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. betamax rip to computer. FREE fotoshop cs6 downloadL-Amino acid oxidase (hereinafter referred to as “l-AAO”) catalyzes the oxidative deamination of l-amino acids to produce ammonium ion, a hydrogen peroxide, and ammonia. The l-amino acids are utilized in proteinogenic pathways, and therefore l-AAO is an important enzyme that can be applied for producing valuable feed additives, such as lysine, threonine, methionine, tryptophan, isoleucine, leucine, valine, phenylalanine and taurine.
L-AAO enzymes are widely distributed in prokaryotes and eukaryotes. However, l-AAOs are generally catalytically and structurally restricted to vertebrates. These characteristics have made vertebrate l-AAOs difficult to over-express in heterologous systems and isolate in large quantities. Furthermore, the low yield of expressed vertebrate l-AAOs in heterologous systems remains one of the major hurdles to developing cost-effective expression systems.
The recent discovery of L-amino acid oxidase from Pseudomonas stutzeri (P. stutzeri AAO) (WO 2003/027866; Hopp et al., FEBS Lett, 563: 170-174, 2004) and L-amino acid oxidase from Hyperthermus butylicus (H. butylicus AAO) (WO 2004/095941; Hopp et al., Biochem J, 416: 517-522, 2004), both of which are capable of catalyzing oxidative deamination of alanine (alanine), has created new possibilities for producing amino acid-based animal feed supplements and preventing the European outbreak of mad cow disease.
Although AAO enzymes from these sources have been previously characterized, it has not been reported that these enzymes could be used to produce animal feed supplements.
AAO from Pseudomonas stutzeri has also been cloned and overexpressed in recombinant Bacillus subtilis (WO 2003/017426). However, the yield of the overexpressed enzyme is only in the range of 10 mg/L of fermentation broth. Thus, the reaction conditions need to be changed to improve the yield of enzyme protein.One of the reasons I choose to seek employment with a company
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