Optimal Conditions for Continuous Immobilization of Pseudozyma hubeiensis (Strain HB85A) Lipase by Adsorption in a Packed-Bed Reactor by Response Surface Methodology
This study aimed to develop an optimal continuous process for lipase immobilization in a bed reactor in order to investigate the possibility of large-scale production. An extracellular lipase of Pseudozyma hubeiensis (strain HB85A) was immobilized by adsorption onto a polystyrene-divinylbenzene supp...
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| Veröffentlicht in: | Enzyme Research 2012, Vol.2012 (2012), p.88-99 |
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| creator | Bussamara, Roberta Dall'Agnol, Luciane Schrank, Augusto Fernandes, Kátia Flávia Vainstein, Marilene Henning |
| description | This study aimed to develop an optimal continuous process for lipase immobilization in a bed reactor in order to investigate the possibility of large-scale production. An extracellular lipase of Pseudozyma hubeiensis (strain HB85A) was immobilized by adsorption onto a polystyrene-divinylbenzene support. Furthermore, response surface methodology (RSM) was employed to optimize enzyme immobilization and evaluate the optimum temperature and pH for free and immobilized enzyme. The optimal immobilization conditions observed were 150 min incubation time, pH 4.76, and an enzyme/support ratio of 1282 U/g support. Optimal activity temperature for free and immobilized enzyme was found to be 68°C and 52°C, respectively. Optimal activity pH for free and immobilized lipase was pH 4.6 and 6.0, respectively. Lipase immobilization resulted in improved enzyme stability in the presence of nonionic detergents, at high temperatures, at acidic and neutral pH, and at high concentrations of organic solvents such as 2-propanol, methanol, and acetone. |
| doi_str_mv | 10.1155/2012/329178 |
| format | Article |
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An extracellular lipase of Pseudozyma hubeiensis (strain HB85A) was immobilized by adsorption onto a polystyrene-divinylbenzene support. Furthermore, response surface methodology (RSM) was employed to optimize enzyme immobilization and evaluate the optimum temperature and pH for free and immobilized enzyme. The optimal immobilization conditions observed were 150 min incubation time, pH 4.76, and an enzyme/support ratio of 1282 U/g support. Optimal activity temperature for free and immobilized enzyme was found to be 68°C and 52°C, respectively. Optimal activity pH for free and immobilized lipase was pH 4.6 and 6.0, respectively. Lipase immobilization resulted in improved enzyme stability in the presence of nonionic detergents, at high temperatures, at acidic and neutral pH, and at high concentrations of organic solvents such as 2-propanol, methanol, and acetone.</description><identifier>ISSN: 2090-0414</identifier><identifier>ISSN: 2090-0406</identifier><identifier>EISSN: 2090-0414</identifier><identifier>DOI: 10.1155/2012/329178</identifier><identifier>PMID: 22315670</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Limiteds</publisher><subject>acetone ; adsorption ; detergents ; enzyme stability ; immobilized enzymes ; isopropyl alcohol ; methanol ; Pseudozyma ; response surface methodology ; solvents ; temperature ; triacylglycerol lipase</subject><ispartof>Enzyme Research, 2012, Vol.2012 (2012), p.88-99</ispartof><rights>Copyright © 2012 Roberta Bussamara et al.</rights><rights>Copyright © 2012 Roberta Bussamara et al. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a5188-357df43d589166f43876eeddd29d0fe1b7aae87e3e46b0dc9f54c6624ff68e313</citedby><cites>FETCH-LOGICAL-a5188-357df43d589166f43876eeddd29d0fe1b7aae87e3e46b0dc9f54c6624ff68e313</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3270537/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3270537/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,4010,27900,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22315670$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Palomo, Jose Miguel</contributor><creatorcontrib>Bussamara, Roberta</creatorcontrib><creatorcontrib>Dall'Agnol, Luciane</creatorcontrib><creatorcontrib>Schrank, Augusto</creatorcontrib><creatorcontrib>Fernandes, Kátia Flávia</creatorcontrib><creatorcontrib>Vainstein, Marilene Henning</creatorcontrib><title>Optimal Conditions for Continuous Immobilization of Pseudozyma hubeiensis (Strain HB85A) Lipase by Adsorption in a Packed-Bed Reactor by Response Surface Methodology</title><title>Enzyme Research</title><addtitle>Enzyme Res</addtitle><description>This study aimed to develop an optimal continuous process for lipase immobilization in a bed reactor in order to investigate the possibility of large-scale production. An extracellular lipase of Pseudozyma hubeiensis (strain HB85A) was immobilized by adsorption onto a polystyrene-divinylbenzene support. Furthermore, response surface methodology (RSM) was employed to optimize enzyme immobilization and evaluate the optimum temperature and pH for free and immobilized enzyme. The optimal immobilization conditions observed were 150 min incubation time, pH 4.76, and an enzyme/support ratio of 1282 U/g support. Optimal activity temperature for free and immobilized enzyme was found to be 68°C and 52°C, respectively. Optimal activity pH for free and immobilized lipase was pH 4.6 and 6.0, respectively. Lipase immobilization resulted in improved enzyme stability in the presence of nonionic detergents, at high temperatures, at acidic and neutral pH, and at high concentrations of organic solvents such as 2-propanol, methanol, and acetone.</description><subject>acetone</subject><subject>adsorption</subject><subject>detergents</subject><subject>enzyme stability</subject><subject>immobilized enzymes</subject><subject>isopropyl alcohol</subject><subject>methanol</subject><subject>Pseudozyma</subject><subject>response surface methodology</subject><subject>solvents</subject><subject>temperature</subject><subject>triacylglycerol lipase</subject><issn>2090-0414</issn><issn>2090-0406</issn><issn>2090-0414</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>RHX</sourceid><recordid>eNqFkk1v1DAQhiMEolXpiTPINwoo1N9OLkjbFdCiRV21cLaceNJ1SeIQJ6Dt_-F_4jRl1V7AsmRb8_i1Z-ZNkucEvyNEiGOKCT1mNCcqe5TsU5zjFHPCH9_b7yWHIVzjOFgep3ya7FHKiJAK7ye_z7vBNaZGS99aNzjfBlT5fjoOrh39GNBZ0_jC1e7GTGHkK7QOMFp_s20M2owFOGiDC-jocuiNa9HpSSYWr9HKdSYAKrZoYYPvu9vLMWzQ2pTfwaYnYNEFmHKIz0XqAkIXXwd0OfaVKQF9gWHjra_91fZZ8qQydYDDu_Ug-fbxw9flabo6_3S2XKxSI0iWpUwoW3FmRZYTKeMuUxLAWktziysghTIGMgUMuCywLfNK8FJKyqtKZsAIO0jez7rdWDRgS2hjSrXu-liifqu9cfphpHUbfeV_akYVFkxFgVd3Ar3_MUIYdONCCXVtWoi11DnFKpNK8kge_ZOkHGPOOabTr97OaNn7EHqodh8iWE8u0JML9OyCSL-8n8OO_dvzCLyZgY1rrfnl_qP2YoYhIlCZHcwly_NJ7PMcN66P9tHXfuzb2CK9jiqCxHQxJreKUTMuCksqMabi4SHLdJ6zP7gh2cI</recordid><startdate>2012</startdate><enddate>2012</enddate><creator>Bussamara, Roberta</creator><creator>Dall'Agnol, Luciane</creator><creator>Schrank, Augusto</creator><creator>Fernandes, Kátia Flávia</creator><creator>Vainstein, Marilene Henning</creator><general>Hindawi Limiteds</general><general>Hindawi Puplishing Corporation</general><general>Hindawi Publishing Corporation</general><scope>188</scope><scope>ADJCN</scope><scope>AHFXO</scope><scope>RHU</scope><scope>RHW</scope><scope>RHX</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7S9</scope><scope>L.6</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>2012</creationdate><title>Optimal Conditions for Continuous Immobilization of Pseudozyma hubeiensis (Strain HB85A) Lipase by Adsorption in a Packed-Bed Reactor by Response Surface Methodology</title><author>Bussamara, Roberta ; 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An extracellular lipase of Pseudozyma hubeiensis (strain HB85A) was immobilized by adsorption onto a polystyrene-divinylbenzene support. Furthermore, response surface methodology (RSM) was employed to optimize enzyme immobilization and evaluate the optimum temperature and pH for free and immobilized enzyme. The optimal immobilization conditions observed were 150 min incubation time, pH 4.76, and an enzyme/support ratio of 1282 U/g support. Optimal activity temperature for free and immobilized enzyme was found to be 68°C and 52°C, respectively. Optimal activity pH for free and immobilized lipase was pH 4.6 and 6.0, respectively. Lipase immobilization resulted in improved enzyme stability in the presence of nonionic detergents, at high temperatures, at acidic and neutral pH, and at high concentrations of organic solvents such as 2-propanol, methanol, and acetone.</abstract><cop>Cairo, Egypt</cop><pub>Hindawi Limiteds</pub><pmid>22315670</pmid><doi>10.1155/2012/329178</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| source | Wiley Online Library Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection; PubMed Central Open Access |
| subjects | acetone adsorption detergents enzyme stability immobilized enzymes isopropyl alcohol methanol Pseudozyma response surface methodology solvents temperature triacylglycerol lipase |
| title | Optimal Conditions for Continuous Immobilization of Pseudozyma hubeiensis (Strain HB85A) Lipase by Adsorption in a Packed-Bed Reactor by Response Surface Methodology |
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