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代尔夫特菌属TBKNP-05对增塑剂邻苯二甲酸二丁酯的降解作用

Degradation of plasticizer di-n-butylphthalate by Delftia sp. TBKNP-05.

作者信息

Patil Neelakanteshwar K, Kundapur Rajesh, Shouche Yogesh S, Karegoudar T B

机构信息

Department of Biochemistry, Gulbarga University, Gulbarga, Karnataka, 585 106, India.

出版信息

Curr Microbiol. 2006 May;52(5):369-74. doi: 10.1007/s00284-005-5258-2. Epub 2006 Apr 6.

Abstract

Bacterial strain Delftia sp. TBKNP-05, isolated by para-hydroxybenzoate enrichment technique, is capable of degrading di-n-butylphthalate (DBP) as a sole source of carbon and energy. Analysis of intermediates by thin-layer chromatography and high-performance liquid chromatography indicated the presence of monobutylphthalate (MBP), phthalate (PA), and protocatechuate (PCA). The washed cells grown on DBP and PA showed appreciable oxidation of DBP, MBP, PA, and PCA. The enzyme activities in cell-free extracts of Delftia sp. TBKNP-05 exhibited the presence of DBP esterase, MBP esterase, PA-dioxygenase, and PCA 4,5-dioxygenase. The PCA is metabolized by meta-cleavage pathway, leading to further mineralization of the compound in this bacterium.

摘要

通过对羟基苯甲酸富集技术分离得到的细菌菌株代尔夫特菌属TBKNP - 05能够以邻苯二甲酸二丁酯(DBP)作为唯一碳源和能源进行降解。通过薄层色谱和高效液相色谱对中间产物的分析表明存在单丁基邻苯二甲酸酯(MBP)、邻苯二甲酸(PA)和原儿茶酸(PCA)。在DBP和PA上生长的洗涤细胞对DBP、MBP、PA和PCA表现出明显的氧化作用。代尔夫特菌属TBKNP - 05无细胞提取物中的酶活性表明存在DBP酯酶、MBP酯酶、PA - 双加氧酶和PCA 4,5 - 双加氧酶。PCA通过间位裂解途径进行代谢,导致该化合物在这种细菌中进一步矿化。

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