Blueprint for a lipase support: Use of hydrophobic controlled‐pore glasses as model systems

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Abstract
For the commercial exploitation of lipase biocatalysis to be successful, it is essential that effective supports are selected for lipase immobilization. In this study hydrophobic controlled-pore glasses have been used as model systems for the immobilization of Rhizomucor miehei lipase. The effect of pore diameter and surface chemistry on enzyme efficiency in a typical esterification reaction under essentially nonaqueous conditions has been examined. It has been found that pore diameters of at least 35 nm are needed for the lipase to be able to utilize the internal volume of the support particles in the immobilization process. Despite the small size of the substrates in the esterification reaction, even larger pores (>100 nm) are required for the lipase efficiency to become independent of pore diameter; below 100 nm lipase activity and efficiency are markedly reduced. It has also been shown that the chemical nature of the hydrophobic surface plays an important part in catalyst design. Although lipase will adsorb readily to a wide range of hydrophobic groups, the highest catalyst activities are obtained when the glass surface is derivatized to give long alkyl chains; the presence of unsaturated derivatives gonerally leads to a reduction in activity. © 1994 John Wiley & Sons, Inc.