Transformation of 17β-estradiol to estrone by unknown wild-type enzyme in commercial arylsulfatase from Helix pomatia.

Autor: Zhang J; School of Environment and Energy, South China University of Technology, Guangzhou 510006, Guangdong, China., Liu ZH; School of Environment and Energy, South China University of Technology, Guangzhou 510006, Guangdong, China; Key Lab Pollution Control & Ecosystem Restoration in Industry Cluster, Ministry of Education, Guangzhou 510006, Guangdong, China; Guangdong Provincial Key Laboratory of Solid Wastes Pollution Control and Recycling, Guangzhou 510006, Guangdong, China; Guangdong Provincial Engineering and Technology Research Center for Environment Risk Prevention and Emergency Disposal, South China University of Technology, Guangzhou 510006, Guangdong, China. Electronic address: zehualiu@scut.edu.cn., Zhao KM; School of Environment and Energy, South China University of Technology, Guangzhou 510006, Guangdong, China., Dang Z; Key Lab Pollution Control & Ecosystem Restoration in Industry Cluster, Ministry of Education, Guangzhou 510006, Guangdong, China., Liu Y; South China Institute of Environmental Sciences, Ministry of Ecology and Environment of the People's Republic of China, Guangzhou 510655, China., Liu Y; Engineering Laboratory of Low-Carbon Unconventional Water Resources Utilization and Water Quality Assurance, College of Environmental Science and Engineering, Nankai University, Tianjin 300350, China.
Jazyk: angličtina
Zdroj: Journal of chromatography. B, Analytical technologies in the biomedical and life sciences [J Chromatogr B Analyt Technol Biomed Life Sci] 2024 Oct 01; Vol. 1246, pp. 124293. Date of Electronic Publication: 2024 Aug 31.
DOI: 10.1016/j.jchromb.2024.124293
Abstrakt: This work for the first time reported the complete transformation of 17β-estradiol (E2) to estrone (E1) by unknown wild-type enzyme present in the widely used commercial arylsulfatase derived from Helix pomatia. It was found that acetate could effectively inhibit the unknown enzyme with a half inhibitory concentration (IC 50 ) of 140.9 μM, while phosphate and citrate showed no inhibition. Since the buffer solutions with phosphate and citrate have been used in the enzymatic hydrolysis of natural estrogen conjugates for decades, the transformation of E2 to E1 likely occurred during such procedure, inevitably leading to overestimated E1, but underestimated E2. It was further suggested that acetate should be used to prevent this undesirable transformation during the enzymatic hydrolysis of natural estrogen conjugates.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
Externí odkaz: