Highly Efficient Method Towards In Situ Immobilization of Invertase Using Cryogelation
A novel method was developed for the immobilization of Saccharomyces cerevisiae invertase within supermacroporous polyacrylamide cryogel and was used to produce invert sugar. First, the cross-linking of invertase with soluble polyglutaraldehyde (PGA) was carried out prior to immobilization in order...
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| Veröffentlicht in: | Applied biochemistry and biotechnology 2013-12, Vol.171 (8), p.2142-2152 |
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| creator | Olcer, Zehra Ozmen, Mehmet Murat Sahin, Zeynep M Yilmaz, Faruk Tanriseven, Aziz |
| description | A novel method was developed for the immobilization of Saccharomyces cerevisiae invertase within supermacroporous polyacrylamide cryogel and was used to produce invert sugar. First, the cross-linking of invertase with soluble polyglutaraldehyde (PGA) was carried out prior to immobilization in order to increase the bulkiness of invertase and thus preventing the leakage of the cross-linked enzyme after immobilization by entrapment. And then, in situ immobilization of PGA cross-linked invertase within cryogel synthesis was achieved by free radical polymerization in semi-frozen state. The method resulted in 100 % immobilization and 74 % activity yields. The immobilized invertase retained all the initial activity for 30 days and 30 batch reactions. Immobilization had no effect on optimum temperature and it was 60 °C for both free and immobilized enzyme. However, optimum pH was affected upon immobilization. Optimum pH values for free and immobilized enzyme were 4.5 and 5.0, respectively. The immobilized enzyme was more stable than the free enzyme at high pH and temperatures. The kinetic parameters for free and immobilized invertase were also determined. The newly developed method is simple yet effective and could be used for the immobilization of some other enzymes and microorganisms. |
| doi_str_mv | 10.1007/s12010-013-0507-5 |
| format | Article |
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First, the cross-linking of invertase with soluble polyglutaraldehyde (PGA) was carried out prior to immobilization in order to increase the bulkiness of invertase and thus preventing the leakage of the cross-linked enzyme after immobilization by entrapment. And then, in situ immobilization of PGA cross-linked invertase within cryogel synthesis was achieved by free radical polymerization in semi-frozen state. The method resulted in 100 % immobilization and 74 % activity yields. The immobilized invertase retained all the initial activity for 30 days and 30 batch reactions. Immobilization had no effect on optimum temperature and it was 60 °C for both free and immobilized enzyme. However, optimum pH was affected upon immobilization. Optimum pH values for free and immobilized enzyme were 4.5 and 5.0, respectively. The immobilized enzyme was more stable than the free enzyme at high pH and temperatures. The kinetic parameters for free and immobilized invertase were also determined. The newly developed method is simple yet effective and could be used for the immobilization of some other enzymes and microorganisms.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-013-0507-5</identifier><identifier>PMID: 24026416</identifier><identifier>CODEN: ABIBDL</identifier><language>eng</language><publisher>Boston: Springer-Verlag</publisher><subject>beta-fructofuranosidase ; beta-Fructofuranosidase - chemistry ; Biochemistry ; Biological and medical sciences ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; crosslinking ; Cryogels - chemistry ; Enzymes ; Enzymes, Immobilized - chemistry ; Fundamental and applied biological sciences. Psychology ; General aspects ; Glutaral - analogs & derivatives ; Glutaral - chemistry ; Hydrogen-Ion Concentration ; Immobilization techniques ; immobilized enzymes ; Kinetics ; Methods. Procedures. Technologies ; Microbiology ; Microorganisms ; new methods ; polyacrylamide ; polymerization ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - chemistry ; Saccharomyces cerevisiae - enzymology ; sugars ; Temperature ; Yeast</subject><ispartof>Applied biochemistry and biotechnology, 2013-12, Vol.171 (8), p.2142-2152</ispartof><rights>Springer Science+Business Media New York 2013</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c463t-4f065559f9130bac07cd3678668c85e7de8095b4456c46df147cea3c708590223</citedby><cites>FETCH-LOGICAL-c463t-4f065559f9130bac07cd3678668c85e7de8095b4456c46df147cea3c708590223</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/s12010-013-0507-5$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-013-0507-5$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27923,27924,41487,42556,51318</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=28051813$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24026416$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Olcer, Zehra</creatorcontrib><creatorcontrib>Ozmen, Mehmet Murat</creatorcontrib><creatorcontrib>Sahin, Zeynep M</creatorcontrib><creatorcontrib>Yilmaz, Faruk</creatorcontrib><creatorcontrib>Tanriseven, Aziz</creatorcontrib><title>Highly Efficient Method Towards In Situ Immobilization of Invertase Using Cryogelation</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>A novel method was developed for the immobilization of Saccharomyces cerevisiae invertase within supermacroporous polyacrylamide cryogel and was used to produce invert sugar. First, the cross-linking of invertase with soluble polyglutaraldehyde (PGA) was carried out prior to immobilization in order to increase the bulkiness of invertase and thus preventing the leakage of the cross-linked enzyme after immobilization by entrapment. And then, in situ immobilization of PGA cross-linked invertase within cryogel synthesis was achieved by free radical polymerization in semi-frozen state. The method resulted in 100 % immobilization and 74 % activity yields. The immobilized invertase retained all the initial activity for 30 days and 30 batch reactions. Immobilization had no effect on optimum temperature and it was 60 °C for both free and immobilized enzyme. However, optimum pH was affected upon immobilization. Optimum pH values for free and immobilized enzyme were 4.5 and 5.0, respectively. The immobilized enzyme was more stable than the free enzyme at high pH and temperatures. The kinetic parameters for free and immobilized invertase were also determined. The newly developed method is simple yet effective and could be used for the immobilization of some other enzymes and microorganisms.</description><subject>beta-fructofuranosidase</subject><subject>beta-Fructofuranosidase - chemistry</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>crosslinking</subject><subject>Cryogels - chemistry</subject><subject>Enzymes</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects</subject><subject>Glutaral - analogs & derivatives</subject><subject>Glutaral - chemistry</subject><subject>Hydrogen-Ion Concentration</subject><subject>Immobilization techniques</subject><subject>immobilized enzymes</subject><subject>Kinetics</subject><subject>Methods. Procedures. Technologies</subject><subject>Microbiology</subject><subject>Microorganisms</subject><subject>new methods</subject><subject>polyacrylamide</subject><subject>polymerization</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - chemistry</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>sugars</subject><subject>Temperature</subject><subject>Yeast</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</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>eNp9kEtv1DAUhS1ERYfCD2ADlhASm5Rrx68s0ajQkVp10Q5by-PYqaskLnYCGn49bjM8xILVXZzvnHt0EHpF4JQAyA-ZUCBQAakr4CAr_gStCOdNBbQhT9EKqKwrSlVzjJ7nfAdAqOLyGTqmDKhgRKzQl_PQ3fZ7fOZ9sMGNE750021s8U38blKb8WbE12Ga8WYY4i704YeZQhxx9EX55tJkssPbHMYOr9M-dq5_1F-gI2_67F4e7gnafjq7WZ9XF1efN-uPF5Vlop4q5kHwUtg3pIadsSBtWwuphFBWcSdbp6DhO8a4KIbWEyatM7WVoHgDlNYn6P2Se5_i19nlSQ8hW9f3ZnRxzpowQZQkDRcFffsPehfnNJZ2j5TkUilSKLJQNsWck_P6PoXBpL0moB9G18vouoyuH0bXvHheH5Ln3eDa345fKxfg3QEw2ZreJzPakP9wCjgpvwtHFy4Xaexc-qvif76_WUzeRG26VIK31wViAMCp4LT-CdowoFk</recordid><startdate>20131201</startdate><enddate>20131201</enddate><creator>Olcer, Zehra</creator><creator>Ozmen, Mehmet Murat</creator><creator>Sahin, Zeynep M</creator><creator>Yilmaz, Faruk</creator><creator>Tanriseven, Aziz</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>20131201</creationdate><title>Highly Efficient Method Towards In Situ Immobilization of Invertase Using Cryogelation</title><author>Olcer, Zehra ; Ozmen, Mehmet Murat ; Sahin, Zeynep M ; Yilmaz, Faruk ; Tanriseven, Aziz</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c463t-4f065559f9130bac07cd3678668c85e7de8095b4456c46df147cea3c708590223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>beta-fructofuranosidase</topic><topic>beta-Fructofuranosidase - chemistry</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>crosslinking</topic><topic>Cryogels - chemistry</topic><topic>Enzymes</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects</topic><topic>Glutaral - analogs & derivatives</topic><topic>Glutaral - chemistry</topic><topic>Hydrogen-Ion Concentration</topic><topic>Immobilization techniques</topic><topic>immobilized enzymes</topic><topic>Kinetics</topic><topic>Methods. Procedures. Technologies</topic><topic>Microbiology</topic><topic>Microorganisms</topic><topic>new methods</topic><topic>polyacrylamide</topic><topic>polymerization</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - chemistry</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>sugars</topic><topic>Temperature</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Olcer, Zehra</creatorcontrib><creatorcontrib>Ozmen, Mehmet Murat</creatorcontrib><creatorcontrib>Sahin, Zeynep M</creatorcontrib><creatorcontrib>Yilmaz, Faruk</creatorcontrib><creatorcontrib>Tanriseven, Aziz</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>Olcer, Zehra</au><au>Ozmen, Mehmet Murat</au><au>Sahin, Zeynep M</au><au>Yilmaz, Faruk</au><au>Tanriseven, Aziz</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Highly Efficient Method Towards In Situ Immobilization of Invertase Using Cryogelation</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><stitle>Appl Biochem Biotechnol</stitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2013-12-01</date><risdate>2013</risdate><volume>171</volume><issue>8</issue><spage>2142</spage><epage>2152</epage><pages>2142-2152</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><coden>ABIBDL</coden><abstract>A novel method was developed for the immobilization of Saccharomyces cerevisiae invertase within supermacroporous polyacrylamide cryogel and was used to produce invert sugar. First, the cross-linking of invertase with soluble polyglutaraldehyde (PGA) was carried out prior to immobilization in order to increase the bulkiness of invertase and thus preventing the leakage of the cross-linked enzyme after immobilization by entrapment. And then, in situ immobilization of PGA cross-linked invertase within cryogel synthesis was achieved by free radical polymerization in semi-frozen state. The method resulted in 100 % immobilization and 74 % activity yields. The immobilized invertase retained all the initial activity for 30 days and 30 batch reactions. Immobilization had no effect on optimum temperature and it was 60 °C for both free and immobilized enzyme. However, optimum pH was affected upon immobilization. Optimum pH values for free and immobilized enzyme were 4.5 and 5.0, respectively. The immobilized enzyme was more stable than the free enzyme at high pH and temperatures. The kinetic parameters for free and immobilized invertase were also determined. The newly developed method is simple yet effective and could be used for the immobilization of some other enzymes and microorganisms.</abstract><cop>Boston</cop><pub>Springer-Verlag</pub><pmid>24026416</pmid><doi>10.1007/s12010-013-0507-5</doi><tpages>11</tpages></addata></record> |
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| subjects | beta-fructofuranosidase beta-Fructofuranosidase - chemistry Biochemistry Biological and medical sciences Biotechnology Chemistry Chemistry and Materials Science crosslinking Cryogels - chemistry Enzymes Enzymes, Immobilized - chemistry Fundamental and applied biological sciences. Psychology General aspects Glutaral - analogs & derivatives Glutaral - chemistry Hydrogen-Ion Concentration Immobilization techniques immobilized enzymes Kinetics Methods. Procedures. Technologies Microbiology Microorganisms new methods polyacrylamide polymerization Saccharomyces cerevisiae Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae - enzymology sugars Temperature Yeast |
| title | Highly Efficient Method Towards In Situ Immobilization of Invertase Using Cryogelation |
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