Amylase production by Bacillus cereus IND4 was investigated by solid state fermentation (SSF) using cow dung substrate. The SSF conditions were optimized by using one-variable-at-a-time approach and two level full factorial design. Two level full factorial design demonstrated that moisture, pH, fructose, yeast extract and ammonium sulphate have significantly influenced enzyme production (p < 0.05). A central composite design was employed to investigate the optimum concentration of these variables affecting amylase production. Maximal amylase production of 464 units/ml of enzyme was observed in the presence of 100% moisture, 0.1% fructose and 0.01% ammonium sulphate. The enzyme production increased three fold compared to the original medium. The optimum pH and temperature for the activity of amylase were found to be 8.0 and 50 °C, respectively. This enzyme was highly stable at wide pH range (7.0–9.0) and showed 32% enzyme activity after initial denaturation at 50 °C for 1 h. This is the first detailed report on the production of amylase by microorganisms using cow dung as the low cost medium.

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In this work, Langmuir¯lms of organized assemblies of -lactoglobulin (LG) with 1-ethyl-3-methyl imidazolium ethyl sulfate (IL-emes) have been characterized at air/water interface using surface pressure-speci¯c area isotherms and dilational rheology. The protein in the IL-mediated assembly shows excellent packing at the interface and is stable as seen in circular dichroic spectroscopy. These spread¯lms on nickel chloride were transferred as Langmuir-Scha®er¯lms of LG and LGþIL-emes and used as template for designing nanoclusters of nickel oxide. The nanoclusters have been characterized using transmission electron microscopy (TEM) and powder XRD. While pure protein template gives needle-shaped structures, the IL-mediated template gives spherical shapes of hexagonal nickel oxide in the range 30 nm to 40 nm. Presence of ionic liquid seems to slow down the growth of the cluster and also prevents aggregation of the clusters.