Purification and characterization of agarases from a marine bacterium Vibrio sp. F-6
Marine bacterium Vibrio sp. F-6, utilizing agarose as a carbon source to produce agarases, was isolated from seawater samples taken from Qingdao, China. Two agarases (AG-a and AG-b) were purified to a homogeneity from the cultural supernatant of Vibrio sp. F-6 through ammonium sulfate precipitation,...
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| Veröffentlicht in: | Journal of industrial microbiology & biotechnology 2008-08, Vol.35 (8), p.915-922 |
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| creator | Fu, Wandong Han, Baoqin Duan, Delin Liu, Wanshun Wang, Changhong |
| description | Marine bacterium Vibrio sp. F-6, utilizing agarose as a carbon source to produce agarases, was isolated from seawater samples taken from Qingdao, China. Two agarases (AG-a and AG-b) were purified to a homogeneity from the cultural supernatant of Vibrio sp. F-6 through ammonium sulfate precipitation, Q-Sepharose FF chromatography, and Sephacryl S-100 gel filtration. Molecular weights of agarases were estimated to be 54.0 kDa (AG-a) and 34.5 kDa (AG-b) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimum pH values for AG-a and AG-b were about 7.0 and 9.0, respectively. AG-a was stable in the pH range of 4.0-9.0 and AG-b was stable in the pH range of 4.0-10.0. The optimum temperatures of AG-a and AG-b were 40 and 55 °C, respectively. AG-a was stable at temperature below 50 °C. AG-b was stable at temperature below 60 °C. Zn²⁺, Mg²⁺ or Ca²⁺ increased AG-a activity, while Mn²⁺, Cu²⁺ or Ca²⁺ increased AG-b activity. However, Ag⁺, Hg²⁺, Fe³⁺, EDTA and SDS inhibited AG-a and AG-b activities. The main hydrolysates of agarose by AG-a were neoagarotetraose and neoagarohexaose. The main hydrolysates of agarose by AG-b were neoagarooctaose and neoagarohexaose. When the mixture of AG-a and AG-b were used, agarose was mainly degraded into neoagarobiose. |
| doi_str_mv | 10.1007/s10295-008-0365-2 |
| format | Article |
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F-6</title><source>Oxford Journals Open Access Collection</source><source>MEDLINE</source><source>SpringerLink Journals</source><creator>Fu, Wandong ; Han, Baoqin ; Duan, Delin ; Liu, Wanshun ; Wang, Changhong</creator><creatorcontrib>Fu, Wandong ; Han, Baoqin ; Duan, Delin ; Liu, Wanshun ; Wang, Changhong</creatorcontrib><description>Marine bacterium Vibrio sp. F-6, utilizing agarose as a carbon source to produce agarases, was isolated from seawater samples taken from Qingdao, China. Two agarases (AG-a and AG-b) were purified to a homogeneity from the cultural supernatant of Vibrio sp. F-6 through ammonium sulfate precipitation, Q-Sepharose FF chromatography, and Sephacryl S-100 gel filtration. Molecular weights of agarases were estimated to be 54.0 kDa (AG-a) and 34.5 kDa (AG-b) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimum pH values for AG-a and AG-b were about 7.0 and 9.0, respectively. AG-a was stable in the pH range of 4.0-9.0 and AG-b was stable in the pH range of 4.0-10.0. The optimum temperatures of AG-a and AG-b were 40 and 55 °C, respectively. AG-a was stable at temperature below 50 °C. AG-b was stable at temperature below 60 °C. Zn²⁺, Mg²⁺ or Ca²⁺ increased AG-a activity, while Mn²⁺, Cu²⁺ or Ca²⁺ increased AG-b activity. However, Ag⁺, Hg²⁺, Fe³⁺, EDTA and SDS inhibited AG-a and AG-b activities. The main hydrolysates of agarose by AG-a were neoagarotetraose and neoagarohexaose. The main hydrolysates of agarose by AG-b were neoagarooctaose and neoagarohexaose. When the mixture of AG-a and AG-b were used, agarose was mainly degraded into neoagarobiose.</description><identifier>ISSN: 1367-5435</identifier><identifier>EISSN: 1476-5535</identifier><identifier>DOI: 10.1007/s10295-008-0365-2</identifier><identifier>PMID: 18478285</identifier><language>eng</language><publisher>Berlin/Heidelberg: Berlin/Heidelberg : Springer-Verlag</publisher><subject>Ammonium ; Ammonium Sulfate ; Bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - isolation & purification ; Bacterial Proteins - metabolism ; Biochemistry ; Bioinformatics ; Biological and medical sciences ; Biomedical and Life Sciences ; Biotechnology ; Carbon - metabolism ; Carbon sources ; Cations, Divalent - pharmacology ; Chemical analysis ; Chemical Fractionation ; China ; Chromatography ; Chromatography, Gel ; Chromatography, Ion Exchange ; Culture Media - chemistry ; Edetic Acid - pharmacology ; Electrophoresis, Polyacrylamide Gel ; Enzyme Activators - pharmacology ; Enzyme Inhibitors - pharmacology ; Enzyme Stability ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Galactosides - metabolism ; Genetic Engineering ; Glycoside Hydrolases - chemistry ; Glycoside Hydrolases - isolation & purification ; Glycoside Hydrolases - metabolism ; Hydrogen-Ion Concentration ; Inorganic Chemistry ; Life Sciences ; Marine biology ; Metals - pharmacology ; Microbiology ; Molecular Weight ; Oligosaccharides - metabolism ; Original Paper ; Phylogeny ; Proteins ; RNA, Ribosomal, 16S - genetics ; Seawater ; Seawater - microbiology ; Sepharose - metabolism ; Sequence Analysis, DNA ; Sodium Dodecyl Sulfate - pharmacology ; Studies ; Sulfates ; Temperature ; Vibrio - classification ; Vibrio - enzymology ; Vibrio - isolation & purification ; Water analysis</subject><ispartof>Journal of industrial microbiology & biotechnology, 2008-08, Vol.35 (8), p.915-922</ispartof><rights>Society for Industrial Microbiology 2008 2008</rights><rights>Society for Industrial Microbiology 2008</rights><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-289f7e2d0660448ee2995be5e1b71e66b8640e3fa67259fde78d451a077e63a93</citedby><cites>FETCH-LOGICAL-c526t-289f7e2d0660448ee2995be5e1b71e66b8640e3fa67259fde78d451a077e63a93</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/s10295-008-0365-2$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10295-008-0365-2$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20540513$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18478285$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fu, Wandong</creatorcontrib><creatorcontrib>Han, Baoqin</creatorcontrib><creatorcontrib>Duan, Delin</creatorcontrib><creatorcontrib>Liu, Wanshun</creatorcontrib><creatorcontrib>Wang, Changhong</creatorcontrib><title>Purification and characterization of agarases from a marine bacterium Vibrio sp. F-6</title><title>Journal of industrial microbiology & biotechnology</title><addtitle>J Ind Microbiol Biotechnol</addtitle><addtitle>J Ind Microbiol Biotechnol</addtitle><description>Marine bacterium Vibrio sp. F-6, utilizing agarose as a carbon source to produce agarases, was isolated from seawater samples taken from Qingdao, China. Two agarases (AG-a and AG-b) were purified to a homogeneity from the cultural supernatant of Vibrio sp. F-6 through ammonium sulfate precipitation, Q-Sepharose FF chromatography, and Sephacryl S-100 gel filtration. Molecular weights of agarases were estimated to be 54.0 kDa (AG-a) and 34.5 kDa (AG-b) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimum pH values for AG-a and AG-b were about 7.0 and 9.0, respectively. AG-a was stable in the pH range of 4.0-9.0 and AG-b was stable in the pH range of 4.0-10.0. The optimum temperatures of AG-a and AG-b were 40 and 55 °C, respectively. AG-a was stable at temperature below 50 °C. AG-b was stable at temperature below 60 °C. Zn²⁺, Mg²⁺ or Ca²⁺ increased AG-a activity, while Mn²⁺, Cu²⁺ or Ca²⁺ increased AG-b activity. However, Ag⁺, Hg²⁺, Fe³⁺, EDTA and SDS inhibited AG-a and AG-b activities. The main hydrolysates of agarose by AG-a were neoagarotetraose and neoagarohexaose. The main hydrolysates of agarose by AG-b were neoagarooctaose and neoagarohexaose. When the mixture of AG-a and AG-b were used, agarose was mainly degraded into neoagarobiose.</description><subject>Ammonium</subject><subject>Ammonium Sulfate</subject><subject>Bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biochemistry</subject><subject>Bioinformatics</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Carbon - metabolism</subject><subject>Carbon sources</subject><subject>Cations, Divalent - pharmacology</subject><subject>Chemical analysis</subject><subject>Chemical Fractionation</subject><subject>China</subject><subject>Chromatography</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Ion Exchange</subject><subject>Culture Media - chemistry</subject><subject>Edetic Acid - pharmacology</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Activators - pharmacology</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Galactosides - metabolism</subject><subject>Genetic Engineering</subject><subject>Glycoside Hydrolases - chemistry</subject><subject>Glycoside Hydrolases - isolation & purification</subject><subject>Glycoside Hydrolases - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Inorganic Chemistry</subject><subject>Life Sciences</subject><subject>Marine biology</subject><subject>Metals - pharmacology</subject><subject>Microbiology</subject><subject>Molecular Weight</subject><subject>Oligosaccharides - metabolism</subject><subject>Original Paper</subject><subject>Phylogeny</subject><subject>Proteins</subject><subject>RNA, Ribosomal, 16S - genetics</subject><subject>Seawater</subject><subject>Seawater - microbiology</subject><subject>Sepharose - metabolism</subject><subject>Sequence Analysis, DNA</subject><subject>Sodium Dodecyl Sulfate - pharmacology</subject><subject>Studies</subject><subject>Sulfates</subject><subject>Temperature</subject><subject>Vibrio - classification</subject><subject>Vibrio - enzymology</subject><subject>Vibrio - isolation & purification</subject><subject>Water analysis</subject><issn>1367-5435</issn><issn>1476-5535</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9ksGKFDEQhoMo7jr6AF40CHoyayXpSrqPsrgqLCi46zWkuytjlunOmEwf9OnN0oMrgp4SKl9V_nyEsacSziSAfVMkqA4FQCtAGxTqHjuVjTUCUeP9utfGCmw0nrBHpdwAAFqrHrIT2Ta2VS2esqvPS44hDv4Q08z9PPLhm89-OFCOP9diCtxva61Q4SGniXs--Rxn4v3KLRP_GvscEy_7M34hzGP2IPhdoSfHdcOuL95dnX8Ql5_efzx_eykGVOYgVNsFS2oEY6BpWiLVddgTkuytJGP61jRAOnhjFXZhJNuODUoP1pLRvtMb9mqdu8_p-0Ll4KZYBtrt_ExpKc50GrWuMjbsxV_gTVryXLM5pVEqidZUSK7QkFMpmYLb51hf-sNJcLe-3erbVd_u1nft3bBnx8FLP9F413EUXIGXR8CXwe9C9vMQy29OATaAUldOrVypR_OW8l3C_93-em1Ky_4fYf_4HBV_vuLBJ-e3uea4_qJAaoBOQY2rfwE9Gaui</recordid><startdate>20080801</startdate><enddate>20080801</enddate><creator>Fu, Wandong</creator><creator>Han, Baoqin</creator><creator>Duan, Delin</creator><creator>Liu, Wanshun</creator><creator>Wang, Changhong</creator><general>Berlin/Heidelberg : Springer-Verlag</general><general>Oxford University Press</general><general>Springer-Verlag</general><general>Springer</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>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</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>8FL</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20080801</creationdate><title>Purification and characterization of agarases from a marine bacterium Vibrio sp. F-6</title><author>Fu, Wandong ; Han, Baoqin ; Duan, Delin ; Liu, Wanshun ; Wang, Changhong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c526t-289f7e2d0660448ee2995be5e1b71e66b8640e3fa67259fde78d451a077e63a93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Ammonium</topic><topic>Ammonium Sulfate</topic><topic>Bacteria</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biochemistry</topic><topic>Bioinformatics</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Carbon - metabolism</topic><topic>Carbon sources</topic><topic>Cations, Divalent - pharmacology</topic><topic>Chemical analysis</topic><topic>Chemical Fractionation</topic><topic>China</topic><topic>Chromatography</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Ion Exchange</topic><topic>Culture Media - chemistry</topic><topic>Edetic Acid - pharmacology</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Activators - pharmacology</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Galactosides - metabolism</topic><topic>Genetic Engineering</topic><topic>Glycoside Hydrolases - chemistry</topic><topic>Glycoside Hydrolases - isolation & purification</topic><topic>Glycoside Hydrolases - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Inorganic Chemistry</topic><topic>Life Sciences</topic><topic>Marine biology</topic><topic>Metals - pharmacology</topic><topic>Microbiology</topic><topic>Molecular Weight</topic><topic>Oligosaccharides - metabolism</topic><topic>Original Paper</topic><topic>Phylogeny</topic><topic>Proteins</topic><topic>RNA, Ribosomal, 16S - genetics</topic><topic>Seawater</topic><topic>Seawater - microbiology</topic><topic>Sepharose - metabolism</topic><topic>Sequence Analysis, DNA</topic><topic>Sodium Dodecyl Sulfate - pharmacology</topic><topic>Studies</topic><topic>Sulfates</topic><topic>Temperature</topic><topic>Vibrio - classification</topic><topic>Vibrio - enzymology</topic><topic>Vibrio - isolation & 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Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of industrial microbiology & biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fu, Wandong</au><au>Han, Baoqin</au><au>Duan, Delin</au><au>Liu, Wanshun</au><au>Wang, Changhong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of agarases from a marine bacterium Vibrio sp. F-6</atitle><jtitle>Journal of industrial microbiology & biotechnology</jtitle><stitle>J Ind Microbiol Biotechnol</stitle><addtitle>J Ind Microbiol Biotechnol</addtitle><date>2008-08-01</date><risdate>2008</risdate><volume>35</volume><issue>8</issue><spage>915</spage><epage>922</epage><pages>915-922</pages><issn>1367-5435</issn><eissn>1476-5535</eissn><abstract>Marine bacterium Vibrio sp. F-6, utilizing agarose as a carbon source to produce agarases, was isolated from seawater samples taken from Qingdao, China. Two agarases (AG-a and AG-b) were purified to a homogeneity from the cultural supernatant of Vibrio sp. F-6 through ammonium sulfate precipitation, Q-Sepharose FF chromatography, and Sephacryl S-100 gel filtration. Molecular weights of agarases were estimated to be 54.0 kDa (AG-a) and 34.5 kDa (AG-b) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimum pH values for AG-a and AG-b were about 7.0 and 9.0, respectively. AG-a was stable in the pH range of 4.0-9.0 and AG-b was stable in the pH range of 4.0-10.0. The optimum temperatures of AG-a and AG-b were 40 and 55 °C, respectively. AG-a was stable at temperature below 50 °C. AG-b was stable at temperature below 60 °C. Zn²⁺, Mg²⁺ or Ca²⁺ increased AG-a activity, while Mn²⁺, Cu²⁺ or Ca²⁺ increased AG-b activity. However, Ag⁺, Hg²⁺, Fe³⁺, EDTA and SDS inhibited AG-a and AG-b activities. The main hydrolysates of agarose by AG-a were neoagarotetraose and neoagarohexaose. The main hydrolysates of agarose by AG-b were neoagarooctaose and neoagarohexaose. When the mixture of AG-a and AG-b were used, agarose was mainly degraded into neoagarobiose.</abstract><cop>Berlin/Heidelberg</cop><pub>Berlin/Heidelberg : Springer-Verlag</pub><pmid>18478285</pmid><doi>10.1007/s10295-008-0365-2</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1367-5435 |
| ispartof | Journal of industrial microbiology & biotechnology, 2008-08, Vol.35 (8), p.915-922 |
| issn | 1367-5435 1476-5535 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_69353355 |
| source | Oxford Journals Open Access Collection; MEDLINE; SpringerLink Journals |
| subjects | Ammonium Ammonium Sulfate Bacteria Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Biochemistry Bioinformatics Biological and medical sciences Biomedical and Life Sciences Biotechnology Carbon - metabolism Carbon sources Cations, Divalent - pharmacology Chemical analysis Chemical Fractionation China Chromatography Chromatography, Gel Chromatography, Ion Exchange Culture Media - chemistry Edetic Acid - pharmacology Electrophoresis, Polyacrylamide Gel Enzyme Activators - pharmacology Enzyme Inhibitors - pharmacology Enzyme Stability Enzymes Fundamental and applied biological sciences. Psychology Galactosides - metabolism Genetic Engineering Glycoside Hydrolases - chemistry Glycoside Hydrolases - isolation & purification Glycoside Hydrolases - metabolism Hydrogen-Ion Concentration Inorganic Chemistry Life Sciences Marine biology Metals - pharmacology Microbiology Molecular Weight Oligosaccharides - metabolism Original Paper Phylogeny Proteins RNA, Ribosomal, 16S - genetics Seawater Seawater - microbiology Sepharose - metabolism Sequence Analysis, DNA Sodium Dodecyl Sulfate - pharmacology Studies Sulfates Temperature Vibrio - classification Vibrio - enzymology Vibrio - isolation & purification Water analysis |
| title | Purification and characterization of agarases from a marine bacterium Vibrio sp. F-6 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-08T08%3A26%3A43IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Purification%20and%20characterization%20of%20agarases%20from%20a%20marine%20bacterium%20Vibrio%20sp.%20F-6&rft.jtitle=Journal%20of%20industrial%20microbiology%20&%20biotechnology&rft.au=Fu,%20Wandong&rft.date=2008-08-01&rft.volume=35&rft.issue=8&rft.spage=915&rft.epage=922&rft.pages=915-922&rft.issn=1367-5435&rft.eissn=1476-5535&rft_id=info:doi/10.1007/s10295-008-0365-2&rft_dat=%3Cproquest_cross%3E1897352631%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=235121576&rft_id=info:pmid/18478285&rft_oup_id=10.1007/s10295-008-0365-2&rfr_iscdi=true |