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Functional protein capable of degrading chrysene

A protein and functional technology, applied in the field of bioengineering technology and biological treatment of refractory organic pollutants, can solve the problems of lack of research reports on high-ring polycyclic aromatic hydrocarbon functional proteins, lack of research on polycyclic aromatic hydrocarbon degrading microorganisms, etc.

Inactive Publication Date: 2015-06-03
BEIJING NORMAL UNIVERSITY
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  • Abstract
  • Description
  • Claims
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Problems solved by technology

However, due to the lack of in-depth research on PAH-degrading microorganisms, there is a lack of research reports on high-ring PAH functional proteins at home and abroad.

Method used

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  • Functional protein capable of degrading chrysene

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Experimental program
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Effect test

Embodiment

[0027] Inoculate the bacterial strain Ochrobactrum anthropi DW1 preserved in the General Microbiology Center of China Microbiological Culture Collection Management Committee into the culture bottle that has added 198ml induction medium, 2.0ml trace metal liquid and 0.2ml vitamin c solution, then put the culture bottle in The culture temperature is 25-28° C., and the rotation speed is 100 r / min, and the shaker is cultured for 40 days to obtain the bacteria liquid after amplification culture.

[0028] The obtained bacterial solution was ultrasonically disrupted for 15 minutes and then centrifuged at 8000 r / min for 15 minutes to separate the bacterial cells and supernatant. Add 30 ml of deionized water to the isolated cells, continue ultrasonication for 15 min, centrifuge at 8000 r / min for 15 min, separate the cells and supernatant, and repeat twice. The supernatants collected three times were combined to obtain crude functional protein extracts.

[0029] Add finely ground (NH ...

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Abstract

The invention provides functional protein capable of degrading chrysene. The functional protein capable of catalyzing and degrading the chrysene is obtained by extracting and purifying a bacterium liquid of Ochrobactrum anthropic DW1 with the strain preservation number of CGMCC NO.8621. When the functional protein catalyzes and degrades the chrysene, the proper pH value ranges from 6.0 to 8.0, the most proper pH value is 7.0, the functional protein can be deactivated and denaturized easily when the pH value is smaller than 4 or larger than 10, the proper reaction temperature ranges from 30 DEG C to 45 DEG C, the most proper reaction temperature is 35 DEG C, the functional protein can be deactivated and denaturized easily when the temperature is higher than 50 DEG C, and Cu<2+>, Ni<2+> and Hg<2+> ions with the concentration of 1 mmol / L have stronger inhibition effects on the activity of the functional protein. The functional protein can effectively catalyze and degrade the chrysene and has the application potential for soil and water polluted by the polycyclic aromatic hydrocarbon chrysene.

Description

technical field [0001] The invention belongs to the technical field of bioengineering technology and biological treatment of refractory organic pollutants, in particular to a biodegradable functional protein. Background technique [0002] Polycyclic aromatic hydrocarbons (Polycyclic Aromatic Hydrocarbons, PAHs) are a class of toxic organic pollutants containing two or more benzene rings, which have strong carcinogenic, teratogenic and mutagenic effects. PAHs can cause great harm to the ecological environment and human health through bioaccumulation and food chain transmission, which has attracted great attention from environmental scientists in various countries. As early as the 1980s, the U.S. Environmental Protection Agency identified 16 unbranched PAHs as priority pollutants in the environment, and my country also included PAHs in the blacklist of environmental pollution. [0003] At present, the treatment technologies for polycyclic aromatic hydrocarbons in the enviro...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C12N9/00C12R1/01
CPCC07K14/195
Inventor 朱宜袁静谢恩郑蕾丁爱中豆俊峰
Owner BEIJING NORMAL UNIVERSITY
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