The global high prevalence of hypertension and cardiovascular disease has raised concerns regarding the sodium content of the foods which we consume. Over 75% of sodium intake in industrialized diets is likely to come from processed and restaurant foods. Therefore international authorities, such as the World Health Organisation, are encouraging the food industry to reduce sodium levels in their products. Significant sodium reduction is not without complications as salt plays an important role in taste, and in some products is needed also for preservation and processing. The most promising sodium reduction strategy is to adapt the preference of consumers for saltiness by reducing sodium in products in small steps. However, this is a time-consuming approach that needs to be applied industry-wide in order to be effective. Therefore the food industry is also investigating solutions that will maintain the same perceived salt intensity at lower sodium levels. Each of these has specific advantages, disadvantages, and time lines for implementation. Currently applied approaches are resulting in sodium reduction between 20-30%. Further reduction will require new technologies. Research into the physiology of taste perception and salt receptors is an emerging area of science that is needed in order to achieve larger sodium reductions.

The food industry is under high pressure to significantly reduce the salt levels in their products. This study shows that it is possible to compensate salt reduction in instant bouillons by higher levels of savory aroma. A combination of potassium chloride based salt replacer and extra aroma was found to compensate approximately 30% sodium reduction without significant change of the flavor profile.

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A heat-stable lipase from Pseudomonas glumae was purified to homogeneity. Its positional and stereospecific properties were investigated and compared with those of the well-known porcine pancreatic lipase. The kinetic properties of both enzymes were determined by use of six isomeric synthetic pseudoglycerides all composed of a single hydrolyzable fatty acyl ester bond and two lipase-resistant groups: one acylamino and one ether function. Two enzyme assay techniques were applied: a detergent-free system, the monomolecular surface film technique, and the pH-stat technique using clear micellar solutions of substrate in the presence of Triton X-100. Regarding the cleavage of primary ester bonds, P. glumae lipase possesses no stereopreference. In contrast, a large stereopreference in favor of the R-isomer is found for the hydrolysis of secondary ester bonds. Secondary ester bonds are efficiently cleaved by the lipase, which makes it of potential interest for enzymatic synthetic purposes. For the hydrolysis of this R-isomer a correlation between the experimental catalytic turnover rate and the binding constant for micelles was observed. The kinetic data of P. glumae lipase have been analyzed in terms of the scooting and hopping models for the action of lipolytic enzymes [Upreti, G.C., & Jain, M.K. (1980) J. Membr. Biol. 55, 113-121]. The results presented in this study are best explained by assuming that glumae lipase leaves the interface after a limited number of catalytic cycles.

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