Bioconversion of trans-cinnamic acid to l-phenylalanine by l-phenylalanine ammonia-lyase of Rhodotorula glutinis: Parameters and kinetics
The kinetics of the bioconversion of trans-cinnamic acid to l-phenylalanine by the l-phenylalanine ammonialyase (PAL) enzyme of resting cells of Rhodotorula glutinis have been studied under the optimum bioreaction conditions determined. The optimum pH, temperature, ammonia concentration, and biocata...
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| Veröffentlicht in: | Enzyme and microbial technology 1995, Vol.17 (5), p.445-452 |
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| creator | Takaç, Serpil Akay, Bülent Özdamar, Tunçer H. |
| description | The kinetics of the bioconversion of
trans-cinnamic acid to
l-phenylalanine by the
l-phenylalanine ammonialyase (PAL) enzyme of resting cells of
Rhodotorula glutinis have been studied under the optimum bioreaction conditions determined. The optimum pH, temperature, ammonia concentration, and biocatalyst loading were 10.5, 30°C, 8
m, and ca. 2 (w/w), respectively. Among various chemicals, sodium glutamate and penicillin were found to increase the PAL activity of the cells. A maximum concentration of 76.18 m
m (12.57 g dm
−3)
l-phenylalanine was maintained from 100 m
m (14.8 g dm
−3)
trans-cinnamic acid after 104 h of residence time in the fed-batch operation of the bioreactor.
trans-Cinnamic acid concentrations higher than 30–50 m
m were shown to cause the substrate inhibition, besides the mixed-type inhibition effect of the chloride ions. Mechanistic bioreaction rate equations that incorporate separately the inhibition effects of the
trans-cinnamic acid and chloride ions, and the activation effect of sodium glutamate, were proposed and the kinetic parameters of the models were calculated. |
| doi_str_mv | 10.1016/0141-0229(94)00072-Y |
| format | Article |
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trans-cinnamic acid to
l-phenylalanine by the
l-phenylalanine ammonialyase (PAL) enzyme of resting cells of
Rhodotorula glutinis have been studied under the optimum bioreaction conditions determined. The optimum pH, temperature, ammonia concentration, and biocatalyst loading were 10.5, 30°C, 8
m, and ca. 2 (w/w), respectively. Among various chemicals, sodium glutamate and penicillin were found to increase the PAL activity of the cells. A maximum concentration of 76.18 m
m (12.57 g dm
−3)
l-phenylalanine was maintained from 100 m
m (14.8 g dm
−3)
trans-cinnamic acid after 104 h of residence time in the fed-batch operation of the bioreactor.
trans-Cinnamic acid concentrations higher than 30–50 m
m were shown to cause the substrate inhibition, besides the mixed-type inhibition effect of the chloride ions. Mechanistic bioreaction rate equations that incorporate separately the inhibition effects of the
trans-cinnamic acid and chloride ions, and the activation effect of sodium glutamate, were proposed and the kinetic parameters of the models were calculated.</description><identifier>ISSN: 0141-0229</identifier><identifier>EISSN: 1879-0909</identifier><identifier>DOI: 10.1016/0141-0229(94)00072-Y</identifier><identifier>CODEN: EMTED2</identifier><language>eng</language><publisher>Amsterdam: Elsevier Inc</publisher><subject>bioconversion of trans-cinnamic acid ; Bioconversions. Hemisynthesis ; Biological and medical sciences ; Biotechnology ; Fundamental and applied biological sciences. Psychology ; kinetic models ; l-phenylalanine ammonia-lyase (PAL) enzyme ; l-Phenylalanine production ; Methods. Procedures. Technologies ; Rhodotorula glutinis</subject><ispartof>Enzyme and microbial technology, 1995, Vol.17 (5), p.445-452</ispartof><rights>1995</rights><rights>1995 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c400t-5d7a8f3bad815eff6ccabf338e78c988a99e13bc9ee21567cc541d95f93392e3</citedby><cites>FETCH-LOGICAL-c400t-5d7a8f3bad815eff6ccabf338e78c988a99e13bc9ee21567cc541d95f93392e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0141-0229(94)00072-Y$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3549,4023,27922,27923,27924,45994</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3518140$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Takaç, Serpil</creatorcontrib><creatorcontrib>Akay, Bülent</creatorcontrib><creatorcontrib>Özdamar, Tunçer H.</creatorcontrib><title>Bioconversion of trans-cinnamic acid to l-phenylalanine by l-phenylalanine ammonia-lyase of Rhodotorula glutinis: Parameters and kinetics</title><title>Enzyme and microbial technology</title><description>The kinetics of the bioconversion of
trans-cinnamic acid to
l-phenylalanine by the
l-phenylalanine ammonialyase (PAL) enzyme of resting cells of
Rhodotorula glutinis have been studied under the optimum bioreaction conditions determined. The optimum pH, temperature, ammonia concentration, and biocatalyst loading were 10.5, 30°C, 8
m, and ca. 2 (w/w), respectively. Among various chemicals, sodium glutamate and penicillin were found to increase the PAL activity of the cells. A maximum concentration of 76.18 m
m (12.57 g dm
−3)
l-phenylalanine was maintained from 100 m
m (14.8 g dm
−3)
trans-cinnamic acid after 104 h of residence time in the fed-batch operation of the bioreactor.
trans-Cinnamic acid concentrations higher than 30–50 m
m were shown to cause the substrate inhibition, besides the mixed-type inhibition effect of the chloride ions. Mechanistic bioreaction rate equations that incorporate separately the inhibition effects of the
trans-cinnamic acid and chloride ions, and the activation effect of sodium glutamate, were proposed and the kinetic parameters of the models were calculated.</description><subject>bioconversion of trans-cinnamic acid</subject><subject>Bioconversions. Hemisynthesis</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>kinetic models</subject><subject>l-phenylalanine ammonia-lyase (PAL) enzyme</subject><subject>l-Phenylalanine production</subject><subject>Methods. Procedures. Technologies</subject><subject>Rhodotorula glutinis</subject><issn>0141-0229</issn><issn>1879-0909</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNp9kMGKFDEQhoMoOK6-gYccRPQQTbrT0x0PwrrsqrCgyF72FGqqK240nYxJZmEewbc24yx7ETwVFN__F_Ux9lzJN0qq9VuptBKy68wro19LKcdOXD9gKzWNRkgjzUO2ukcesyel_GiQ0lqu2O8PPmGKt5SLT5Enx2uGWAT6GGHxyAH9zGviQWxvKO4DBIg-Et_s_1nBsqToQYQ9FDpUfbtJc6op7wLw72FXffTlHf8KGRaq7SKHOPOfLVo9lqfskYNQ6NndPGFXF-dXZ5_E5ZePn89OLwVqKasY5hEm129gntRAzq0RYeP6fqJxQjNNYAypfoOGqFPDekQctJrN4Ezfm476E_byWLvN6deOSrWLL0ih_UBpV6wa5SC7UTdQH0HMqZRMzm6zXyDvrZL2oN0enNqDU2u0_avdXrfYi7t-KAjBNZvoy322H9SktGzY-yNG7dVbT9kW9BSRZp8Jq52T__-dP6fzmgc</recordid><startdate>1995</startdate><enddate>1995</enddate><creator>Takaç, Serpil</creator><creator>Akay, Bülent</creator><creator>Özdamar, Tunçer H.</creator><general>Elsevier Inc</general><general>Elsevier Science</general><scope>IQODW</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></search><sort><creationdate>1995</creationdate><title>Bioconversion of trans-cinnamic acid to l-phenylalanine by l-phenylalanine ammonia-lyase of Rhodotorula glutinis: Parameters and kinetics</title><author>Takaç, Serpil ; Akay, Bülent ; Özdamar, Tunçer H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c400t-5d7a8f3bad815eff6ccabf338e78c988a99e13bc9ee21567cc541d95f93392e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>bioconversion of trans-cinnamic acid</topic><topic>Bioconversions. Hemisynthesis</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>kinetic models</topic><topic>l-phenylalanine ammonia-lyase (PAL) enzyme</topic><topic>l-Phenylalanine production</topic><topic>Methods. Procedures. Technologies</topic><topic>Rhodotorula glutinis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Takaç, Serpil</creatorcontrib><creatorcontrib>Akay, Bülent</creatorcontrib><creatorcontrib>Özdamar, Tunçer H.</creatorcontrib><collection>Pascal-Francis</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><jtitle>Enzyme and microbial technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Takaç, Serpil</au><au>Akay, Bülent</au><au>Özdamar, Tunçer H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bioconversion of trans-cinnamic acid to l-phenylalanine by l-phenylalanine ammonia-lyase of Rhodotorula glutinis: Parameters and kinetics</atitle><jtitle>Enzyme and microbial technology</jtitle><date>1995</date><risdate>1995</risdate><volume>17</volume><issue>5</issue><spage>445</spage><epage>452</epage><pages>445-452</pages><issn>0141-0229</issn><eissn>1879-0909</eissn><coden>EMTED2</coden><abstract>The kinetics of the bioconversion of
trans-cinnamic acid to
l-phenylalanine by the
l-phenylalanine ammonialyase (PAL) enzyme of resting cells of
Rhodotorula glutinis have been studied under the optimum bioreaction conditions determined. The optimum pH, temperature, ammonia concentration, and biocatalyst loading were 10.5, 30°C, 8
m, and ca. 2 (w/w), respectively. Among various chemicals, sodium glutamate and penicillin were found to increase the PAL activity of the cells. A maximum concentration of 76.18 m
m (12.57 g dm
−3)
l-phenylalanine was maintained from 100 m
m (14.8 g dm
−3)
trans-cinnamic acid after 104 h of residence time in the fed-batch operation of the bioreactor.
trans-Cinnamic acid concentrations higher than 30–50 m
m were shown to cause the substrate inhibition, besides the mixed-type inhibition effect of the chloride ions. Mechanistic bioreaction rate equations that incorporate separately the inhibition effects of the
trans-cinnamic acid and chloride ions, and the activation effect of sodium glutamate, were proposed and the kinetic parameters of the models were calculated.</abstract><cop>Amsterdam</cop><pub>Elsevier Inc</pub><doi>10.1016/0141-0229(94)00072-Y</doi><tpages>8</tpages></addata></record> |
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| ispartof | Enzyme and microbial technology, 1995, Vol.17 (5), p.445-452 |
| issn | 0141-0229 1879-0909 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_17050274 |
| source | Elsevier ScienceDirect Journals Complete - AutoHoldings |
| subjects | bioconversion of trans-cinnamic acid Bioconversions. Hemisynthesis Biological and medical sciences Biotechnology Fundamental and applied biological sciences. Psychology kinetic models l-phenylalanine ammonia-lyase (PAL) enzyme l-Phenylalanine production Methods. Procedures. Technologies Rhodotorula glutinis |
| title | Bioconversion of trans-cinnamic acid to l-phenylalanine by l-phenylalanine ammonia-lyase of Rhodotorula glutinis: Parameters and kinetics |
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