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Study On Biodegradation Of Anthraquinone Compounds By Sphingomonas Xenophaga QYY And Rhodococcus Pyridinivorans GF3

Posted on:2015-10-23Degree:MasterType:Thesis
Country:ChinaCandidate:X F GuanFull Text:PDF
GTID:2181330467486283Subject:Environmental Engineering
Abstract/Summary:PDF Full Text Request
Bacteria, which have been isolated, can only slowly degrade several anthraquinone compounds. Moreover, the degradation products of these anthraquinone compounds are easily auto-oxidized under aerobic conditions. In the present study, the effects of additional nutrients on anthraquinone compounds degradation by Sphingomonas xenophaga QYY and accelerating mechanism were studied. Meanwhile, a novel bacterium capable of degrading several anthraquinone compounds was isolated. The growth characteristics of the isolated Rhodococcus pyridinivorans GF3, its ability to degrade anthraquinone compounds and1-aminoanthraquinone-2-sulfonic acid (ASA-2) degradation pathway were investigated.Nutrients amendment could enhance the bio-decolorization of ASA-2and1-amino-4-bromoanthraquinone-2-sulfonic acid (ABSA) by strain QYY. Yeast extract and peptone increased the bio-decolorization rates of ASA-2and ABSA. Glucose, fructose, sucrose and casamino acids could promote ASA-2and ABSA bio-decolorization. Among these nutrients,glucose showed the most significant influence on ASA-2and ABSA decolorization, with76.7%and50.8%increases, respectively. Additional urea, ammonium nitrate and vitamins did not promote the bio-decolorization of the two anthraquinone compounds. Further studies found that L-leucine, L-glutamic acid, L-proline L-cystine, L-aspartate and L-phenylalanine could accelerate ASA-2and ABSA bio-decolorization. Especially, in the presence of L-proline, the decolorization efficiencies of ASA-2and ABSA increased79.9%and67.3%, respectively. Crude enzymes from celll extracts were obtained by sonication and ultracentrifugation, then used for studying the relationship between the decolorization enzyme(s) activities and L-proline. The experiments showed that ASA-2and ABSA decolorization enzyme(s) was located in cellular membranes. Instead of NADH, L-proline could be directly invovled in ASA-2and ABSA decolorization by cellular membranes.A new strain GF3capable of degrading anthraquinone compounds was isolated under aerobic conditions. The16S rDNA sequence of strain GF3shared100%similarity with Rhodococcus pyridinivorans NR025033and KF38149. The16S rDNA sequence of strain GF3was submitted to GenBank with the number KF953541.The characteristics of strain GF3growth and ASA-2bio-decolorization were investigated and the cleavage process of anthraquinone ring was analyzed. The optimal conditions for strain GF3growth and ASA-2bio-decolorization process were as follows:pH=7.0,30℃ and150r/min.. Additional yeast extract as an carbon source could significantly enhance the growth of strain GF3and ASA-2bio-decolorization. Additional nitrogen sources could promote ASA-2decolorization in different levels. Among these nitrogen sources, urea and ammonium nitrate showed the most significant influence on ASA-2bio-decolorization, with49.1%and47.1%increases, respectively. Among the tested trace elements, ferric trichloride could accelerate ASA-2bio-decolorization with7.4%increase. Strain GF3can degrade not only ASA-2, but also other anthraquinone compounds including ABSA, anthraquinone-2-carboxylic acid and anthraquinone-2-sulfonic acid. However, strain GF3can not degrade anthraquinone-2,6-disulfonic acid. Additionally, during ASA-2bio-decolorization, the removal percentage of TOC reached60.6%, indicating the cleavage of the anthraquinone ring of ASA-2. HPLC-MASS spectra analysis showed that the main decolorization products were proposed to be2-amino-3-carboxyl benzenesulfonic acid and2-amino-4-carboxyl benzenesulfonic acid.
Keywords/Search Tags:Anthraquinones, Sphingomonas xenophaga QYY, Rhodococcuspyridinivorans GF3, Decolorization
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