Enzyme and Microbial Technology 2012-12-10

A protein from Pleurotus eryngii var. tuoliensis C.J. Mou with strong removal activity against the natural steroid hormone, estriol: purification, characterization, and identification as a laccase.

Mitsuhiro Ueda, Kayo Shintani, Akiko Nakanishi-Anjyuin, Masami Nakazawa, Mizuho Kusuda, Fumiki Nakatani, Takashi Kawaguchi, Sho-Ichi Tsujiyama, Masanobu Kawanishi, Takashi Yagi, Kazutaka Miyatake

Index: Enzyme Microb. Technol. 51(6-7) , 402-7, (2012)

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Abstract

A protein with strong removal activity against the natural estrogen estriol was purified from a culture supernatant of Pleurotus eryngii var. tuoliensis C.J. Mou. The protein was characterized as a laccase and had a molecular mass of 60kDa on SDS-PAGE. The enzyme was most active at pH 7.0 and 50°C. The partial N-terminal amino acid sequence of the enzyme showed homology with laccases from mushrooms, such as Pleurotus ostreatus, Coriolus versicolor (current name: Trametes versicolor), Pycnoporus cinnabarinus, and P. eryngii. A recombinant yeast assay confirmed that laccase treatment was very efficient for removing the estrogenic activity of steroid estrogens. Our results suggest that the enzyme may be applicable as a potential factor for removing natural steroid hormones.Copyright © 2012 Elsevier Inc. All rights reserved.

Related Compounds

  • Estriol
  • 17-Epiestriol

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