Promotion of Activity and Thermal Stability of Chloroperoxidase by Trace Amount of Metal Ions (M²⁺/M ³⁺)
The effect of M²⁺ (Zn²⁺, Cu²⁺, Cd²⁺, Mn²⁺, Pb²⁺) and M³⁺ (Cr³⁺, La³⁺, Fe³⁺, Ce³⁺, Y³⁺, Al³⁺) metal ions on the activity and thermal stability of chloroperoxidase (CPO) was investigated in this work. It was found that the lower concentration of metal ions was favorable to CPO activity whereas the hig...
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| Veröffentlicht in: | Applied biochemistry and biotechnology 2014-03, Vol.172 (5), p.2338-2347 |
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| container_title | Applied biochemistry and biotechnology |
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| creator | Li, Haiyun Gao, Jinwei Wang, Limin Li, Xiaohong Jiang, Yucheng Hu, Mancheng Li, Shuni Zhai, Quanguo |
| description | The effect of M²⁺ (Zn²⁺, Cu²⁺, Cd²⁺, Mn²⁺, Pb²⁺) and M³⁺ (Cr³⁺, La³⁺, Fe³⁺, Ce³⁺, Y³⁺, Al³⁺) metal ions on the activity and thermal stability of chloroperoxidase (CPO) was investigated in this work. It was found that the lower concentration of metal ions was favorable to CPO activity whereas the higher concentration reversed the results. CPO activity could be increased to 116.4–127.1 % in the presence of a trace amount of these M²⁺/M³⁺ metal ions at a concentration range of 0–25 μmol L⁻¹ after 2 h of incubation at 25 °C. The activating effect of M³⁺ is better than that of M²⁺, and Cr³⁺ was mostly efficient. The thermal stability of the enzyme was also improved significantly. Only 30.3 % of CPO activity was retained at 50 °C whereas 82.6 % of CPO activity was maintained in the presence of Cr³⁺ after 2 h of incubation at the same temperature. The activation of CPO by metal ions at their low concentration was studied through intrinsic fluorescence, circular dichroism (CD), and UV–Vis spectra assay. A favorable environment around the active site was achieved in the presence of metal ions. Intrinsic fluorescence and CD spectra indicated that the α-helix structure of CPO was strengthened in metal ion-contained media. More exposure of the heme ring was achieved for easy access of the substrate, which was suggested by UV–Vis spectrum analysis. This strategy for enhancing CPO activity is very simple and useful. It will be favorable to the practical application of this enzyme. |
| doi_str_mv | 10.1007/s12010-013-0677-1 |
| format | Article |
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It was found that the lower concentration of metal ions was favorable to CPO activity whereas the higher concentration reversed the results. CPO activity could be increased to 116.4–127.1 % in the presence of a trace amount of these M²⁺/M³⁺ metal ions at a concentration range of 0–25 μmol L⁻¹ after 2 h of incubation at 25 °C. The activating effect of M³⁺ is better than that of M²⁺, and Cr³⁺ was mostly efficient. The thermal stability of the enzyme was also improved significantly. Only 30.3 % of CPO activity was retained at 50 °C whereas 82.6 % of CPO activity was maintained in the presence of Cr³⁺ after 2 h of incubation at the same temperature. The activation of CPO by metal ions at their low concentration was studied through intrinsic fluorescence, circular dichroism (CD), and UV–Vis spectra assay. A favorable environment around the active site was achieved in the presence of metal ions. Intrinsic fluorescence and CD spectra indicated that the α-helix structure of CPO was strengthened in metal ion-contained media. More exposure of the heme ring was achieved for easy access of the substrate, which was suggested by UV–Vis spectrum analysis. This strategy for enhancing CPO activity is very simple and useful. It will be favorable to the practical application of this enzyme.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-013-0677-1</identifier><identifier>PMID: 24363219</identifier><identifier>CODEN: ABIBDL</identifier><language>eng</language><publisher>Boston: Springer-Verlag</publisher><subject>aluminum ; Biochemistry ; Biological and medical sciences ; Biotechnology ; cadmium ; Catalysis ; Catalytic Domain ; Cations ; Chemistry ; Chemistry and Materials Science ; Chloride Peroxidase - chemistry ; Chloride Peroxidase - isolation & purification ; chromium ; copper ; Enzyme Activation ; Enzyme Assays ; Enzyme Stability ; Enzymes ; Fluorescence ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - agonists ; Fungal Proteins - chemistry ; Fungal Proteins - isolation & purification ; heme ; Ions ; iron ; Kinetics ; lead ; manganese ; Metal concentrations ; Metal ions ; Metals ; Metals - chemistry ; Oxidation-Reduction ; Protein Structure, Secondary ; Saccharomycetales - chemistry ; Saccharomycetales - enzymology ; Temperature ; thermal stability ; zinc</subject><ispartof>Applied biochemistry and biotechnology, 2014-03, Vol.172 (5), p.2338-2347</ispartof><rights>Springer Science+Business Media New York 2013</rights><rights>2015 INIST-CNRS</rights><rights>Springer Science+Business Media New York 2014</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c463t-676f4f94429ba3c63d498e7d2c84df8747bae89d23efe522a0a9efc92c624e143</citedby><cites>FETCH-LOGICAL-c463t-676f4f94429ba3c63d498e7d2c84df8747bae89d23efe522a0a9efc92c624e143</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12010-013-0677-1$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-013-0677-1$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=28577994$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24363219$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Haiyun</creatorcontrib><creatorcontrib>Gao, Jinwei</creatorcontrib><creatorcontrib>Wang, Limin</creatorcontrib><creatorcontrib>Li, Xiaohong</creatorcontrib><creatorcontrib>Jiang, Yucheng</creatorcontrib><creatorcontrib>Hu, Mancheng</creatorcontrib><creatorcontrib>Li, Shuni</creatorcontrib><creatorcontrib>Zhai, Quanguo</creatorcontrib><title>Promotion of Activity and Thermal Stability of Chloroperoxidase by Trace Amount of Metal Ions (M²⁺/M ³⁺)</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>The effect of M²⁺ (Zn²⁺, Cu²⁺, Cd²⁺, Mn²⁺, Pb²⁺) and M³⁺ (Cr³⁺, La³⁺, Fe³⁺, Ce³⁺, Y³⁺, Al³⁺) metal ions on the activity and thermal stability of chloroperoxidase (CPO) was investigated in this work. It was found that the lower concentration of metal ions was favorable to CPO activity whereas the higher concentration reversed the results. CPO activity could be increased to 116.4–127.1 % in the presence of a trace amount of these M²⁺/M³⁺ metal ions at a concentration range of 0–25 μmol L⁻¹ after 2 h of incubation at 25 °C. The activating effect of M³⁺ is better than that of M²⁺, and Cr³⁺ was mostly efficient. The thermal stability of the enzyme was also improved significantly. Only 30.3 % of CPO activity was retained at 50 °C whereas 82.6 % of CPO activity was maintained in the presence of Cr³⁺ after 2 h of incubation at the same temperature. The activation of CPO by metal ions at their low concentration was studied through intrinsic fluorescence, circular dichroism (CD), and UV–Vis spectra assay. A favorable environment around the active site was achieved in the presence of metal ions. Intrinsic fluorescence and CD spectra indicated that the α-helix structure of CPO was strengthened in metal ion-contained media. More exposure of the heme ring was achieved for easy access of the substrate, which was suggested by UV–Vis spectrum analysis. This strategy for enhancing CPO activity is very simple and useful. It will be favorable to the practical application of this enzyme.</description><subject>aluminum</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>cadmium</subject><subject>Catalysis</subject><subject>Catalytic Domain</subject><subject>Cations</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chloride Peroxidase - chemistry</subject><subject>Chloride Peroxidase - isolation & purification</subject><subject>chromium</subject><subject>copper</subject><subject>Enzyme Activation</subject><subject>Enzyme Assays</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Fluorescence</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - agonists</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - isolation & purification</subject><subject>heme</subject><subject>Ions</subject><subject>iron</subject><subject>Kinetics</subject><subject>lead</subject><subject>manganese</subject><subject>Metal concentrations</subject><subject>Metal ions</subject><subject>Metals</subject><subject>Metals - chemistry</subject><subject>Oxidation-Reduction</subject><subject>Protein Structure, Secondary</subject><subject>Saccharomycetales - chemistry</subject><subject>Saccharomycetales - enzymology</subject><subject>Temperature</subject><subject>thermal stability</subject><subject>zinc</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kcFu1DAQhi0EokvhAbiApQqpHELtsRPHx9WqQKWuQOr2bDmO3aZK4sVOEHvsK8GNYx-FJ8FRtgVx4DSS5_v_Gc-P0EtK3lFCxEmkQCjJCGUZKYTI6CO0oHkuMwKSPkYLAoJlAKU8QM9ivCGEQpmLp-gAOCsYULlA_efgOz80vsfe4aUZmq_NsMO6r_Hm2oZOt_hi0FXTTq-JWF23PvitDf5bU-tocbXDm6CNxcvOj_0wMWs7JNmZ7yM-Xt99_3X782SN736k-vY5euJ0G-2LfT1El-9PN6uP2fmnD2er5XlmeMGGrBCF405yDrLSzBSs5rK0ogZT8tqVgotK21LWwKyzOYAmWlpnJJgCuKWcHaLj2Xcb_JfRxkF1TTS2bXVv_RgVzdMBJXAgCT36B73xY-jTdokikoqiEBNFZ8oEH2OwTm1D0-mwU5SoKQw1h6FSGGoKQ9GkebV3HqvO1g-K--sn4M0e0NHo1gXdmyb-4VJYQsrpNzBzMbX6Kxv-WvE_01_PIqe90lchGV9eJIgTQnKQRLLf8NqsYg</recordid><startdate>20140301</startdate><enddate>20140301</enddate><creator>Li, Haiyun</creator><creator>Gao, Jinwei</creator><creator>Wang, Limin</creator><creator>Li, Xiaohong</creator><creator>Jiang, Yucheng</creator><creator>Hu, Mancheng</creator><creator>Li, Shuni</creator><creator>Zhai, Quanguo</creator><general>Springer-Verlag</general><general>Springer US</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>IQODW</scope><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>3V.</scope><scope>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope></search><sort><creationdate>20140301</creationdate><title>Promotion of Activity and Thermal Stability of Chloroperoxidase by Trace Amount of Metal Ions (M²⁺/M ³⁺)</title><author>Li, Haiyun ; Gao, Jinwei ; Wang, Limin ; Li, Xiaohong ; Jiang, Yucheng ; Hu, Mancheng ; Li, Shuni ; Zhai, Quanguo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c463t-676f4f94429ba3c63d498e7d2c84df8747bae89d23efe522a0a9efc92c624e143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>aluminum</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>cadmium</topic><topic>Catalysis</topic><topic>Catalytic Domain</topic><topic>Cations</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chloride Peroxidase - chemistry</topic><topic>Chloride Peroxidase - isolation & purification</topic><topic>chromium</topic><topic>copper</topic><topic>Enzyme Activation</topic><topic>Enzyme Assays</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Fluorescence</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - agonists</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - isolation & purification</topic><topic>heme</topic><topic>Ions</topic><topic>iron</topic><topic>Kinetics</topic><topic>lead</topic><topic>manganese</topic><topic>Metal concentrations</topic><topic>Metal ions</topic><topic>Metals</topic><topic>Metals - chemistry</topic><topic>Oxidation-Reduction</topic><topic>Protein Structure, Secondary</topic><topic>Saccharomycetales - chemistry</topic><topic>Saccharomycetales - enzymology</topic><topic>Temperature</topic><topic>thermal stability</topic><topic>zinc</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Haiyun</creatorcontrib><creatorcontrib>Gao, Jinwei</creatorcontrib><creatorcontrib>Wang, Limin</creatorcontrib><creatorcontrib>Li, Xiaohong</creatorcontrib><creatorcontrib>Jiang, Yucheng</creatorcontrib><creatorcontrib>Hu, Mancheng</creatorcontrib><creatorcontrib>Li, Shuni</creatorcontrib><creatorcontrib>Zhai, Quanguo</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Applied biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Haiyun</au><au>Gao, Jinwei</au><au>Wang, Limin</au><au>Li, Xiaohong</au><au>Jiang, Yucheng</au><au>Hu, Mancheng</au><au>Li, Shuni</au><au>Zhai, Quanguo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Promotion of Activity and Thermal Stability of Chloroperoxidase by Trace Amount of Metal Ions (M²⁺/M ³⁺)</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><stitle>Appl Biochem Biotechnol</stitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2014-03-01</date><risdate>2014</risdate><volume>172</volume><issue>5</issue><spage>2338</spage><epage>2347</epage><pages>2338-2347</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><coden>ABIBDL</coden><abstract>The effect of M²⁺ (Zn²⁺, Cu²⁺, Cd²⁺, Mn²⁺, Pb²⁺) and M³⁺ (Cr³⁺, La³⁺, Fe³⁺, Ce³⁺, Y³⁺, Al³⁺) metal ions on the activity and thermal stability of chloroperoxidase (CPO) was investigated in this work. It was found that the lower concentration of metal ions was favorable to CPO activity whereas the higher concentration reversed the results. CPO activity could be increased to 116.4–127.1 % in the presence of a trace amount of these M²⁺/M³⁺ metal ions at a concentration range of 0–25 μmol L⁻¹ after 2 h of incubation at 25 °C. The activating effect of M³⁺ is better than that of M²⁺, and Cr³⁺ was mostly efficient. The thermal stability of the enzyme was also improved significantly. Only 30.3 % of CPO activity was retained at 50 °C whereas 82.6 % of CPO activity was maintained in the presence of Cr³⁺ after 2 h of incubation at the same temperature. The activation of CPO by metal ions at their low concentration was studied through intrinsic fluorescence, circular dichroism (CD), and UV–Vis spectra assay. A favorable environment around the active site was achieved in the presence of metal ions. Intrinsic fluorescence and CD spectra indicated that the α-helix structure of CPO was strengthened in metal ion-contained media. More exposure of the heme ring was achieved for easy access of the substrate, which was suggested by UV–Vis spectrum analysis. This strategy for enhancing CPO activity is very simple and useful. It will be favorable to the practical application of this enzyme.</abstract><cop>Boston</cop><pub>Springer-Verlag</pub><pmid>24363219</pmid><doi>10.1007/s12010-013-0677-1</doi><tpages>10</tpages></addata></record> |
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| ispartof | Applied biochemistry and biotechnology, 2014-03, Vol.172 (5), p.2338-2347 |
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| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | aluminum Biochemistry Biological and medical sciences Biotechnology cadmium Catalysis Catalytic Domain Cations Chemistry Chemistry and Materials Science Chloride Peroxidase - chemistry Chloride Peroxidase - isolation & purification chromium copper Enzyme Activation Enzyme Assays Enzyme Stability Enzymes Fluorescence Fundamental and applied biological sciences. Psychology Fungal Proteins - agonists Fungal Proteins - chemistry Fungal Proteins - isolation & purification heme Ions iron Kinetics lead manganese Metal concentrations Metal ions Metals Metals - chemistry Oxidation-Reduction Protein Structure, Secondary Saccharomycetales - chemistry Saccharomycetales - enzymology Temperature thermal stability zinc |
| title | Promotion of Activity and Thermal Stability of Chloroperoxidase by Trace Amount of Metal Ions (M²⁺/M ³⁺) |
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