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Biosynthesis and properties of an extracellular metalloprotease from the Antarctic marine bacterium Sphingomonas paucimobilis

机译:从南极海洋细菌鞘氨基氨基磷肌细胞外细胞间金属蛋白酶的生物合成及性质

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An extracellular protease from the marine bacterium Sphingomonas paucimobilis, strain 116, isolated from the stomach of Antarctic krill, Euphausia superba Dana, was purified and characterized. The exretion of protease was maximal at temperatures from 5 to 10 deg C, i.e. below the temperature optimum for the strain growth (15 deg C). The highly purified enzxyme was a metalloprotease (sensivity to ethylenediaminetetraacetic acid (EDTA)) and showed maximal activity against proteins at 20-30 deg C and pH 6.5-7.0, and towards N-benzoyl-tyrosine ethyl ester (BzTyrOEt) at pH 8.0. At 0 deg C the enzyme retained as much as 47
机译:纯化并表征了从南极KRILL,南极KRILL的胃中分离的肺癌鞘氨基氨基菌菌株116的细胞外蛋白酶。蛋白酶的稀释在5至10℃的温度下最大,即低于菌株生长的温度(15℃)。高度纯化的酶是金属蛋白酶(对乙二胺四乙酸(EDTA)的灵敏度),并在20-30℃和pH6.5-7.0中显示出对蛋白质的最大活性,并在pH8.0下朝向N-苯甲酰基酪氨酸乙酯(Bztyroet)。在0℃下,酶保留多达47

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