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The non-linear optical properties of gemifloxacin (C18H20FN5O4) have been examined using density functional theory (DFT). The molecular HOMO, LUMO composition, their respective energy gaps, MESP contours/surfaces have also been drawn to explain the activity of gemifloxacin. The equilibrium geometries and harmonic frequencies of title molecule was determined and analyzed at DFT/B3LYP level employing the 6-31G(d,p) basis set. The skeleton of both the optimized molecules is non-planar. In general, a good agreement between experimental and calculated normal modes of vibrations has been observed.

Possibility of using full fat soy flour (FFSF) for replacer for whole milk powder (WMP), stevia-mannitol blend as replacer for sugar and soybean oil (SBO) as replacer for cocoa butter in chocolate manufacture without impairing the sensory quality characteristics of chocolate was explored. Data on the sensory evaluation of WMP, sugar and cocoa butter substituted chocolates revealed that 40% (w/w) of WMP, sugar and cocoa butter can be successfully substituted by FFSF, stevia-mannitol blend and SBO, respectively in the preparation of high protein and low sugar chocolate without impairing the sensory attributes. Lecithin was found to be optimum at 0.32% (w/w) level of chocolate mix. Protein content of optimized formulation increased by 21.8% over control. Storage study of the product indicated an increase in hardness, free fatty acid content, peroxide value, total plate count, yeast and mold count, whereas a decrease in moisture content, pH value and sensory scores. The optimized chocolate was found acceptable (score ≥7.0) after 90 days of storage at 16±1°C and~65% RH.

Yeast glutathione reductase was inactivated by the bifunctional reagent, o-phthalaldehyde. The initial rate of inactivation followed pseudo-first order kinetics. Fluorescence spectral properties of modified enzyme indicated the formation of an isoindole derivative from cysteine and lyaine residues present in close proximity as shown by typical fluorescence emission and excitation maximum at 410 nm and 337 nm, respectively. The fluorescence spectral studies with o-phthalaldehyde in the presence and absence of N-ethylmaleimide indicated that both the inhibitors react with the same cysteine residue, which is non-essential for enzyme activity. The coenzyme NADPH did not protect the enzyme against the o-phthalaldehyde reaction while oxidised glutathione prevented o-phthalaldehyde inactivation. This could be due to reaction of the amino group of glutathione with o-phthalaldehyde. Stoichiometry of the reaction showed that the formation of approximately 2 isoindole derivatives per subunit of glutathione reductase is accompanied by 75% loss of activity. The results suggest that o-phthalaldehyde binds to non-essential cysteine and lysine residues present in close proximity which results in conformational changes leading to enzyme inactivation.

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