A Mono-2-Ethylhexyl Phthalate Hydrolase from a Gordonia sp. That Is Able To Dissimilate Di-2-Ethylhexyl Phthalate-Reference-Cited by-同舟云学术

A Mono-2-Ethylhexyl Phthalate Hydrolase from a Gordonia sp. That Is Able To Dissimilate Di-2-Ethylhexyl Phthalate

Published:2006-04 Issue:4 Volume:72 Page:2394-2399
ISSN:0099-2240
Container-title:Applied and Environmental Microbiology
language:en
Short-container-title:Appl Environ Microbiol

Author:

Nishioka Tuguhiro¹,Iwata Makoto²,Imaoka Takuya¹,Mutoh Maiko¹,Egashira Yoshihiro¹,Nishiyama Takashi¹,Shin Takashi³,Fujii Takao¹

Affiliation:

1. Departments of Applied Life Science

2. IMB Co., Ltd., Ooaza Hitotugi 1070-10, Amagi City, Fukuoka 838-0065, Japan

3. Applied Microbial Technology, Faculty of Biotechnology and Life Science, Sojo University, 4-22-1 Ikeda, Kumamoto 860-0082, Japan

Abstract

ABSTRACT Gordonia sp. strain P8219, a strain able to decompose di-2-ethylhexyl phthalate, was isolated from machine oil-contaminated soil. Mono-2-ethylhexyl phthalate hydrolase was purified from cell extracts of this strain. This enzyme was a 32,164-Da homodimeric protein, and it effectively hydrolyzed monophthalate esters, such as monoethyl, monobutyl, monohexyl, and mono-2-ethylhexyl phthalate. The K m and V max values for mono-2-ethylhexyl phthalate were 26.9 ± 4.3 μM and 18.1 ± 0.9 μmol/min · mg protein, respectively. The deduced amino acid sequence of the enzyme exhibited less than 30% homology with those of meta -cleavage hydrolases which are serine hydrolases but exhibited no significant homology with the sequences of serine esterases. The pentapeptide motif GXSXG, which is conserved in serine hydrolases, was present in the sequence. The enzymatic properties and features of the primary structure suggested that this enzyme is a novel enzyme belonging to an independent group of serine hydrolases.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Link

https://journals.asm.org/doi/pdf/10.1128/AEM.72.4.2394-2399.2006

Reference37 articles.

1. Ahmad, D., J. Fraser, M. Sylvestre, A. Larose, A. Khan, J. Bergeron, J. M. Juteau, and M. Sondossi. 1995. Sequence of the bphD gene encoding 2-hydroxy-6-oxo-(phenyl/chlorophenyl)hexa-2,4-dienoic acid (HOP/cPDA) hydrolase involved in the biphenyl/polychlorinated biphenyl degradation pathway in Comamonas testosteroni: evidence suggesting involvement of Ser112 in catalytic activity. Gene156:69-74.

2. Akita, K., C. Naitou, and K. Maruyama. 2001. Purification and characterization of an esterase from Micrococcus sp. YGJ1 hydrolyzing phthalate esters. Biosci. Biotechnol. Biochem.65:1680-1683.

3. Aleshchenkova, Z. M., A. S. Samsonova, S. V. Baikova, and T. A. Kukulianskaia. 1996. The degradation of plasticizers by Rhodococcus erythropolis 40F. Mikrobiol. Z.58:34-38.

4. Barber, E. D., and D. C. Topping. 1995. Subchronic 90-day oral toxicology of di(2-ethylhexyl) terephthalate in the rat. Food Chem. Toxicol.33:971-978.

5. Blom, A., E. Ekman, A. Johannisson, L. Norrgren, and M. Pesonen. 1998. Effects of xenoestrogenic environmental pollutants on the proliferation of a human breast cancer cell line (MCF-7). Arch. Environ. Contam. Toxicol.34:306-310.

Cited by 83 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Unveiling Mechanistic and Structural Insights of EstS1 Esterase: A Potent Broad-Spectrum Phthalate Diester Degrading Enzyme;2024-08-14

2. Genomic, Phylogenetic and Physiological Characterization of the PAH-Degrading Strain Gordonia polyisoprenivorans 135;Biology;2024-05-13

3. Biodegradation of DEP, DIBP, and BBP by a psychrotolerant Sphingobium yanoikuyae strain P4: Degradation potentiality and mechanism study;Archives of Microbiology;2024-05-10

4. Enzymatic depolymerization of plastic materials by a highly efficient two-enzyme system;Biochemical Engineering Journal;2024-04

5. A novel and efficient strategy for the biodegradation of di(2-ethylhexyl) phthalate by Fusarium culmorum;Applied Microbiology and Biotechnology;2024-01-11