The growth, water use, ionic composition, photosynthesis, and chlorophyll fluorescence were measured. Both high Na+ and high Cl- reduced growth of faba bean but plants were more sensitive to Cl- than to Na+. The reductions in growth and photosynthesis were greater under NaCl stress and the effect was mainly additive. An important difference to previous hydroponic studies was that increasing the concentrations of NaCl in the soil increased the concentration of Cl- more than the concentration of

Na+. The data showed that salinity caused by high concentrations of NaCl can reduce growth by the accumulation of high concentrations of both Na+ and Cl- simultaneously, but the effects of the two ions may differ. High Cl- concentration reduces the photosynthetic capacity and quantum yield due to chlorophyll degradation which may result from a structural GDC-0973 cost impact of high Cl- concentration on PSII. High Na+ interferes with K+ and Ca2+ nutrition and disturbs efficient stomatal regulation which results in a depression of photosynthesis and growth. These results suggest that the importance of Cl- toxicity as a cause of reductions in growth and yield under salinity

stress may have been underestimated.”
“The interactions of a commercial soy protein buy BAY 57-1293 isolate (SPI) and a 2:1 SPI:high methoxy pectin (PEC) complex were evaluated over a range of pH values (3-7). The SPI formed very large (>50 mu m) and largely insoluble aggregates (<10%) close to its isoelectric point (IEP, pH 4 and 5) and smaller, more soluble (>80%) particles at higher and lower pH values. The addition of PEC

increased the solubility of SPI close to its IEP (pH 4 and 5) and prevented the formation of very large aggregates. However. PEC reduced the solubility of HMPL-504 SPI at higher and lower pH values presumably via a depletion mechanism. The zeta-potential of diluted SPI dispersions decreased from positive to negative with increasing pH, passing through zero at pH 4.6, the isoelectric point (IEP) of the protein. At pH <6, the addition of PEC reduced the charge of the protein suggesting the formation of a complex while at pH 6 or 7 there was no evidence of complex formation. The increased SPI solubility in the IEP in the presence of PEC is probably due to the formation of charged complex which do not aggregate while the decreased solubility of protein in the presence at high and low PEC is probably due to the formation of insoluble complexes and a depletion interaction respectively. Thermal treatment (30 min, 90 degrees C) enhanced the solubility of the SPI:PEC complexes close to the IEP (pH 4 and 5), but reduces it at low pH (pH 3). The SPI: PEC complexes could be manufactured in the form of a beverage at pilot scale where their solubility was enhanced by homogenization.