Immobilization of Aspergillus oryzae tannase and properties of the immobilized enzyme
Tannase enzyme from Aspergillus oryzae was immobilized on various carriers by different methods. The immobilized enzyme on chitosan with a bifunctional agent (glutaraldehyde) had the highest activity. The catalytic properties and stability of the immobilized tannase were compared with the correspond...
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| Veröffentlicht in: | Journal of applied microbiology 1999-07, Vol.87 (1), p.108-114 |
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| container_title | Journal of applied microbiology |
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| creator | Abdel-Naby, M.A Sherif, A.A El-Tanash, A.B Mankarios, A.T |
| description | Tannase enzyme from Aspergillus oryzae was immobilized on various carriers by different methods. The immobilized enzyme on chitosan with a bifunctional agent (glutaraldehyde) had the highest activity. The catalytic properties and stability of the immobilized tannase were compared with the corresponding free enzyme. The bound enzyme retained 20(.)3% of the original specific activity exhibited by the free enzyme. The optimum pH of the immobilized enzyme was shifted to a more acidic range compared with the free enzyme. The optimum temperature of the reaction was determined to be 40 degrees C for the free enzyme and 55 degrees C for the immobilized form. The stability at low pH, as well as thermal stability, were significantly improved by the immobilization process. The immobilized enzyme exhibited mass transfer limitation as reflected by a higher apparent K(m) value and a lower energy of activation. The immobilized enzyme retained about 85% of the initial catalytic activity, even after being used 17 times. |
| doi_str_mv | 10.1046/j.1365-2672.1999.00799.x |
| format | Article |
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The immobilized enzyme on chitosan with a bifunctional agent (glutaraldehyde) had the highest activity. The catalytic properties and stability of the immobilized tannase were compared with the corresponding free enzyme. The bound enzyme retained 20(.)3% of the original specific activity exhibited by the free enzyme. The optimum pH of the immobilized enzyme was shifted to a more acidic range compared with the free enzyme. The optimum temperature of the reaction was determined to be 40 degrees C for the free enzyme and 55 degrees C for the immobilized form. The stability at low pH, as well as thermal stability, were significantly improved by the immobilization process. The immobilized enzyme exhibited mass transfer limitation as reflected by a higher apparent K(m) value and a lower energy of activation. The immobilized enzyme retained about 85% of the initial catalytic activity, even after being used 17 times.</description><identifier>ISSN: 1364-5072</identifier><identifier>EISSN: 1365-2672</identifier><identifier>DOI: 10.1046/j.1365-2672.1999.00799.x</identifier><identifier>CODEN: JAMIFK</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Aspergillus oryzae ; Biological and medical sciences ; Biological Sciences ; Biotechnology ; food microbiology ; food processing ; Fundamental and applied biological sciences. Psychology ; Immobilization of enzymes and other molecules ; Immobilization techniques ; Methods. Procedures. Technologies ; nonfood animal products ; plant biochemistry ; plant physiology</subject><ispartof>Journal of applied microbiology, 1999-07, Vol.87 (1), p.108-114</ispartof><rights>1999 INIST-CNRS</rights><rights>Copyright Blackwell Science Ltd. 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The immobilized enzyme on chitosan with a bifunctional agent (glutaraldehyde) had the highest activity. The catalytic properties and stability of the immobilized tannase were compared with the corresponding free enzyme. The bound enzyme retained 20(.)3% of the original specific activity exhibited by the free enzyme. The optimum pH of the immobilized enzyme was shifted to a more acidic range compared with the free enzyme. The optimum temperature of the reaction was determined to be 40 degrees C for the free enzyme and 55 degrees C for the immobilized form. The stability at low pH, as well as thermal stability, were significantly improved by the immobilization process. The immobilized enzyme exhibited mass transfer limitation as reflected by a higher apparent K(m) value and a lower energy of activation. The immobilized enzyme retained about 85% of the initial catalytic activity, even after being used 17 times.</description><subject>Aspergillus oryzae</subject><subject>Biological and medical sciences</subject><subject>Biological Sciences</subject><subject>Biotechnology</subject><subject>food microbiology</subject><subject>food processing</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immobilization of enzymes and other molecules</subject><subject>Immobilization techniques</subject><subject>Methods. Procedures. Technologies</subject><subject>nonfood animal products</subject><subject>plant biochemistry</subject><subject>plant physiology</subject><issn>1364-5072</issn><issn>1365-2672</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNqNkUtP3DAUhSPUSqWU31ALIXYZ_IodS92MEE9RdVFmbTn2DXiUxIOdEcz8ehwGisSqG_tK9zvnXh8XBSJ4RjAXp8sZYaIqqZB0RpRSM4xlPp_3iv1_jS-vNS8rLOm34ntKS4wJw5XYLxbXfR8a3_mtGX0YUGjRPK0g3vuuWycU4mZrAI1mGEwCZAaHVjHk_ughTfD4AMi_W4BDMGw3PfwovramS3D4dh8Ui4vzu7Or8vbP5fXZ_La0leSqZNIqYmgtVMMZ5bVzNTcchFDYOdZK1zhhXUNsS3glKGBliJOCWgLYNvkJB8XJzjcv9biGNOreJwtdZwYI66SJZFjxus7g0SdwGdZxyLtpyqiqGGeTW72DbAwpRWj1KvrexI0mWE9h66WeMtVTpnoKW7-GrZ-z9PjN3yRrujaawfr0oVeYS4Iz9muHPfkONv9tr2_mv3OR5T938tYEbe5jnrD4S6evpIoRUWP2Ap_xm8w</recordid><startdate>199907</startdate><enddate>199907</enddate><creator>Abdel-Naby, M.A</creator><creator>Sherif, A.A</creator><creator>El-Tanash, A.B</creator><creator>Mankarios, A.T</creator><general>Blackwell Science Ltd</general><general>Blackwell Science</general><general>Oxford University Press</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>7TM</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>199907</creationdate><title>Immobilization of Aspergillus oryzae tannase and properties of the immobilized enzyme</title><author>Abdel-Naby, M.A ; Sherif, A.A ; El-Tanash, A.B ; Mankarios, A.T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5749-37c91a2869b43248dd84a4e6690dd3f7dbd6cdb1cf14562e09a1d762c1e0cb013</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Aspergillus oryzae</topic><topic>Biological and medical sciences</topic><topic>Biological Sciences</topic><topic>Biotechnology</topic><topic>food microbiology</topic><topic>food processing</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Immobilization of enzymes and other molecules</topic><topic>Immobilization techniques</topic><topic>Methods. Procedures. Technologies</topic><topic>nonfood animal products</topic><topic>plant biochemistry</topic><topic>plant physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Abdel-Naby, M.A</creatorcontrib><creatorcontrib>Sherif, A.A</creatorcontrib><creatorcontrib>El-Tanash, A.B</creatorcontrib><creatorcontrib>Mankarios, A.T</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Journal of applied microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Abdel-Naby, M.A</au><au>Sherif, A.A</au><au>El-Tanash, A.B</au><au>Mankarios, A.T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immobilization of Aspergillus oryzae tannase and properties of the immobilized enzyme</atitle><jtitle>Journal of applied microbiology</jtitle><date>1999-07</date><risdate>1999</risdate><volume>87</volume><issue>1</issue><spage>108</spage><epage>114</epage><pages>108-114</pages><issn>1364-5072</issn><eissn>1365-2672</eissn><coden>JAMIFK</coden><abstract>Tannase enzyme from Aspergillus oryzae was immobilized on various carriers by different methods. The immobilized enzyme on chitosan with a bifunctional agent (glutaraldehyde) had the highest activity. The catalytic properties and stability of the immobilized tannase were compared with the corresponding free enzyme. The bound enzyme retained 20(.)3% of the original specific activity exhibited by the free enzyme. The optimum pH of the immobilized enzyme was shifted to a more acidic range compared with the free enzyme. The optimum temperature of the reaction was determined to be 40 degrees C for the free enzyme and 55 degrees C for the immobilized form. The stability at low pH, as well as thermal stability, were significantly improved by the immobilization process. The immobilized enzyme exhibited mass transfer limitation as reflected by a higher apparent K(m) value and a lower energy of activation. The immobilized enzyme retained about 85% of the initial catalytic activity, even after being used 17 times.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><doi>10.1046/j.1365-2672.1999.00799.x</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of applied microbiology, 1999-07, Vol.87 (1), p.108-114 |
| issn | 1364-5072 1365-2672 |
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| source | Access via Wiley Online Library; Oxford University Press Journals All Titles (1996-Current) |
| subjects | Aspergillus oryzae Biological and medical sciences Biological Sciences Biotechnology food microbiology food processing Fundamental and applied biological sciences. Psychology Immobilization of enzymes and other molecules Immobilization techniques Methods. Procedures. Technologies nonfood animal products plant biochemistry plant physiology |
| title | Immobilization of Aspergillus oryzae tannase and properties of the immobilized enzyme |
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