Studies on Immobilization and Partial Characterization of Lipases from Wheat Seeds (Triticum aestivum)
The objective of this study was to provide some features on immobilization and partial characterization of lipases from wheat seeds. The optimum pH and temperature were found to be 5.5 and 32–37 °C, respectively. The stability of the concentrated enzymatic extract to high temperatures (25, 35, 45, a...
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Veröffentlicht in: | Applied biochemistry and biotechnology 2011-09, Vol.165 (1), p.75-86 |
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description | The objective of this study was to provide some features on immobilization and partial characterization of lipases from wheat seeds. The optimum pH and temperature were found to be 5.5 and 32–37 °C, respectively. The stability of the concentrated enzymatic extract to high temperatures (25, 35, 45, and 55 °C) showed that the incubation of the extract at 55 °C led to its complete inactivation. The concentrated enzymatic extract kept 90% of its hydrolytic and esterification activities until 70 and 40 days of storage at 4 °C, respectively. The extract presented higher hydrolytic specificity to substrates of medium and long chains and higher esterification affinity to fatty acids of short and medium chains and alcohols with two and three carbon atoms. After the immobilization process using activated coal and sodium alginate as supports, an enhancement of about threefold in lipase activity was observed. The development of the present work permitted us to point out some characteristics of lipases from wheat seeds necessary for the proposition of new future industrial applications for this important biocatalyst. |
doi_str_mv | 10.1007/s12010-011-9234-y |
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Vladimir ; Oliveira, Débora ; Treichel, Helen ; Cansian, Rogério Luís</creator><creatorcontrib>Pierozan, Morgana Karin ; Oestreicher, Enrique Guillermo ; Oliveira, J. Vladimir ; Oliveira, Débora ; Treichel, Helen ; Cansian, Rogério Luís</creatorcontrib><description>The objective of this study was to provide some features on immobilization and partial characterization of lipases from wheat seeds. The optimum pH and temperature were found to be 5.5 and 32–37 °C, respectively. The stability of the concentrated enzymatic extract to high temperatures (25, 35, 45, and 55 °C) showed that the incubation of the extract at 55 °C led to its complete inactivation. The concentrated enzymatic extract kept 90% of its hydrolytic and esterification activities until 70 and 40 days of storage at 4 °C, respectively. The extract presented higher hydrolytic specificity to substrates of medium and long chains and higher esterification affinity to fatty acids of short and medium chains and alcohols with two and three carbon atoms. After the immobilization process using activated coal and sodium alginate as supports, an enhancement of about threefold in lipase activity was observed. The development of the present work permitted us to point out some characteristics of lipases from wheat seeds necessary for the proposition of new future industrial applications for this important biocatalyst.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-011-9234-y</identifier><identifier>PMID: 21468634</identifier><identifier>CODEN: ABIBDL</identifier><language>eng</language><publisher>New York: Humana Press Inc</publisher><subject>Biochemistry ; Biological and medical sciences ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; Enzymes ; Enzymes, Immobilized - chemistry ; Enzymes, Immobilized - metabolism ; Fundamental and applied biological sciences. Psychology ; General aspects ; High temperature ; Immobilization techniques ; Inactivation ; Lipase - chemistry ; Lipase - metabolism ; Methods. Procedures. Technologies ; Plant biology ; Seeds ; Seeds - enzymology ; Temperature ; Triticum - enzymology ; Wheat</subject><ispartof>Applied biochemistry and biotechnology, 2011-09, Vol.165 (1), p.75-86</ispartof><rights>Springer Science+Business Media, LLC 2011</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c400t-73b70db5712e91fee66f58f538acf0e4b49a0447a60d6fea297e5d05b314c4bd3</citedby><cites>FETCH-LOGICAL-c400t-73b70db5712e91fee66f58f538acf0e4b49a0447a60d6fea297e5d05b314c4bd3</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/s12010-011-9234-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-011-9234-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24637278$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21468634$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pierozan, Morgana Karin</creatorcontrib><creatorcontrib>Oestreicher, Enrique Guillermo</creatorcontrib><creatorcontrib>Oliveira, J. Vladimir</creatorcontrib><creatorcontrib>Oliveira, Débora</creatorcontrib><creatorcontrib>Treichel, Helen</creatorcontrib><creatorcontrib>Cansian, Rogério Luís</creatorcontrib><title>Studies on Immobilization and Partial Characterization of Lipases from Wheat Seeds (Triticum aestivum)</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>The objective of this study was to provide some features on immobilization and partial characterization of lipases from wheat seeds. The optimum pH and temperature were found to be 5.5 and 32–37 °C, respectively. The stability of the concentrated enzymatic extract to high temperatures (25, 35, 45, and 55 °C) showed that the incubation of the extract at 55 °C led to its complete inactivation. The concentrated enzymatic extract kept 90% of its hydrolytic and esterification activities until 70 and 40 days of storage at 4 °C, respectively. The extract presented higher hydrolytic specificity to substrates of medium and long chains and higher esterification affinity to fatty acids of short and medium chains and alcohols with two and three carbon atoms. After the immobilization process using activated coal and sodium alginate as supports, an enhancement of about threefold in lipase activity was observed. The development of the present work permitted us to point out some characteristics of lipases from wheat seeds necessary for the proposition of new future industrial applications for this important biocatalyst.</description><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Enzymes</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Enzymes, Immobilized - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects</subject><subject>High temperature</subject><subject>Immobilization techniques</subject><subject>Inactivation</subject><subject>Lipase - chemistry</subject><subject>Lipase - metabolism</subject><subject>Methods. Procedures. Technologies</subject><subject>Plant biology</subject><subject>Seeds</subject><subject>Seeds - enzymology</subject><subject>Temperature</subject><subject>Triticum - enzymology</subject><subject>Wheat</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</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>eNp1kVtrFEEQhRtRzCb6A3yRQRD1YbS6p6-PYTEmsBAhER-bmp5u02Eua_eMsP56O-zGQCBPRVHfqTrUIeQNhc8UQH3JlAGFGiitDWt4vXtGVlQIUwMz9DlZAVNNzZg2R-Q451sAyrRQL8kRo1xq2fAVCVfz0kWfq2msLoZhamMf_-IcS4tjV33HNEfsq_UNJnSzT_fDKVSbuMVclCFNQ_XzxuNcXXnf5erjdYpzdMtQoc9z_LMMn16RFwH77F8f6gn5cfb1en1eby6_XaxPN7XjAHOtmlZB1wpFmTc0eC9lEDqIRqML4HnLDQLnCiV0MnhkRnnRgWgbyh1vu-aEfNjv3abp91Ku2yFm5_seRz8t2WoDUhmhaSHfPSJvpyWNxZzV2nAJkpoC0T3k0pRz8sFuUxww7SwFexeB3UdgSwT2LgK7K5q3h8VLO_juv-L-5wV4fwAwO-xDwtHF_MBx2SimdOHYnstlNP7y6cHh09f_AbjknwQ</recordid><startdate>20110901</startdate><enddate>20110901</enddate><creator>Pierozan, Morgana Karin</creator><creator>Oestreicher, Enrique Guillermo</creator><creator>Oliveira, J. 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Vladimir ; Oliveira, Débora ; Treichel, Helen ; Cansian, Rogério Luís</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c400t-73b70db5712e91fee66f58f538acf0e4b49a0447a60d6fea297e5d05b314c4bd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Enzymes</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Enzymes, Immobilized - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects</topic><topic>High temperature</topic><topic>Immobilization techniques</topic><topic>Inactivation</topic><topic>Lipase - chemistry</topic><topic>Lipase - metabolism</topic><topic>Methods. Procedures. 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Vladimir</au><au>Oliveira, Débora</au><au>Treichel, Helen</au><au>Cansian, Rogério Luís</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Studies on Immobilization and Partial Characterization of Lipases from Wheat Seeds (Triticum aestivum)</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><stitle>Appl Biochem Biotechnol</stitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2011-09-01</date><risdate>2011</risdate><volume>165</volume><issue>1</issue><spage>75</spage><epage>86</epage><pages>75-86</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><coden>ABIBDL</coden><abstract>The objective of this study was to provide some features on immobilization and partial characterization of lipases from wheat seeds. The optimum pH and temperature were found to be 5.5 and 32–37 °C, respectively. The stability of the concentrated enzymatic extract to high temperatures (25, 35, 45, and 55 °C) showed that the incubation of the extract at 55 °C led to its complete inactivation. The concentrated enzymatic extract kept 90% of its hydrolytic and esterification activities until 70 and 40 days of storage at 4 °C, respectively. The extract presented higher hydrolytic specificity to substrates of medium and long chains and higher esterification affinity to fatty acids of short and medium chains and alcohols with two and three carbon atoms. After the immobilization process using activated coal and sodium alginate as supports, an enhancement of about threefold in lipase activity was observed. The development of the present work permitted us to point out some characteristics of lipases from wheat seeds necessary for the proposition of new future industrial applications for this important biocatalyst.</abstract><cop>New York</cop><pub>Humana Press Inc</pub><pmid>21468634</pmid><doi>10.1007/s12010-011-9234-y</doi><tpages>12</tpages></addata></record> |
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subjects | Biochemistry Biological and medical sciences Biotechnology Chemistry Chemistry and Materials Science Enzymes Enzymes, Immobilized - chemistry Enzymes, Immobilized - metabolism Fundamental and applied biological sciences. Psychology General aspects High temperature Immobilization techniques Inactivation Lipase - chemistry Lipase - metabolism Methods. Procedures. Technologies Plant biology Seeds Seeds - enzymology Temperature Triticum - enzymology Wheat |
title | Studies on Immobilization and Partial Characterization of Lipases from Wheat Seeds (Triticum aestivum) |
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