Mycelium-bound carboxylesterase from Aspergillus oryzae: an efficient catalyst for acetylation in organic solvent
Dry mycelium of a strain of Aspergillus oryzae efficiently catalyzed the esterification between free acetic acid and primary alcohols (geraniol and ethanol) in organic solvent. The growth conditions to obtain high activity of mycelium-bound enzymes were firstly evaluated. A medium containing Tween 8...
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| Veröffentlicht in: | Enzyme and microbial technology 2000-11, Vol.27 (8), p.626-630 |
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| creator | Molinari, F. Gandolfi, R. Converti, A. Zilli, M. |
| description | Dry mycelium of a strain of
Aspergillus oryzae efficiently catalyzed the esterification between free acetic acid and primary alcohols (geraniol and ethanol) in organic solvent. The growth conditions to obtain high activity of mycelium-bound enzymes were firstly evaluated. A medium containing Tween 80 as carbon source furnished mycelium with the highest activity in the hydrolysis of α-naphthyl esters (α-N-acetate, butyrate, caprylate). Dry mycelium was employed to select suited conditions for an efficient acetylation of ethanol and geraniol in heptane. Maximum productions were obtained using 30 g l
−
1 of lyophilized cells: 12.4 g l
−
1 of geranyl acetate were produced at 80°C starting from 75 mM geraniol and acetic acid (84% molar conversion) and 4.1 g l
−
1 of ethyl acetate at 50°C from 50 mM ethanol and acetic acid (94% molar conversion) after 24 h. The stability of the mycelium-bound carboxylesterases are notable since only 10–30% loss of activity was observed after 14 days at temperatures between 30 and 50°C. |
| doi_str_mv | 10.1016/S0141-0229(00)00263-5 |
| format | Article |
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Aspergillus oryzae efficiently catalyzed the esterification between free acetic acid and primary alcohols (geraniol and ethanol) in organic solvent. The growth conditions to obtain high activity of mycelium-bound enzymes were firstly evaluated. A medium containing Tween 80 as carbon source furnished mycelium with the highest activity in the hydrolysis of α-naphthyl esters (α-N-acetate, butyrate, caprylate). Dry mycelium was employed to select suited conditions for an efficient acetylation of ethanol and geraniol in heptane. Maximum productions were obtained using 30 g l
−
1 of lyophilized cells: 12.4 g l
−
1 of geranyl acetate were produced at 80°C starting from 75 mM geraniol and acetic acid (84% molar conversion) and 4.1 g l
−
1 of ethyl acetate at 50°C from 50 mM ethanol and acetic acid (94% molar conversion) after 24 h. The stability of the mycelium-bound carboxylesterases are notable since only 10–30% loss of activity was observed after 14 days at temperatures between 30 and 50°C.</description><identifier>ISSN: 0141-0229</identifier><identifier>EISSN: 1879-0909</identifier><identifier>DOI: 10.1016/S0141-0229(00)00263-5</identifier><identifier>PMID: 11024527</identifier><identifier>CODEN: EMTED2</identifier><language>eng</language><publisher>Amsterdam: Elsevier Inc</publisher><subject>Acetic acid ; Acetylation ; alcohols ; Aspergillus oryzae ; Biocatalysts ; Bioconversions. Hemisynthesis ; Biological and medical sciences ; Biotechnology ; Biotransformation ; Enzyme engineering ; Esterase ; Esterification ; ethyl acetate ; Fermentation ; Fundamental and applied biological sciences. Psychology ; geraniol ; geranyl acetate ; Hydrolysis ; Lipase ; Methods. Procedures. Technologies ; Organic solvent ; Organic solvents ; Production of selected enzymes</subject><ispartof>Enzyme and microbial technology, 2000-11, Vol.27 (8), p.626-630</ispartof><rights>2000 Elsevier Science Inc.</rights><rights>2001 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c519t-540db298b90b770a9303a837b0f5d45ad8f989b9a5cc819b44499a198e189b803</citedby><cites>FETCH-LOGICAL-c519t-540db298b90b770a9303a837b0f5d45ad8f989b9a5cc819b44499a198e189b803</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0141-0229(00)00263-5$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=800907$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11024527$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Molinari, F.</creatorcontrib><creatorcontrib>Gandolfi, R.</creatorcontrib><creatorcontrib>Converti, A.</creatorcontrib><creatorcontrib>Zilli, M.</creatorcontrib><title>Mycelium-bound carboxylesterase from Aspergillus oryzae: an efficient catalyst for acetylation in organic solvent</title><title>Enzyme and microbial technology</title><addtitle>Enzyme Microb Technol</addtitle><description>Dry mycelium of a strain of
Aspergillus oryzae efficiently catalyzed the esterification between free acetic acid and primary alcohols (geraniol and ethanol) in organic solvent. The growth conditions to obtain high activity of mycelium-bound enzymes were firstly evaluated. A medium containing Tween 80 as carbon source furnished mycelium with the highest activity in the hydrolysis of α-naphthyl esters (α-N-acetate, butyrate, caprylate). Dry mycelium was employed to select suited conditions for an efficient acetylation of ethanol and geraniol in heptane. Maximum productions were obtained using 30 g l
−
1 of lyophilized cells: 12.4 g l
−
1 of geranyl acetate were produced at 80°C starting from 75 mM geraniol and acetic acid (84% molar conversion) and 4.1 g l
−
1 of ethyl acetate at 50°C from 50 mM ethanol and acetic acid (94% molar conversion) after 24 h. The stability of the mycelium-bound carboxylesterases are notable since only 10–30% loss of activity was observed after 14 days at temperatures between 30 and 50°C.</description><subject>Acetic acid</subject><subject>Acetylation</subject><subject>alcohols</subject><subject>Aspergillus oryzae</subject><subject>Biocatalysts</subject><subject>Bioconversions. Hemisynthesis</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Biotransformation</subject><subject>Enzyme engineering</subject><subject>Esterase</subject><subject>Esterification</subject><subject>ethyl acetate</subject><subject>Fermentation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>geraniol</subject><subject>geranyl acetate</subject><subject>Hydrolysis</subject><subject>Lipase</subject><subject>Methods. Procedures. Technologies</subject><subject>Organic solvent</subject><subject>Organic solvents</subject><subject>Production of selected enzymes</subject><issn>0141-0229</issn><issn>1879-0909</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNqFkU2LFDEQhoMo7rj6E5SAIOuhtZJOphMvsix-wYoH9Ryq08kSSXdmk-7F9teb2RnWm3sKFM9blaqHkOcM3jBg27ffgQnWAOf6DOA1AN-2jXxANkx1ugEN-iHZ3CEn5EkpvwBqQcBjcsIYcCF5tyHXX1frYljGpk_LNFCLuU-_1-jK7DIWR31OIz0vO5evQoxLoSmvf9C9ozhR532wwU1zjc0Y1zJTnzJF6-Y14hzSRMNUA1c4BUtLijeVfUoeeYzFPTu-p-Tnxw8_Lj43l98-fbk4v2ysZHpupICh51r1GvquA9QttKjargcvByFxUF4r3WuU1iqmeyGE1si0cqyWFbSn5NWh7y6n66XuY8ZQ6q4RJ5eWYjgTXG3ZtoJn_wWZkroVXMvu3p6sU6KDVlRQHkCbUynZebPLYcS8GgZm78_c-jN7OQbA3PozsuZeHAcs_eiGf6mjsAq8PAJYLEafcbKh3HEKqvo99f5AuXrgm-CyKXtP1g0hOzubIYV7PvIX-vO3SQ</recordid><startdate>20001101</startdate><enddate>20001101</enddate><creator>Molinari, F.</creator><creator>Gandolfi, R.</creator><creator>Converti, A.</creator><creator>Zilli, M.</creator><general>Elsevier Inc</general><general>Elsevier Science</general><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20001101</creationdate><title>Mycelium-bound carboxylesterase from Aspergillus oryzae: an efficient catalyst for acetylation in organic solvent</title><author>Molinari, F. ; Gandolfi, R. ; Converti, A. ; Zilli, M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c519t-540db298b90b770a9303a837b0f5d45ad8f989b9a5cc819b44499a198e189b803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Acetic acid</topic><topic>Acetylation</topic><topic>alcohols</topic><topic>Aspergillus oryzae</topic><topic>Biocatalysts</topic><topic>Bioconversions. Hemisynthesis</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Biotransformation</topic><topic>Enzyme engineering</topic><topic>Esterase</topic><topic>Esterification</topic><topic>ethyl acetate</topic><topic>Fermentation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>geraniol</topic><topic>geranyl acetate</topic><topic>Hydrolysis</topic><topic>Lipase</topic><topic>Methods. Procedures. Technologies</topic><topic>Organic solvent</topic><topic>Organic solvents</topic><topic>Production of selected enzymes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Molinari, F.</creatorcontrib><creatorcontrib>Gandolfi, R.</creatorcontrib><creatorcontrib>Converti, A.</creatorcontrib><creatorcontrib>Zilli, M.</creatorcontrib><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</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>MEDLINE - Academic</collection><jtitle>Enzyme and microbial technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Molinari, F.</au><au>Gandolfi, R.</au><au>Converti, A.</au><au>Zilli, M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mycelium-bound carboxylesterase from Aspergillus oryzae: an efficient catalyst for acetylation in organic solvent</atitle><jtitle>Enzyme and microbial technology</jtitle><addtitle>Enzyme Microb Technol</addtitle><date>2000-11-01</date><risdate>2000</risdate><volume>27</volume><issue>8</issue><spage>626</spage><epage>630</epage><pages>626-630</pages><issn>0141-0229</issn><eissn>1879-0909</eissn><coden>EMTED2</coden><abstract>Dry mycelium of a strain of
Aspergillus oryzae efficiently catalyzed the esterification between free acetic acid and primary alcohols (geraniol and ethanol) in organic solvent. The growth conditions to obtain high activity of mycelium-bound enzymes were firstly evaluated. A medium containing Tween 80 as carbon source furnished mycelium with the highest activity in the hydrolysis of α-naphthyl esters (α-N-acetate, butyrate, caprylate). Dry mycelium was employed to select suited conditions for an efficient acetylation of ethanol and geraniol in heptane. Maximum productions were obtained using 30 g l
−
1 of lyophilized cells: 12.4 g l
−
1 of geranyl acetate were produced at 80°C starting from 75 mM geraniol and acetic acid (84% molar conversion) and 4.1 g l
−
1 of ethyl acetate at 50°C from 50 mM ethanol and acetic acid (94% molar conversion) after 24 h. The stability of the mycelium-bound carboxylesterases are notable since only 10–30% loss of activity was observed after 14 days at temperatures between 30 and 50°C.</abstract><cop>Amsterdam</cop><pub>Elsevier Inc</pub><pmid>11024527</pmid><doi>10.1016/S0141-0229(00)00263-5</doi><tpages>5</tpages></addata></record> |
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| source | Elsevier ScienceDirect Journals Complete |
| subjects | Acetic acid Acetylation alcohols Aspergillus oryzae Biocatalysts Bioconversions. Hemisynthesis Biological and medical sciences Biotechnology Biotransformation Enzyme engineering Esterase Esterification ethyl acetate Fermentation Fundamental and applied biological sciences. Psychology geraniol geranyl acetate Hydrolysis Lipase Methods. Procedures. Technologies Organic solvent Organic solvents Production of selected enzymes |
| title | Mycelium-bound carboxylesterase from Aspergillus oryzae: an efficient catalyst for acetylation in organic solvent |
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