The protease Esperase † was modified by covalent bonding with two grades of a reversible soluble-insoluble co-polymer of methacrylic acid and methyl-methacrylate, namely Eudragit † L 100 and Eudragit † S 100. The optimum reaction conditions and washing protocol were investigated and it was found that Esperase † modified with Eudragit † L 100 showed greater activity than if modified with Eudragit † S 100. This should be expected as there is a greater quantity of active sites, namely carboxyl groups, per mass of Eudragit † L 100 in comparison with Eudragit † S 100 to interact with the enzyme. Gel filtration confirmed that Eudragit † L 100 covalently bonded to Esperase † . Treatment of the modified Esperase † on wool showed that the enzyme modified with Eudragit † L 100 had greater activity towards the wool and appeared more effective in shrink resistant finishing.

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(Received M a y 22, 1995)Studies have been made of the local atomic structure ofclustered and porous silicon nanostructures, with the object of obtaining more information on the environments which exist in highly PL-efficient material. In some structures the Si environments can be interpreted in terms of a small crystalline core surrounded by configurationally disordered material. Finally, although the details of the individual mechanisms responsible for the emission appear to be different for clustered and porous material, the overall behaviour can be linked t o the sizes and dimensionality of the units involved.

The use of protease in the raw wool scouring process was investigated. Both native protease and an enlarged protease prepared by chemical modification were used. It was demonstrated that enzymatic treatment with protease in the scouring process (bio-scouring) can achieve cleaning of the fibre and modification of the cuticle layer leading to shrink-resistance. A reduction of lipid content was found and led to an improvement in dyeability of the fibre.