Characterization of 17β-estradiol-degrading enzyme from Microbacterium sp. MZT7 and its function on E2 biodegradation in wastewater

Abstract

Background 17β-estradiol (E2) residues exhibit harmful effects both for human and animals and have got global attention of the scientific community. Microbial enzymes are considered as one of the effective strategies having great potential for removal E2 residues from the environment. However, limited literature is available on the removal of E2 from wastewater using short-chain dehydrogenase. Results In this study, 17β-estradiol degrading enzyme (17β-HSD-0095) was expressed and purified from Microbacterium sp. MZT7. The optimal pH and temperature for reaction was 7 and 40 °C, respectively. Molecular docking studies have shown that the ARG215 residue form a hydrogen bond with oxygen atom of the substrate E2. Likewise, the point mutation results have revealed that the ARG215 residue play an important role in the E2 degradation by 17β-HSD-0095. In addition, 17β-HSD-0095 could remediate E2 contamination in synthetic livestock wastewater. Conclusions These findings offer some fresh perspectives on the molecular process of E2 degradation and the creation of enzyme preparations that can degrade E2. Graphical Abstract

Transcriptomics and metabolomics of blood, urine and ovarian follicular fluid of yak at induced estrus stage

“…Therefore, the transcription levels of the family genes would affect the mating behavior of animals. These family genes are linked to estradiol 17β-dehydrogenase, and these specific substances play a crucial role in the estrous behavior of female animals.Estradiol 17β-dehydrogenase is an enzyme that catalyzes the chemical reaction that converts estradiol-17β and NAD(P) + to ketone and NAD(P)H + H + [ 88 ]. During the estrous cycle of animals, estrogens (such as estradiol) play an important role, affecting sexual behavior and the development of reproductive organs [ 89 , 90 ].…”