Purification and Characterization of a Novel β‑Cypermethrin-Degrading Aminopeptidase from Pseudomonas aeruginosa GF31
In this study, a novel β-cypermethrin-degrading enzyme was isolated and purified by 32.8 fold from the extracellular cell-free filtrate of Pseudomonas aeruginosa GF31with the protein recovery of 26.6%. The molecular mass of the enzyme was determined to be 53 kDa. The optimum temperature for the acti...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2017-11, Vol.65 (43), p.9412-9418 |
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| container_issue | 43 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Tang, Ai-Xing Liu, Hu Liu, You-Yan Li, Qing-Yun Qing, Yi-Ming |
| description | In this study, a novel β-cypermethrin-degrading enzyme was isolated and purified by 32.8 fold from the extracellular cell-free filtrate of Pseudomonas aeruginosa GF31with the protein recovery of 26.6%. The molecular mass of the enzyme was determined to be 53 kDa. The optimum temperature for the activity was surprisingly 60 °C, and moreover, the purified enzyme showed a good pH stability, maintaining over 85% of its initial activity in the pH 5.0–9.0 range. Most of the common metal ions exhibited little influence on the activity except for Hg2+, Ag+, and Cu2+. After the complete gene sequence of the degrading enzyme was obtained by subcloning, sequence analyses as well as enzymatic properties demonstrated that the islolated enzyme should be an aminopeptidase. This is the first reported aminopeptidase for pyrethroid hydrolase, providing new potential enzyme resources for the degradation of this type of pesticide. |
| doi_str_mv | 10.1021/acs.jafc.7b03288 |
| format | Article |
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Agric. Food Chem</addtitle><description>In this study, a novel β-cypermethrin-degrading enzyme was isolated and purified by 32.8 fold from the extracellular cell-free filtrate of Pseudomonas aeruginosa GF31with the protein recovery of 26.6%. The molecular mass of the enzyme was determined to be 53 kDa. The optimum temperature for the activity was surprisingly 60 °C, and moreover, the purified enzyme showed a good pH stability, maintaining over 85% of its initial activity in the pH 5.0–9.0 range. Most of the common metal ions exhibited little influence on the activity except for Hg2+, Ag+, and Cu2+. After the complete gene sequence of the degrading enzyme was obtained by subcloning, sequence analyses as well as enzymatic properties demonstrated that the islolated enzyme should be an aminopeptidase. This is the first reported aminopeptidase for pyrethroid hydrolase, providing new potential enzyme resources for the degradation of this type of pesticide.</description><subject>Aminopeptidases - chemistry</subject><subject>Aminopeptidases - genetics</subject><subject>Aminopeptidases - isolation & purification</subject><subject>Aminopeptidases - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biocatalysis</subject><subject>Enzyme Stability</subject><subject>Hydrogen-Ion Concentration</subject><subject>Molecular Weight</subject><subject>Pseudomonas aeruginosa - chemistry</subject><subject>Pseudomonas aeruginosa - enzymology</subject><subject>Pseudomonas aeruginosa - genetics</subject><subject>Pyrethrins - chemistry</subject><subject>Pyrethrins - metabolism</subject><subject>Substrate Specificity</subject><subject>Temperature</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kLFOwzAURS0EoqWwMyGPDKTYSe0kY1VoQaqgA8zRS_LSumriYCeIMvEL_AofwkfwJbi0sCEPT7LOvdI9hJxy1ufM55eQ2f4Siqwfpizwo2iPdLnwmSc4j_ZJlznGi4TkHXJk7ZIxFomQHZKOH7NAsAHvkpdZa1ShMmiUrihUOR0twEDWoFGv209dUKB3-hlX9PPj6-19tK7RlNgsjKq8K5wbyFU1p8NSVbrGulE5WKSF0SWdWWxzXeoKLAU07dwhFuhkHPBjclDAyuLJ7vbI4_j6YXTjTe8nt6Ph1IMgkI3nh4NIAmS-DDCWvsxl5kalsYhiGUAopOCDlAPkAtwoxkXq8NiFuHshQtAj59ve2uinFm2TlMpmuFpBhbq1CY8Fdy0u6VC2RTOjrTVYJLVRJZh1wlmy8Z0438nGd7Lz7SJnu_Y2LTH_C_wKdsDFFviJ6tZUbuz_fd9NOo3x</recordid><startdate>20171101</startdate><enddate>20171101</enddate><creator>Tang, Ai-Xing</creator><creator>Liu, Hu</creator><creator>Liu, You-Yan</creator><creator>Li, Qing-Yun</creator><creator>Qing, Yi-Ming</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0003-4459-7841</orcidid></search><sort><creationdate>20171101</creationdate><title>Purification and Characterization of a Novel β‑Cypermethrin-Degrading Aminopeptidase from Pseudomonas aeruginosa GF31</title><author>Tang, Ai-Xing ; Liu, Hu ; Liu, You-Yan ; Li, Qing-Yun ; Qing, Yi-Ming</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a336t-27486aac263e9626d6c021b958963a756514b1aad5a290015b86a974818187ea3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Aminopeptidases - chemistry</topic><topic>Aminopeptidases - genetics</topic><topic>Aminopeptidases - isolation & purification</topic><topic>Aminopeptidases - metabolism</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biocatalysis</topic><topic>Enzyme Stability</topic><topic>Hydrogen-Ion Concentration</topic><topic>Molecular Weight</topic><topic>Pseudomonas aeruginosa - chemistry</topic><topic>Pseudomonas aeruginosa - enzymology</topic><topic>Pseudomonas aeruginosa - genetics</topic><topic>Pyrethrins - chemistry</topic><topic>Pyrethrins - metabolism</topic><topic>Substrate Specificity</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tang, Ai-Xing</creatorcontrib><creatorcontrib>Liu, Hu</creatorcontrib><creatorcontrib>Liu, You-Yan</creatorcontrib><creatorcontrib>Li, Qing-Yun</creatorcontrib><creatorcontrib>Qing, Yi-Ming</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tang, Ai-Xing</au><au>Liu, Hu</au><au>Liu, You-Yan</au><au>Li, Qing-Yun</au><au>Qing, Yi-Ming</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Characterization of a Novel β‑Cypermethrin-Degrading Aminopeptidase from Pseudomonas aeruginosa GF31</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2017-11-01</date><risdate>2017</risdate><volume>65</volume><issue>43</issue><spage>9412</spage><epage>9418</epage><pages>9412-9418</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><abstract>In this study, a novel β-cypermethrin-degrading enzyme was isolated and purified by 32.8 fold from the extracellular cell-free filtrate of Pseudomonas aeruginosa GF31with the protein recovery of 26.6%. The molecular mass of the enzyme was determined to be 53 kDa. The optimum temperature for the activity was surprisingly 60 °C, and moreover, the purified enzyme showed a good pH stability, maintaining over 85% of its initial activity in the pH 5.0–9.0 range. Most of the common metal ions exhibited little influence on the activity except for Hg2+, Ag+, and Cu2+. After the complete gene sequence of the degrading enzyme was obtained by subcloning, sequence analyses as well as enzymatic properties demonstrated that the islolated enzyme should be an aminopeptidase. This is the first reported aminopeptidase for pyrethroid hydrolase, providing new potential enzyme resources for the degradation of this type of pesticide.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>29035041</pmid><doi>10.1021/acs.jafc.7b03288</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0003-4459-7841</orcidid></addata></record> |
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| ispartof | Journal of agricultural and food chemistry, 2017-11, Vol.65 (43), p.9412-9418 |
| issn | 0021-8561 1520-5118 |
| language | eng |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Aminopeptidases - chemistry Aminopeptidases - genetics Aminopeptidases - isolation & purification Aminopeptidases - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Biocatalysis Enzyme Stability Hydrogen-Ion Concentration Molecular Weight Pseudomonas aeruginosa - chemistry Pseudomonas aeruginosa - enzymology Pseudomonas aeruginosa - genetics Pyrethrins - chemistry Pyrethrins - metabolism Substrate Specificity Temperature |
| title | Purification and Characterization of a Novel β‑Cypermethrin-Degrading Aminopeptidase from Pseudomonas aeruginosa GF31 |
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