Synergistic action of Acinetobacter baumannii and Talaromyces sp.: Function of enzymes in crude oil degradation

化学 双加氧酶 单加氧酶 生物化学 细胞外 十六烷 儿茶酚 生物修复 微生物学 细菌 生物 有机化学 细胞色素P450 遗传学
作者
Xiaoyan Liu,Zongze Chen,Dewen Kong,Xinying Zhang,Chuanhua Wang,Yongqi Wang
出处
期刊:Biochemical Engineering Journal [Elsevier BV]
卷期号:201: 109144-109144 被引量:2
标识
DOI:10.1016/j.bej.2023.109144
摘要

The purpose of this study was to explore the role of intracellular and extracellular enzymes of Acinetobacter baumannii and Talaromyces sp. in the synergistic degradation of crude oil. The extracellular enzymes of Talaromyces sp. contributed more to the degradation of n-alkanes. The degradation rate of n-hexadecane by extracellular enzymes of Talaromyces sp. was 71.83% after 5 days. The concentration of n-hexadecane decreased from 7700 mg/L to 2169 mg/L. This is related to the high extracellular expression of methane monooxygenase (particulate) and aldehyde dehydrogenase (NAD+) in Talaromyces sp. The extracellular enzymes of Acinetobacter baumannii had a better effect on the degradation of aromatic hydrocarbons. The degradation rate of xylene by extracellular enzymes of Acinetobacter baumannii was 35.65% after 5 days. The concentration of xylene decreased from 8600 mg/L to 5514 mg/L. Catechol 1,2-dioxygenase plays a key role in this process. Meanwhile, the degradation enzyme systems of Acinetobacter baumannii (long-chain alkane monooxygenase, alkane 1-monooxygenase, catechol 1,2-dioxygenase, salicylate hydroxylase, and benzoate 1,2-dioxygenase) and Talaromyces sp. (methane monooxygenase (particulate), benzaldehyde dehydrogenase (NAD+), catechol 2,3-dioxygenase, and gentisate 1,2-dioxygenase) complement each other in the degradation process of n-alkanes and aromatic hydrocarbons, thus improving the degradation ability. These results indicated that bacteria and fungi rely on the difference of degrading enzymes to achieve synergistic degradation.
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