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Characterization of a novel actinomyces species discovered in Hong KongWong, Hiu-ling, Beatrice. January 2003 (has links)
Thesis (M.Med.Sc.)--University of Hong Kong, 2003. / Includes bibliographical references (leaves 30-38). Also available in print.
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The influence of iron on the metabolism of actinomyces with special reference to the rate of proteolysis in milkHicks, Winnifred Odetta January 1941 (has links)
[No abstract submitted] / Land and Food Systems, Faculty of / Graduate
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The influence of nitrogen and carbon sources on the metabolism of the actinomycesGilmour, Campbell Graham January 1945 (has links)
[No abstract submitted] / Land and Food Systems, Faculty of / Graduate
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Modellierung des Wachstums- und Produktbildungsverhaltens von ActinomycetenKammerer, Christine. January 2006 (has links)
Stuttgart, Univ., Diss., 2005.
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Molecular taxonomic studies on some high G+C content gram-positive bacteria from human and animal sourcesPascual Ramos, Christina January 2000 (has links)
No description available.
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Isolation and characterisation of esterases from thermophilic ActinomycesOldale, Megan January 2010 (has links)
<p>Alternative sources of fuel are required worldwide, and bio-ethanol is the leading candidate. Lignocellulosic biomass, a waste component of the agricultural industry, is a promising renewable source. Due to its complex structure it is highly recalcitrant, requiring the synergistic action of a battery of enzymes to achieve complete digestion. These enzymes include cellulases, hemicellulase and the accessory enzymes acetyl xylan esterase (AXE) and ferulic acid esterase (FAE). Thermpohilic Actinomyces isolates with the ability to hydrolyze xylan were screened for esterase activity. Two isolates (ORS10 and GSIV1), identified as Streptomyces spp, were positive for AXE activity. A cosmid library representative of isolate ORS10 was composed and screened for AXE activity using -naphthyl acetate as substrate. An 18 kb cosmid clone, 18D7, tested positive for AXE activity. Intracellular fractions extracted from ORS10 were precipitated with ammonium sulphate and partially purified 161-fold. Specific activity was measured after dialysis and ion-exchange chromatography. Overall yield of the partially purified enzyme was 34 %. Two protein bands of molecular masses 40 kDa and 60 kDa have been subjected to trypsin digestion and MALDI-TOF mass spectrometry analysis. The partially purified AXE displayed optimum activity at pH 9 and at 50° / C. AXE activity was stable for at least 1.5 hours between 30° / C and 40° / C, and for 24 hours between pH 6-9. The kM and Vmax values were 16.93 mg/ml and 1645 units/mg enzyme, respectively. The stability of the partially purified AXE at 30° / C-40° / C suggests potential for industrial applications that utilise mesophilic fermentations.</p>
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Characterization of a novel actinomyces species discovered in Hong Kong黃曉靈, Wong, Hiu-ling, Beatrice. January 2003 (has links)
published_or_final_version / Medical Sciences / Master / Master of Medical Sciences
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Molecular and phenotypic characteristics of the genus actinomyces withparticular reference to the human oral cavity唐高妍, Tang, Gaoyan. January 2004 (has links)
published_or_final_version / abstract / toc / Dentistry / Doctoral / Doctor of Philosophy
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PHYSIOLOGICAL STUDIES OF ANTAGONISTIC ACTINOMYCETES FROM THE RHIZOSPHERE OF DESERT PLANTSWhaley, Julian Wendell, 1937- January 1964 (has links)
No description available.
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Isolation and characterisation of esterases from thermophilic ActinomycesOldale, Megan January 2010 (has links)
<p>Alternative sources of fuel are required worldwide, and bio-ethanol is the leading candidate. Lignocellulosic biomass, a waste component of the agricultural industry, is a promising renewable source. Due to its complex structure it is highly recalcitrant, requiring the synergistic action of a battery of enzymes to achieve complete digestion. These enzymes include cellulases, hemicellulase and the accessory enzymes acetyl xylan esterase (AXE) and ferulic acid esterase (FAE). Thermpohilic Actinomyces isolates with the ability to hydrolyze xylan were screened for esterase activity. Two isolates (ORS10 and GSIV1), identified as Streptomyces spp, were positive for AXE activity. A cosmid library representative of isolate ORS10 was composed and screened for AXE activity using -naphthyl acetate as substrate. An 18 kb cosmid clone, 18D7, tested positive for AXE activity. Intracellular fractions extracted from ORS10 were precipitated with ammonium sulphate and partially purified 161-fold. Specific activity was measured after dialysis and ion-exchange chromatography. Overall yield of the partially purified enzyme was 34 %. Two protein bands of molecular masses 40 kDa and 60 kDa have been subjected to trypsin digestion and MALDI-TOF mass spectrometry analysis. The partially purified AXE displayed optimum activity at pH 9 and at 50° / C. AXE activity was stable for at least 1.5 hours between 30° / C and 40° / C, and for 24 hours between pH 6-9. The kM and Vmax values were 16.93 mg/ml and 1645 units/mg enzyme, respectively. The stability of the partially purified AXE at 30° / C-40° / C suggests potential for industrial applications that utilise mesophilic fermentations.</p>
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