Glass plates tethered with 3-aminopropyl groups were prepared and fullerene (C60) was mounted onto the amine groups via NH insertion of the terminal amine moiety into one of the double bonds of fullerene. Cubic zeolite-A crystals covered with 3-aminopropyl groups on the external surface were independently prepared by treating the crystals with (3-aminopropyl)triethoxysilane. The zeolite-A crystals readily assembled in the form of monolayers on the fullerene-tethering glass substrates when they were allowed to contact in boiling toluene. The assembled zeolite-A monolayers remained intact even after sonication for 5 min in toluene. In contrast, the assembly of zeolite crystals does not occur if the tethering of either 3-aminopropyl or fullerene is omitted. Based on the two contrasting results, the monolayer assembly of zeolite crystals on glass is proposed to occur by formation of a large number of propylamine−fullerene−propylamine covalent linkages between each zeolite crystal and the glass substrate. Scanning electron microscope images revealed that zeolite-A crystals assemble with a face pointing normal to the plane of the substrate. The monolayers consist of small domains comprised of about 110 closely packed zeolite-A crystals aligned in uniform three-dimensional orientation. The same procedure also worked well for the monolayer assembly of larger ZSM-5 crystals. Migration of the weakly bound zeolite crystals over the glass substrate driven by a large number of hydrogen bonds between the surface-bound amine groups on the neighboring crystals is proposed to play an important role in inducing the close packing.

β-Glucosidase and D-glucose-tethering micrometer-sized zeolite crystals self-assemble into thin (2-20 µm) and very long (>1 cm) fibrous aggregates in water. The process proceeds at a faster rate in a buffer solution of pH 4.8 at which the enzymatic activity is highest. The zeolite and enzyme remain intact within the fibrous material. Furthermore, the enzymatic activity of β-glucosidase is preserved even after they are kept in water for more than 6 months at room temperature. With the zeolite to enzyme weight ratio of 5, all the zeolite crystals are buried within the round fibrils which consist of either a single strand or helical double strands. Upon increasing the ratio to 10, clusters of unburied zeolite crystals appear on the exterior of the fibrils, while narrow flat fibers with smooth surfaces are formed upon decreasing the ratio to 2.5. The process is proposed to initiate by the tight binding between the zeolite-bound D-glucose moieties and β-glucosidase followed by crystallization of the enzyme over the zeolite-bound enzyme monolayer. This report thus reveals a novel behavior of β-glucosidase and demonstrates an unprecedented phenomenon that an enzyme and its substrate-tethering inorganic crystals self-assemble into structured aggregates.

The visible absorption band of iodine adsorbed on zeolite blue-shifted with increasing the electropositivity of the countercation and the aluminum content in the framework. This phenomenon was attributed to the increase in the donor strength of the zeolite framework based on the analogous spectral shift of iodine in solution. In support of this, a negative linear correlation was observed between the measured visible bands of iodine adsorbed on various zeolites and their calculated Sanderson's intermediate electronegativities. However, the simultaneous change in the electrostatic field strength within the zeolite pores, as a result of the change in the number and the size of the cation, has to be taken into account in order to interpret the overall spectral shifts more precisely. The iodine band sensitively blue-shifted with decreasing the moisture content in the framework but red-shifted with the loss of NH3 from NH4 +-exchanged zeolites. The visible band of iodine also progressively red-shifted with increasing the adsorbed amount, presumably due to the nature of iodine to deplete electron density from the framework. The framework structure also affected the spectral shift of the visible iodine band. The overall results established that iodine can be used as a novel molecular probe for the quantitative evaluation of the zeolite donor strength.

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