Streptozotocin-induced diabetes resulted in a decrease in the cathepsin D activity (free and total) in rat liver, kidney, brain and heart with a concomitant increase in tissue protein content and amino acids pool size. Treatment with insulin brought about the restoration of the cathepsin D activity to normal or greater than normal levels; tissue protein content and amino acids pool size also returned to normal values.

The efficacy of lipase (triacylglycerol acylhydrolases EC 3.1.1.3) as a detergent additive from a newly isolated marine halophilic bacteria Bacillus sonorensis from marine clams Paphia malabarica collected in the Kalbadevi Estuary, Mumbai, has been assessed and reported. In terms of activity and stability, the lipase exhibited maximum activity in alkaline conditions and was observed to be stable over a temperature range from room temperature to 60°C. The activity of the lipase increased in the presence of surfactants and detergents. Due to these properties of the lipase from marine bacteria, it was used as an additive in detergents to study its efficiency at corn oil removal from fabrics. The washing studies indicated that the efficiency of corn oil removal from the cotton fabrics increased by 20 % when lipase was incorporated in the detergent as compared to the treatment with detergent alone. The lipase was also capable of removing corn oil from natural as well as synthetic fabrics dyed with a respective, preferred class of dyes.Ravindra Adivarekar is currently a professor and the head of the Department of Fibres and Textiles Processing Technology at the Institute of Chemical Technology (ICT), Mumbai, India. His research areas of interest are microbial enzymes for textile processing, detergent formulations, natural dyes and mordants, dyeing and printing of textiles, medical textiles, fiber modification, and energy conservation.J Surfact Deterg (2013) 16:435-443 443

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Characterization, kinetic and thermodynamic parameters of purified pectinase from Bacillus subtilis, isolated from a marine sediment sample collected from Chinchani beach at Tarapore, India, were studied. Marine pectinase produced under submerged growth conditions was purified by ammonium sulfate precipitation followed by gel filtration chromatography using DEAE cellulose. Partial characterization of the marine pectinase was carried out in terms of effect of pH, temperature, substrate concentration, and metal ions. It was found that pectinase from marine B. subtilis showed maximal activity in alkaline buffer at pH 9.0 and at 40°C. It was also found that metal ions, namely, Mn(2+) and Fe(2+), stimulate pectinase activity. Marine pectinase followed Michaelis-Menten kinetics. The kinetics and thermodynamic parameters of the purified marine pectinase from B. subtilis were studied as the characterization of the enzyme is vital for its use in industrial processes.