Phenol degradation by halophilic bacteria isolated from hypersaline environments
Phenol degradation by halophilic bacteria isolated from hypersaline environments
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DOI：
10.1007/s10532-012-9617-y
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发表时间：
2013-09-01
期刊：
影响因子：
3.6
通讯作者：
Durrant, Lucia Regina
中科院分区：
文献类型：
--
作者：
Lindenbah Bonfa, Maricy Raquel;Grossman, Matthew James;Durrant, Lucia Regina
苯酚是一种有毒的芳香族化合物，在许多行业中使用或生产，因此是工业废水的常见成分。含苯酚的废物流通常是高盐的，因此需要嗜盐微生物进行有效的生物处理而无需稀释。在这项研究中，从不同的盐环境中分离出的嗜盐细菌，并确定为嗜盐单胞菌organivorans，Arhocarpus aquaeolei和Modicisalibacter tunisiensis被证明能够在苯酚上生长的高盐培养基中含有100克/升的总盐浓度为3毫米（280毫克/升），远高于大多数废物流中发现的浓度。编码芳香族双加氧酶儿茶酚1，2双加氧酶和原儿茶酸3，4-双加氧酶的基因存在于所有菌株中，如通过PCR扩增使用对基因的高度保守区域特异的引物所确定的。原儿茶酸3，4-双加氧酶基因是从分离的H.通过与来自其它微生物的原儿茶酸3，4-双加氧酶蛋白的比较蛋白质序列分析来评估翻译的蛋白质。尽管分析揭示了原儿茶酸3，4-双加氧酶家族之间的广泛的序列差异，但该酶家族鉴定的所有保守结构域氨基酸结构在H.有机食虫酶。
Phenol is a toxic aromatic compound used or produced in many industries and as a result a common component of industrial wastewaters. Phenol containing waste streams are frequently hypersaline and therefore require halophilic microorganisms for efficient biotreatment without dilution. In this study three halophilic bacteria isolated from different saline environments and identified as Halomonas organivorans, Arhodomonas aquaeolei and Modicisalibacter tunisiensis were shown to be able to grow on phenol in hypersaline media containing 100 g/L of total salts at a concentration of 3 mM (280 mg/L), well above the concentration found in most waste streams. Genes encoding the aromatic dioxygenase enzymes catechol 1,2 dioxygenase and protocatechuate 3,4-dioxygenase were present in all strains as determined by PCR amplification using primers specific for highly conserved regions of the genes. The gene for protocatechuate 3,4-dioxygenase was cloned from the isolated H. organivorans and the translated protein was evaluated by comparative protein sequence analysis with protocatechuate 3,4-dioxygenase proteins from other microorganisms. Although the analysis revealed a wide range of sequence divergence among the protocatechuate 3,4-dioxygenase family, all of the conserved domain amino acid structures identified for this enzyme family are identical or conservatively substituted in the H. organivorans enzyme.