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Cocaine esterase from Pseudomonas sp. NCIMB 40427 for detection of cocaine

机译:来自假单胞菌属的可卡因酯酶。 NCIMB 40427可卡因检测

摘要

A cocaine esterase has been isolated from a strain of the bacteria Pseudomonas maltophilta, The cocaine esterase catalyses the debenzoylation of cocaine, This reaction may be used in the detection of cocaine. The enzyme may be incorporated into sensors for this purpose. The cocaine esterase is preferably obtainable from Pseudomonas sp. NCIMB 40427. It catalyzes the debenzoylation of cocaine, has a molecular weight in the unaggregated form of about 120,000 daltons as determined by gel filtration, has esterase activity specifically at the benzoate ester linkage of cocaine, separates at a major band of Rf about 0.2 on PAGE in its aggregated form, and it is completely inhibited by 1 mM phenylmethylsulphonyl fluoride but ineffectively inhibited by 1 mM eserine, each determined at 30° C. with respect to 2 mM cocaine as substrate.
机译:从细菌假单胞菌麦芽假单胞菌的菌株中分离出可卡因酯酶,可卡因酯酶催化可卡因的脱苯甲酰化,该反应可用于检测可卡因。为此目的,可以将酶掺入传感器中。可卡因酯酶优选可得自假单胞菌(Pseudomonas sp。)。 NCIMB40427。它催化可卡因的脱苯甲酰化,通过凝胶过滤测定,其非聚集形式的分子量约为120,000道尔顿,尤其在可卡因的苯甲酸酯键上具有酯酶活性,在Rf的主带上分离,约为0.2 PAGE以其聚集形式存在,并且被1 mM苯基甲基磺酰氟完全抑制,但被1 mM色氨酸无效抑制,每一个相对于2 mM可卡因作为底物在30°C下测定。

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