ABSTRACT
The quality of dehydrated taro slices in accelerated storage (45°C and 75% RH) was determined as a function of initial water activity (aw) and package type. Color, rehydration capacity, thiamin content, and α-tocopherol content were monitored during 34 weeks of storage in polyethylene and foil laminate packaging at initial storage aw of 0.35 to 0.71. Initial aw at or below 0.54 resulted in less browning and higher rehydration capacity, but not in significantly higher α-tocopherol retention. Foil laminate pouches resulted in a higher rehydration capacity and increased thiamin retention compared to polyethylene bags. Type of packaging had no effect on the color of the samples. Product stability was highest when stored in foil laminate pouches at 0.4aw. Sensory panels were held to determine the acceptability of rehydrated taro slices using samples representative of the taro used in the analytical tests. A hedonic test on rehydrated taro's acceptability was conducted in Fiji, with panelists rating the product an average of 7.2 ± 1.5 on a discrete 9-point scale. Using a modified Weibull analysis (with 50% probability of product failure), it was determined that the shelf life of dehydrated taro stored at 45°C was 38.3 weeks.
ABSTRACT
The macrophage has been shown to bind potentially pathogenic bacteria in the absence of serum components or opsonins but the mechanism is poorly understood. The rich array of sugars on the surface of group B streptococci plus the presence of membrane-associated lectin receptors on the macrophage suggests that this is a likely means for bacterial recognition by these host defense cells. Inhibition studies with free sugars and neoglycoconjugates of bovine serum albumin, however, failed to confirm this hypothesis. Furthermore, neuraminidase-treatment to expose galactose residues and the use of isogenic bacterial strains having no capsule or no capsular sialic acid yielded no confirmation of lectin-mediated recognition. The trypsin-sensitive receptor exhibited temperature dependence and a requirement for divalent cations distinct from that reported for the lectin-like galactose receptor. The activity of this streptococcal binding receptor was inhibited by 2-deoxy-D-glucose but not by neutrophil elastase. Pre-exposure of macrophages to bound fibronectin and treatment with phorbol ester each enhanced bacterial binding. These data fail to support a role for the galactose lectin and provide preliminary evidence for involvement of the leukocyte integrins in macrophage recognition of group B streptococci.
Subject(s)
Integrins/metabolism , Macrophages/microbiology , Receptors, Mitogen/metabolism , Streptococcus agalactiae/metabolism , Animals , Bacterial Adhesion/drug effects , Carbohydrates/pharmacology , Cations, Divalent/pharmacology , Deoxyglucose/pharmacology , Female , Leukocyte Elastase , Mice , Mice, Inbred BALB C , Neuraminidase , Pancreatic Elastase/pharmacology , Phagocytosis/physiology , Phorbol 12,13-Dibutyrate/pharmacology , Receptors, Fibronectin/metabolism , Temperature , Trypsin/pharmacologyABSTRACT
We have developed a solid phase, direct binding, enzyme-linked immunosorbent assay (ELISA) to detect and quantify the adherence of group B streptococci to murine macrophages. The assay correlated well with direct microscopic quantification of adherence. As few as 3.8 x 10(4) bacteria/assay well or less than one bacterium per macrophage could be detected. This assay is both quantitative and selective, and is readily adaptable for multiple sample analysis. It provides a valuable alternative to visual detection of bacterial adherence.
