Ribotyping and a study of transmission of Staphylococcus aureus collected from food preparation facilities.

Food poisoning from Staphylococcus aureus is sometimes caused by improper handling of food items in food preparation facilities. Prevention of contamination by employees is particularly important in facilities where a significant amount of food preparation is performed by hand. Some experiments have been performed to describe bacterial cross-contamination in the food preparation process, but there have been few studies of cross-contamination in actual food preparation facilities.

Decrease in rice allergenic proteins of polished rice grains by incubating with a miso solution.

The effect of miso on allergenic proteins in rice seeds was investigated. When polished rice grains were incubated at 37 degrees C for 30-120 min with a 10% miso solution, but not with heat-treated miso or 1% NaCl, the amount of soluble proteins extracted from the rice grains with 1 M NaCl markedly decreased. SDS-PAGE, immunoblotting and densitometric analyses of these soluble proteins and insoluble proteins indicate that 26 kDa globulin and 14-16 kDa allergens in the grains were decreased to 15-60% during incubation with the miso solution, especially soybean-koji miso, without any large change in the content of major insoluble proteins.

Structural characterization of the 16-kDa allergen, RA17, in rice seeds. Prediction of the secondary structure and identification of intramolecular disulfide bridges.

The 16-kDa rice allergen, RA17, belonging to the alpha-amylase/trypsin inhibitor family was isolated from rice seed and structurally characterized by identifying cystine-containing peptides and predicting the secondary structure and hydrophobic regions. Eight peptides, which constitute three sets of cystine-containing peptides, were purified by HPLC from a thermolytic digest of RA17 and identified by their amino acid sequence and composition, indicating five intramolecular disulfide bridges: Cys34-Cys94, Cys26-(Cys50 or Cys51)-Cys110 and Cys12-(Cys62 or Cys64)-Cys122. Analyses of the CD spectrum and the Chou-Fasman prediction suggested that RA17 had some helical- and sheet-structure regions.