Chemical characterization of groundwater is essential to bring out its nature and utility. Samples from shallow and deep ground water of the same locations were collected and studied for their geochemical characteristics. Sediment samples from different depths were collected and analyzed minerals using Fourier transform infrared spectroscopy (FTIR) and scanning electron microscope (SEM) The resisitivity logging was carried out in the bore well to understand the variations in depth to fresh water potential. The shallow ground water is dominated by Na-Cl-HCO3-SO4 and deeper groundwater by Na-HCO3-SO4-Cl types. It is observed that there is a significant ionic variation with depth. The ionic strength of the deeper samples is lesser than shallower. Wide pH variations in the shallow water samples are due to ion exchange process. The thermodynamic stability plot was used to identify the state of stability. It is inferred that there is no major significant difference in the thermodynamic state of stability in the shallow and the deeper aquifers as the aquifer matrix for the shallow and deeper aquifers are almost similar. Saturation index of gibbsite, kaolinite, calcite, dolomite and anhydrite were studied for shallow and deep aquifers, to identify the difference in hydro chemical signatures. The Si/Al ratios of shallow samples are less when compared to the deeper samples. Leaching of secondary salts was the chief mechanism controlling the ground water chemistry of the region.

Three cytochrome P450 monooxygenase CYP52 gene family members were isolated from the sophorolipid-producing yeast Starmerella bombicola (former Candida bombicola), namely, CYP52E3, CYP52M1, and CYP52N1, and their open reading frames were cloned into the pYES2 vector for expression in Saccharomyces cerevisiae. The functions of the recombinant proteins were analyzed with a variety of alkane and fatty acid substrates using microsome proteins or a whole-cell system. CYP52M1 was found to oxidize C 16 to C 20 fatty acids preferentially. It converted oleic acid (C 18:1 ) more efficiently than stearic acid (C 18:0 ) and linoleic acid (C 18:2 ) and much more effectively than ␣-linolenic acid (C 18:3 ). No products were detected when C 10 to C 12 fatty acids were used as the substrates. Moreover, CYP52M1 hydroxylated fatty acids at their -and -1 positions. CYP52N1 oxidized C 14 to C 20 saturated and unsaturated fatty acids and preferentially oxidized palmitic acid, oleic acid, and linoleic acid. It only catalyzed -hydroxylation of fatty acids. Minor -hydroxylation activity against myristic acid, palmitic acid, palmitoleic acid, and oleic acid was shown for CYP52E3. Furthermore, the three P450s were coassayed with glucosyltransferase UGTA1. UGTA1 glycosylated all hydroxyl fatty acids generated by CYP52E3, CYP52M1, and CYP52N1. The transformation efficiency of fatty acids into glucolipids by CYP52M1/UGTA1 was much higher than those by CYP52N1/UGTA1 and CYP52E3/UGTA1. Taken together, CYP52M1 is demonstrated to be involved in the biosynthesis of sophorolipid, whereas CYP52E3 and CYP52N1 might be involved in alkane metabolism in S. bombicola but downstream of the initial oxidation steps.

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