a b s t r a c tThe effect of heat-moisture treatment (HMT) on the properties of rice starches with high-, medium-and low-amylose content was investigated. The starches were adjusted to 15%, 20% and 25% moisture levels, and heated at 110°C for 1 h. The swelling power, solubility, pasting properties, morphology, enzymatic susceptibility and X-ray crystallinity of the starches were evaluated. HMT reduced the swelling power and solubility of the starches. The strongest effect of HMT occurred on the high-amylose starch; the pasting temperature was increased and the peak viscosity, breakdown, final viscosity and the setback were reduced. HMT increased the starch's susceptibility to a-amylase and promoted a reduction in the starch relative crystallinity.

A hallmark of enteroaggregative Escherichia coli (EAEC) infection is a formation of biofilm, which comprises a mucus layer with immersed bacteria in the intestines of patients. While studying the mucinolytic activity of Pic in an in vivo system, rat ileal loops, we surprisingly found that EAEC induced hypersecretion of mucus, which was accompanied by an increase in the number of mucus-containing goblet cells. Interestingly, an isogenic pic mutant (EAEC ⌬pic) was unable to cause this mucus hypersecretion. Furthermore, purified Pic was also able to induce intestinal mucus hypersecretion, and this effect was abolished when Pic was heat denatured. Site-directed mutagenesis of the serine protease catalytic residue of Pic showed that, unlike the mucinolytic activity, secretagogue activity did not depend on this catalytic serine protease motif. Other pathogens harboring the pic gene, such as Shigella flexneri and uropathogenic E. coli (UPEC), also showed results similar to those for EAEC, and construction of isogenic pic mutants of S. flexneri and UPEC confirmed this secretagogue activity. Thus, Pic mucinase is responsible for one of the pathophysiologic features of the diarrhea mediated by EAEC and the mucoid diarrhea induced by S. flexneri.

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The objective of this study was to produce encapsulated protein hydrolysates from Whitemouth croaker (Micropogonias furnieri) muscle and its industrialization byproduct. The protein hydrolysates were prepared from the muscle (MPH) and byproduct (BPH) from croaker by enzymatic hydrolysis using Flavourzyme Ò. The hydrolysates were encapsulated using phosphatidylcholine as the wall material of the capsules. The capsules were evaluated for particle size, polydispersity, encapsulation efficiency, zeta potential, morphology, thermal properties, Fourier transform infrared (FTIR) spectroscopy and antioxidant activity. The average size of the capsules for both MPH and BPH liposomes range between 266 and 263 nm with low polydispersity. The capsules showed high encapsulation efficiency of around 80%. The FTIR analysis allowed suggesting that there was an effective ionic complexation between phosphatidylcholine and hydrolysate peptides. The antioxidant activity of the hydrolysates and capsules containing MPH and BPH was similar to the activity of a-tocoferol, but lower than that of vitamin C.

In this sample of teeth without apical resorption the distance between the major foramen and the anatomical root apex was always <1 mm. Deviation of the major foramen from the anatomic apex varied widely amongst tooth groups.