The formation of continuous patterns of nanostructured materials using directed self-assembly under external fields has generated considerable current research interest. We demonstrate for the first time such continuous patterning by inducing irreversible self-assembly leading to nucleation in mesocopic materials (inorganic, organic, and nanoparticles) using a tightly focused laser beam in an optical tweezers apparatus. A dense aqueous dispersion or solution of the material which has high absorption at the laser wavelength is taken in a sample holder so that some material is adsorbed on the top surface. A hot spot is created on the top surface when the adsorbed material absorbs the high intensity at the focus of the laser beam (a submicrometer sized spot), due to which a water vapor bubble is formed. This causes self-assembly of material around the bubble due to Gibbs-Marangoni convection and capillary flow after which the material eventually nucleates into a crystalline state. The bubble is "trapped" at the hot spot due to the temperature gradient around it and can be manipulated by thermal forces generated optically, so that the system may be described as a "thermo-optical" tweezers. We translate the trapped bubble using the microscope sample holder stage of the apparatus so that the nucleation site of the material is simultaneously translated generating continuous patterns. We have demonstrated the technique using exotic inorganic materials such as soft oxometalates, an organic material such as glycine, and a fluorescent dye such as perylene as well as with carbon nanotubes. We have written patterns over lengths of nearly 1 mm at the rate of 1 Hz, with best resolution of about 4 μm. The technique has potential for a wide range of applications ranging from solution processed printable electronics to controlled catalysis.

A single novel enzyme, glyoxalase III, which catalyses the conversion of methylglyoxal into D-lactate without involvement of GSH, has been detected in and purified from Escherichia coli. Of several carbonyl compounds tested, only the alpha-ketoaldehydes methylglyoxal and phenylglyoxal were found to be substrates for this enzyme. Glyoxalase III is active over a wide range of pH with no sharp pH optimum. In its native form it has an M(r) of 82000 +/- 2000, and it is composed of two subunits of equal M(r). Glutathione analogues, which are inhibitors of glyoxalase I, do not inhibit glyoxalase III. Glyoxalase III is found to be sensitive to thiol-blocking reagents. The p-hydroxymercuribenzoate-inactivated enzyme could be almost completely re-activated by dithiothreitol and other thiol-group-containing compounds, indicating the possible involvement of thiol group(s) at or near the active site of the enzyme.