• Journal of Technologic Dentistry
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• v.21 no.1
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• pp.27-41
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• 1999

The Ag-Pd-Cu alloys containing a small amount of Au is commonly used for dental purposes, because this alloy cheaper than Au-base alloys for clinical use. However, the most important characteristic of this alloy is age-hardenability, which is not exhibited by other Ag-base dental alloys. The specimens used were Ag-30Pd-10Cu ternary alloy and Au addition alloy. These alloys were melted and casted by induction electric furnace and centrifugal casting machine in Ar atmosphere. These specimens were solution treated for 2hr at $800^{\circ}C$ and were then quenched into iced water, and aged at 350-$550^{\circ}C$ Age-hardening characteristic of the small Au-containing Ag-Pd-Cu dental alloys were investigated by means of hardness testing, X-ray diffraction and electron microscope observations, electrical resistance, differential scanning calorimetric, energy dispersed spectra and electron probe microanalysis. Principal results are as follows ; Maximum hardening occured in two co-phases of ${\alpha}_2$ + PdCu In stage II, decomposition of the $\alpha$ solid solution to a PdCu ordered phase($L1_o$ type) and an Ag-rich ${\alpha}_2$ phase occurred and a discontinuous precipitation occurred at the grain boundary. From the electron microscope study, it was concluded that the cause of age-hardening in this alloy is the precipitation of the PdCu redered phase, which has AuCu I type face-centered tetragonal structure. Precipitation procedure was ${\alpha}{\to}{\alpha}_1+PdCu{\to}{\alpha}_2+PdCu$ at Pd/Cu = 3 Pd element of Ag-Pd-Cu alloy is more effective dental alloy on anti-corrosion and is suitable to isothermal ageing at $450^{\circ}C$.

• Korean Journal of Microbiology
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• v.45 no.4
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• pp.332-338
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• 2009

A xylan-decomposing bacterium, HY-20, was isolated from the gut of a honeybee, Apis mellifera, and identified as Bacillus sp. The extracellular GH11 xylanase (XylP) gene (687-bp) of strain HY-20 encoded a protein of 228 amino acids with a deduced molecular mass of 25,522 Da and a calculated pI of 9.33. The primary structure of XylP was 97% identical to that of B. pumilus xylanase (GenBank accession no.: AY526092) that has not been characterized yet. The recombinant His-tagged enzyme (rXylP) overexpressed in Escherichia coli BL21 harboring pET-28a(+)/xylP was purified to electrophoretic homogeneity by cation exchange and gel permeation chromatographies. The purified enzyme exhibited the highest catalytic activity toward birchwood xylan at pH 6.5 and $50^{\circ}C$ and retained approximately 50% of its original activity when pre-incubated at $55^{\circ}C$ for 15 min. The recombinant enzyme was completely inactivated by $Hg^{2+}$ (1 mM) and N-bromosuccinimide (5 mM), while its activity was slightly stimulated by approximately 10% in the presence of $Mn^{2+}$ (1 mM), $Fe^{2+}$ (1 mM), and sodium azide (5 mM). rXylP was able to efficiently degrade various polymeric xylose-based substrates but PNP-sugar derivatives and glucose-based polymers were not susceptible to the enzyme.