Surface crystallization of melt-spun Pd40Ni40P20 glass

The crystallization of Pd₄₀Ni₄₀P₂₀ glass, produced by melt-spinning in air, has been studied by optical metallography. Crystallization is predominantly from the surface and is more prevalent on the wheel-side. The non-uniformity is attributed to variation in quench rate during production. A three-stage anneal permits crystals which have nucleated at the surface to be identified and their size distribution to be analysed. The surface nucleation is heterogeneous and appears to be hindered by mild oxidation. The annealing atmosphere markedly affects the surface crystallization behaviour, as does removal of the original ribbon surface. When nucleation is sparse, partial crystallization causes the development of noticeable relief on the sample surfaces.     

Sensory Evaluation and Acceptability of Cookies Enriched with Sweet Lupine Flour (Lupinus albus cv Multolupa)

Cookies enriched with 0, 5, 10, 15, 20, and 25% full-fat sweet lupine flour (FFSL) were evaluated by a sensory panel using the rank of preference and paired comparison tests. Cookies with 0, 5, and 10% FFSL were preferred while those containing 20 and 25% FFSL were rejected (p≤0.01). Studies conducted with school children showed similar acceptability for 0 and 10% FFSL-containing cookies which was different (p = 0.05) from those containing 20% FFSL. Fortification of the basic formula with 10% FFSL was recommended on the basis of acceptability.     

Improved GaAs-based quantum cascade laser (/spl lambda//spl sim/11 /spl mu/m) using high-reflectivity metal facet coating

By applying a high-reflectivity metal coating to the rear facet of a GaAs-based quantum cascade laser operating at /spl lambda//spl sim/11.5 /spl mu/m, the threshold current has been reduced by 11% at 260 K and pulsed operation of the epilayer-up mounted device was extended from 283 to 294 K.     

Identification and characterization of a two-component regulatory system involved in invasion of eukaryotic cells and heavy-metal resistance in Burkholderia pseudomallei

Burkholderia pseudomallei is the causative agent of melioidosis, a disease increasingly recognized as an important cause of morbidity and mortality in many regions of the world. B. pseudomallei is a facultative intracellular pathogen capable of invading eukaryotic cells. We used Tn5-OT182 mutagenesis to generate mutants deficient in the ability to invade a human type II pneumocyte cell line (A549 cells). One of these mutants, AJ1D8, exhibited approximately 10% of the ability of the parental strain, 1026b, to invade A549 cells. There was no difference in the abilities of 1026b and AJ1D8 to resist killing by RAW macrophages or the human defensin HNP-1. The nucleotide sequence flanking the Tn5-OT182 integration in AJ1D8 was determined, and two open reading frames were identified. The predicted proteins shared considerable homology with two-component regulatory systems involved in the regulation of heavy-metal resistance in other organisms. AJ1D8 was 16-fold more sensitive to Cd2+ and twofold more sensitive to Zn2+ than was 1026b but was not sensitive to any of the other heavy metals examined. The B. pseudomallei two-component regulatory system, termed irlRS, complemented the invasion-deficient and heavy-metal-sensitive phenotype of AJ1D8 in trans. There was no significant difference between the virulence of AJ1D8 and that of 1026b in infant diabetic rats and Syrian hamsters, suggesting that the irlRS locus is probably not a virulence determinant in these animal models of acute B. pseudomallei infection.     

β-hydroxyacyl-coa-dehydrogenase (HADH) activity of unfrozen and frozen—thawed frog (Rana esculenta) legs

The β-hydroxyacyl-CoA-dehydrogenase (HADH) activity of unfrozen and thawed frog legs was investigated. The enzyme was extracted by either immersing frog legs in phosphate buffer 0.1 M, pH 6.0 at 25°C for 15 min or pressing them between trichinoscopy glasses. The enzyme activity was assayed using acetoacetyl-CoA as substrate and measured spectrophotometrically at 340 nm. It was possible by both extraction methods to distinguish between thawed and unfrozen samples although when the juice was obtained by pressing the HADH activity of the dilution was ～ 1.5 times higher than that obtained by immersion. The HADH activity was significantly higher (P≤0·001) in frozen-thawed frogs than in unfrozen legs because during freezing there is a release of HADH. No significative differences were found in the HADH activity in samples frozen in the temperature range -10 to -196°C. HADH activity was not affected by the storage time in crushed ice up to 6 days.