggest that porous silicon can be an ideal matrix, where immobilization of a predictable quantity of biological material is desired.