Febrile urinary tract infection in children: changes in epidemiology, etiology, and antibiotic resistance patterns over a decade.

Background: Understanding the epidemiology and prevalence of febrile urinary tract infection (fUTI) in children is important for risk stratification and selecting appropriate urine sample collection candidates to aid in its diagnosis and treatment.

Purpose: This study aimed to analyze the epidemiology, etiology, and changes in antibiotic susceptibility patterns of the first fUTI in children.

Methods: This retrospective observational cohort study included children younger than 19 years of age who were diagnosed and treated for their first fUTI in 2006-2016.

Production of 8-hydroxydaidzein from soybean extract by Aspergillus oryzae KACC 40247.

Aspergillus oryzae KACC 40247 was selected from among 60 fungal strains as an effective 7,8,4'-trihydroxyisoflavone (8-hydroxydaidzein)-producing fungus. The optimal culture conditions for production by this strain in a 7-L fermentor were found to be 30 °C, pH 6, and 300 rpm. Under these conditions, A.

Hydrolysis of isoflavone glycosides by a thermostable β-glucosidase from Pyrococcus furiosus.

The recombinant β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus was purified with a specific activity of 330 U/mg for genistin by His-trap chromatography. The specific activity of the purified enzyme followed the order genistin > daidzin > glycitin> malonyl glycitin > malonyl daidzin > malonyl genistin. The hydrolytic activity for genistin was highest at pH 6.

Production of 10-hydroxystearic acid from oleic acid and olive oil hydrolyzate by an oleate hydratase from Lysinibacillus fusiformis.

A recombinant enzyme from Lysinibacillus fusiformis was expressed, purified, and identified as an oleate hydratase because the hydration activity of the enzyme was the highest for oleic acid (with a k (cat) of 850 min(-1) and a K (m) of 540 μM), followed by palmitoleic acid, γ-linolenic acid, linoleic acid, myristoleic acid, and α-linolenic acid. The optimal reaction conditions for the enzymatic production of 10-hydroxystearic acid were pH 6.5, 35 °C, 4% (v/v) ethanol, 2,500 U ml(-1) (8.

Characterization of a β-glucosidase from Sulfolobus solfataricus for isoflavone glycosides.

The specific activity of a recombinant β-glucosidase from Sulfolobus solfataricus for isoflavones was: daidzin > glycitin > genistin > malonyl genistin > malonyl daidzin > malonyl glycitin. The hydrolytic activity of this enzyme for daidzin was highest at pH 5.5 and 90°C with a half-life of 18 h, a K (m) of 0.

Conversion of oleic acid to 10-hydroxystearic acid by whole cells of Stenotrophomonas nitritireducens.

The optimal reaction conditions for the conversion of oleic acid to 10-hydroxystearic acid by whole cells of Stenotrophomonas nitritireducens were: pH 7.5, 35 °C, 0.05% (w/v) Tween 80, 20 g cells l(-1), and 30 g oleic acid l(-1) in an anaerobic atmosphere.

Characterization of a mannose-6-phosphate isomerase from Thermus thermophilus and increased L-ribose production by its R142N mutant.

An uncharacterized gene from Thermus thermophilus, thought to encode a mannose-6-phosphate isomerase, was cloned and expressed in Escherichia coli. The maximal activity of the recombinant enzyme for L-ribulose isomerization was observed at pH 7.0 and 75°C in the presence of 0.

Substrate specificity of ribose-5-phosphate isomerases from Clostridium difficile and Thermotoga maritima.

The activity of ribose-5-phosphate isomerases (RpiB) from Clostridium difficile for D-ribose isomerization was optimal at pH 7.5 and 40 degrees C, while that from Thermotoga maritima for L-talose isomerization was optimal at pH 8.0 and 70 degrees C.