Improved activity of a lipase by vacuum drying on to a hydrophobic microporous support
Lipase from Rhizopus arrhizus was immobilized by physical adsorption on hydrophobic microporous polypropylene supports. The immobilized enzyme catalyst was employed for the hydrolysis of palm kernel olein in the presence of n-hexane. The initial rate of lipolysis for vacuum dried immobilized lipase...
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| Veröffentlicht in: | Biotechnology techniques 1994-11, Vol.8 (11), p.827-830 |
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| container_title | Biotechnology techniques |
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| creator | Huang, F.C Ju, Y.H |
| description | Lipase from Rhizopus arrhizus was immobilized by physical adsorption on hydrophobic microporous polypropylene supports. The immobilized enzyme catalyst was employed for the hydrolysis of palm kernel olein in the presence of n-hexane. The initial rate of lipolysis for vacuum dried immobilized lipase is nearly double that of air dried. The initial rate of lipolysis declines with increase of drying time. Immobilized lipase clearly reveals a relatively high initial rate after 30 days of storage at 4 degree C. Stability of the immobilized lipase in buffer could be enhanced up to three-fold that of the free lipase. |
| doi_str_mv | 10.1007/BF00152892 |
| format | Article |
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The immobilized enzyme catalyst was employed for the hydrolysis of palm kernel olein in the presence of n-hexane. The initial rate of lipolysis for vacuum dried immobilized lipase is nearly double that of air dried. The initial rate of lipolysis declines with increase of drying time. Immobilized lipase clearly reveals a relatively high initial rate after 30 days of storage at 4 degree C. Stability of the immobilized lipase in buffer could be enhanced up to three-fold that of the free lipase.</description><identifier>ISSN: 0951-208X</identifier><identifier>EISSN: 1573-6784</identifier><identifier>DOI: 10.1007/BF00152892</identifier><identifier>CODEN: BTECE6</identifier><language>eng</language><publisher>London: Chapman and Hall</publisher><subject>Biological and medical sciences ; Biotechnology ; enzyme activity ; Enzyme engineering ; Fundamental and applied biological sciences. Psychology ; hydrolysis ; immobilization ; Immobilization of enzymes and other molecules ; Immobilization techniques ; immobilized enzymes ; Methods. Procedures. Technologies ; Miscellaneous ; olein ; palm oils ; polypropylenes ; Rhizopus arrhizus ; triacylglycerol lipase ; vacuum drying</subject><ispartof>Biotechnology techniques, 1994-11, Vol.8 (11), p.827-830</ispartof><rights>1995 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c349t-e2227818ce3a0db752ad0f923319e1e66de21e5ad3c4029295c8d6561efa7d1d3</citedby><cites>FETCH-LOGICAL-c349t-e2227818ce3a0db752ad0f923319e1e66de21e5ad3c4029295c8d6561efa7d1d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27915,27916</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3325863$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Huang, F.C</creatorcontrib><creatorcontrib>Ju, Y.H</creatorcontrib><title>Improved activity of a lipase by vacuum drying on to a hydrophobic microporous support</title><title>Biotechnology techniques</title><description>Lipase from Rhizopus arrhizus was immobilized by physical adsorption on hydrophobic microporous polypropylene supports. The immobilized enzyme catalyst was employed for the hydrolysis of palm kernel olein in the presence of n-hexane. The initial rate of lipolysis for vacuum dried immobilized lipase is nearly double that of air dried. The initial rate of lipolysis declines with increase of drying time. Immobilized lipase clearly reveals a relatively high initial rate after 30 days of storage at 4 degree C. Stability of the immobilized lipase in buffer could be enhanced up to three-fold that of the free lipase.</description><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>enzyme activity</subject><subject>Enzyme engineering</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>hydrolysis</subject><subject>immobilization</subject><subject>Immobilization of enzymes and other molecules</subject><subject>Immobilization techniques</subject><subject>immobilized enzymes</subject><subject>Methods. Procedures. Technologies</subject><subject>Miscellaneous</subject><subject>olein</subject><subject>palm oils</subject><subject>polypropylenes</subject><subject>Rhizopus arrhizus</subject><subject>triacylglycerol lipase</subject><subject>vacuum drying</subject><issn>0951-208X</issn><issn>1573-6784</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><recordid>eNpFkFFLwzAUhYMoOKcv_gHzID4I1ZukadNHHU4HAx904lvJknSLtE1N2kH_vZENfboH7ncP5x6ELgncEYD8_nEOQDgVBT1CE8JzlmS5SI_RBApOEgri8xSdhfAFAAwgnaCPRdN5tzMaS9Xbne1H7CoscW07GQxej3gn1TA0WPvRthvsWty7uN-O2rtu69ZW4caqqJ13Q8Bh6KLqz9FJJetgLg5zilbzp_fZS7J8fV7MHpaJYmnRJ4ZSmgsilGES9DrnVGqoCsoYKQwxWaYNJYZLzVQKtKAFV0JnPCOmkrkmmk3Rzd43PvE9mNCXjQ3K1LVsTYxTkiwnPIuGU3S7B2PUELypys7bRvqxJFD-Vlf-Vxfh64OrDErWlZetsuHvgjHKRcYidrXHKulKufERWb1RIAxIWgiIX_wA9vR3CA</recordid><startdate>19941101</startdate><enddate>19941101</enddate><creator>Huang, F.C</creator><creator>Ju, Y.H</creator><general>Chapman and Hall</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>19941101</creationdate><title>Improved activity of a lipase by vacuum drying on to a hydrophobic microporous support</title><author>Huang, F.C ; Ju, Y.H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c349t-e2227818ce3a0db752ad0f923319e1e66de21e5ad3c4029295c8d6561efa7d1d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>enzyme activity</topic><topic>Enzyme engineering</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>hydrolysis</topic><topic>immobilization</topic><topic>Immobilization of enzymes and other molecules</topic><topic>Immobilization techniques</topic><topic>immobilized enzymes</topic><topic>Methods. Procedures. Technologies</topic><topic>Miscellaneous</topic><topic>olein</topic><topic>palm oils</topic><topic>polypropylenes</topic><topic>Rhizopus arrhizus</topic><topic>triacylglycerol lipase</topic><topic>vacuum drying</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Huang, F.C</creatorcontrib><creatorcontrib>Ju, Y.H</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Biotechnology techniques</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Huang, F.C</au><au>Ju, Y.H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Improved activity of a lipase by vacuum drying on to a hydrophobic microporous support</atitle><jtitle>Biotechnology techniques</jtitle><date>1994-11-01</date><risdate>1994</risdate><volume>8</volume><issue>11</issue><spage>827</spage><epage>830</epage><pages>827-830</pages><issn>0951-208X</issn><eissn>1573-6784</eissn><coden>BTECE6</coden><abstract>Lipase from Rhizopus arrhizus was immobilized by physical adsorption on hydrophobic microporous polypropylene supports. The immobilized enzyme catalyst was employed for the hydrolysis of palm kernel olein in the presence of n-hexane. The initial rate of lipolysis for vacuum dried immobilized lipase is nearly double that of air dried. The initial rate of lipolysis declines with increase of drying time. Immobilized lipase clearly reveals a relatively high initial rate after 30 days of storage at 4 degree C. Stability of the immobilized lipase in buffer could be enhanced up to three-fold that of the free lipase.</abstract><cop>London</cop><pub>Chapman and Hall</pub><doi>10.1007/BF00152892</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0951-208X |
| ispartof | Biotechnology techniques, 1994-11, Vol.8 (11), p.827-830 |
| issn | 0951-208X 1573-6784 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_16715692 |
| source | Springer Nature - Complete Springer Journals |
| subjects | Biological and medical sciences Biotechnology enzyme activity Enzyme engineering Fundamental and applied biological sciences. Psychology hydrolysis immobilization Immobilization of enzymes and other molecules Immobilization techniques immobilized enzymes Methods. Procedures. Technologies Miscellaneous olein palm oils polypropylenes Rhizopus arrhizus triacylglycerol lipase vacuum drying |
| title | Improved activity of a lipase by vacuum drying on to a hydrophobic microporous support |
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