da Fonseca Francine S A, Angolini Célio F F, Arruda Marco A Zezzi, Junior Cícero A L, Santos Clelton A, Saraiva Antonio M, Pilau Eduardo, Souza Anete P, Laborda Prianda R, de Oliveira Patrícia F L, de Oliveira Valéria M, Reis Francisco de Assis M, Marsaioli Anita J
Chemistry Institute, University of Campinas, P.B 6154, 13083-970 Campinas, São Paulo, Brazil; Institute of Agricultural Sciences, Federal University of Minas Gerais, 39404-547 Minas Gerais, Brazil.
Chemistry Institute, University of Campinas, P.B 6154, 13083-970 Campinas, São Paulo, Brazil.
Biotechnol Rep (Amst). 2015 Sep 5;8:152-159. doi: 10.1016/j.btre.2015.09.001. eCollection 2015 Dec.
A gram-positive bacterium, denominated CFA-06, was isolated from Brazilian petroleum in the Campos Basin and is responsible for the degradation of aromatic compounds and petroleum aromatic fractions. The CFA-06 strain was identified as using the 16S rRNA and gyrase B sequence. Enzymatic assays revealed the presence of two oxidoreductases: a catalase and a new oxidoreductase. The oxidoreductases were enzymatically digested and analyzed via ESI-LTQ-Orbitrap mass spectrometry. The mass data revealed a novel oxidoreductase (named BsPMO) containing 224 amino acids and 89% homology with a hypothetic protein from (CFA-06) and a catalase (named BsCat) with 491 amino acids and 60% similarity with the catalase from (SAFR-032). The new protein BsPMO contains iron atom(s) and shows catalytic activity toward a monooxygenase fluorogenic probe in the presence of cofactors (NADH, NADPH and NAD). This study enhances our knowledge of the biodegradation process of petroleum by .
一种革兰氏阳性细菌，命名为CFA - 06，从巴西坎波斯盆地的石油中分离出来，它负责芳香族化合物和石油芳香馏分的降解。使用16S rRNA和gyrase B序列对CFA - 06菌株进行了鉴定。酶活性测定显示存在两种氧化还原酶：一种过氧化氢酶和一种新的氧化还原酶。对氧化还原酶进行酶解，并通过电喷雾离子阱轨道阱质谱法（ESI - LTQ - Orbitrap MS）进行分析。质谱数据显示一种新型氧化还原酶（命名为BsPMO）含有224个氨基酸，与来自（CFA - 06）的一种假定蛋白有89%的同源性，以及一种含有491个氨基酸的过氧化氢酶（命名为BsCat），与来自（SAFR - 032）的过氧化氢酶有60%的相似性。新蛋白BsPMO含有铁原子，并且在存在辅因子（NADH、NADPH和NAD）的情况下对单加氧酶荧光探针具有催化活性。这项研究增进了我们对（该细菌）石油生物降解过程的了解。
