Thermal Stabilities of Peroxidases from Fresh Pinto Beans
ABSTRACT Heat stabilities of crude and partially purified soluble (SPOX), ionically bound (IPOX) and total peroxidase (TPOX) from fresh pinto beans were investigated at 55–90°C. Heat inactivation of peroxidase (POX) followed first‐order reaction kinetics. Each inactivation curve consisted of two lin...
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| Veröffentlicht in: | Journal of food science 1998-11, Vol.63 (6), p.987-990 |
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| creator | YEMENICIOGLU, A ÖZKAN, M CEMEROGLU, B |
| description | ABSTRACT
Heat stabilities of crude and partially purified soluble (SPOX), ionically bound (IPOX) and total peroxidase (TPOX) from fresh pinto beans were investigated at 55–90°C. Heat inactivation of peroxidase (POX) followed first‐order reaction kinetics. Each inactivation curve consisted of two linear parts: initial rapid inactivation (heat‐labile) followed by slower inactivation (heat‐stable). IPOX showed activation during heat treatment with a highly heat‐stable isoenzyme (D90=40 min) which was more heat‐stable than SPOX. Activation energies for heat‐stable parts of crude IPOX and SPOX were, respectively, 12.1 and 36.4 kcalmol‐1 with z values 45.4 and 14.1C°. Heat stable SPOX isoenzymes (D70=22.6) were obtained by 65–95% (NH4)2SO4 precipitation from crude SPOX. Two POX fractions (F1 and F2) were separated from TPOX by ion‐exchange chromatography. |
| doi_str_mv | 10.1111/j.1365-2621.1998.tb15839.x |
| format | Article |
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Heat stabilities of crude and partially purified soluble (SPOX), ionically bound (IPOX) and total peroxidase (TPOX) from fresh pinto beans were investigated at 55–90°C. Heat inactivation of peroxidase (POX) followed first‐order reaction kinetics. Each inactivation curve consisted of two linear parts: initial rapid inactivation (heat‐labile) followed by slower inactivation (heat‐stable). IPOX showed activation during heat treatment with a highly heat‐stable isoenzyme (D90=40 min) which was more heat‐stable than SPOX. Activation energies for heat‐stable parts of crude IPOX and SPOX were, respectively, 12.1 and 36.4 kcalmol‐1 with z values 45.4 and 14.1C°. Heat stable SPOX isoenzymes (D70=22.6) were obtained by 65–95% (NH4)2SO4 precipitation from crude SPOX. Two POX fractions (F1 and F2) were separated from TPOX by ion‐exchange chromatography.</description><identifier>ISSN: 0022-1147</identifier><identifier>EISSN: 1750-3841</identifier><identifier>DOI: 10.1111/j.1365-2621.1998.tb15839.x</identifier><identifier>CODEN: JFDSAZ</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Beans ; Biological and medical sciences ; Chemistry ; Food industries ; Fruit and vegetable industries ; Fundamental and applied biological sciences. Psychology ; Heat ; heat activation ; heat inactivation ; peroxidase ; pinto beans ; purification</subject><ispartof>Journal of food science, 1998-11, Vol.63 (6), p.987-990</ispartof><rights>1999 INIST-CNRS</rights><rights>Copyright Institute of Food Technologists Nov 1998</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4117-b5878112ed0707abba9f285e8262187883cbe0e62a6f3d722f5fffa0af6727583</citedby><cites>FETCH-LOGICAL-c4117-b5878112ed0707abba9f285e8262187883cbe0e62a6f3d722f5fffa0af6727583</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-2621.1998.tb15839.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2621.1998.tb15839.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1650946$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>YEMENICIOGLU, A</creatorcontrib><creatorcontrib>ÖZKAN, M</creatorcontrib><creatorcontrib>CEMEROGLU, B</creatorcontrib><title>Thermal Stabilities of Peroxidases from Fresh Pinto Beans</title><title>Journal of food science</title><description>ABSTRACT
Heat stabilities of crude and partially purified soluble (SPOX), ionically bound (IPOX) and total peroxidase (TPOX) from fresh pinto beans were investigated at 55–90°C. Heat inactivation of peroxidase (POX) followed first‐order reaction kinetics. Each inactivation curve consisted of two linear parts: initial rapid inactivation (heat‐labile) followed by slower inactivation (heat‐stable). IPOX showed activation during heat treatment with a highly heat‐stable isoenzyme (D90=40 min) which was more heat‐stable than SPOX. Activation energies for heat‐stable parts of crude IPOX and SPOX were, respectively, 12.1 and 36.4 kcalmol‐1 with z values 45.4 and 14.1C°. Heat stable SPOX isoenzymes (D70=22.6) were obtained by 65–95% (NH4)2SO4 precipitation from crude SPOX. Two POX fractions (F1 and F2) were separated from TPOX by ion‐exchange chromatography.</description><subject>Beans</subject><subject>Biological and medical sciences</subject><subject>Chemistry</subject><subject>Food industries</subject><subject>Fruit and vegetable industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Heat</subject><subject>heat activation</subject><subject>heat inactivation</subject><subject>peroxidase</subject><subject>pinto beans</subject><subject>purification</subject><issn>0022-1147</issn><issn>1750-3841</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNqVkF1PwjAYhRujiYj-h4V4u9mPrR_eGEWHX0EiqJdNN9pQHAzbEeHf2wWi1_amOXlPn_P2ANBDMEHhXMwTRGgWY4pRgoTgSVOgjBORbA5AB7EMxoSn6BB0IMQ4Rihlx-DE-zlsNaEdICYz7RaqisaNKmxlG6t9VJtopF29sVPlgzSuXkS5034WjeyyqaMbrZb-FBwZVXl9tr-74C2_m_Tv4-eXwUP_-jkuU4RYXGSccYSwnkIGmSoKJQzmmebtzmHESVloqClW1JApw9hkxhgFlaEMs_CXLujtuCtXf621b-S8XrtliJRIpIQxiNNgutyZSld777SRK2cXym0lgrJtSs5l25RsU2XblNw3JTfh8fk-QflSVcapZWn9H4FmUKQ02K52tm9b6e0_AuRjfjsWnAVCvCNY3-jNL0G5T0kZYZn8GA7kU87exZAT-Up-AA7wiyg</recordid><startdate>199811</startdate><enddate>199811</enddate><creator>YEMENICIOGLU, A</creator><creator>ÖZKAN, M</creator><creator>CEMEROGLU, B</creator><general>Blackwell Publishing Ltd</general><general>Institute of Food Technologists</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7QR</scope><scope>7ST</scope><scope>7T7</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>SOI</scope></search><sort><creationdate>199811</creationdate><title>Thermal Stabilities of Peroxidases from Fresh Pinto Beans</title><author>YEMENICIOGLU, A ; ÖZKAN, M ; CEMEROGLU, B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4117-b5878112ed0707abba9f285e8262187883cbe0e62a6f3d722f5fffa0af6727583</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Beans</topic><topic>Biological and medical sciences</topic><topic>Chemistry</topic><topic>Food industries</topic><topic>Fruit and vegetable industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Heat</topic><topic>heat activation</topic><topic>heat inactivation</topic><topic>peroxidase</topic><topic>pinto beans</topic><topic>purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>YEMENICIOGLU, A</creatorcontrib><creatorcontrib>ÖZKAN, M</creatorcontrib><creatorcontrib>CEMEROGLU, B</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><jtitle>Journal of food science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>YEMENICIOGLU, A</au><au>ÖZKAN, M</au><au>CEMEROGLU, B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thermal Stabilities of Peroxidases from Fresh Pinto Beans</atitle><jtitle>Journal of food science</jtitle><date>1998-11</date><risdate>1998</risdate><volume>63</volume><issue>6</issue><spage>987</spage><epage>990</epage><pages>987-990</pages><issn>0022-1147</issn><eissn>1750-3841</eissn><coden>JFDSAZ</coden><abstract>ABSTRACT
Heat stabilities of crude and partially purified soluble (SPOX), ionically bound (IPOX) and total peroxidase (TPOX) from fresh pinto beans were investigated at 55–90°C. Heat inactivation of peroxidase (POX) followed first‐order reaction kinetics. Each inactivation curve consisted of two linear parts: initial rapid inactivation (heat‐labile) followed by slower inactivation (heat‐stable). IPOX showed activation during heat treatment with a highly heat‐stable isoenzyme (D90=40 min) which was more heat‐stable than SPOX. Activation energies for heat‐stable parts of crude IPOX and SPOX were, respectively, 12.1 and 36.4 kcalmol‐1 with z values 45.4 and 14.1C°. Heat stable SPOX isoenzymes (D70=22.6) were obtained by 65–95% (NH4)2SO4 precipitation from crude SPOX. Two POX fractions (F1 and F2) were separated from TPOX by ion‐exchange chromatography.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><doi>10.1111/j.1365-2621.1998.tb15839.x</doi><tpages>4</tpages></addata></record> |
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| subjects | Beans Biological and medical sciences Chemistry Food industries Fruit and vegetable industries Fundamental and applied biological sciences. Psychology Heat heat activation heat inactivation peroxidase pinto beans purification |
| title | Thermal Stabilities of Peroxidases from Fresh Pinto Beans |
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