Enzymic resolution of dl-phenylglycine
An enzymic process of production of d- and l-phenylglycine is described. The unnatural amino acid dl-phenylglycine was synthesized from benzaldehyde and its dl- N-acetyl derivative obtained. Hog kidney acylase I, an amidohydrolase, was used as catalyst to hydrolyse enantiospecifically with 100% conv...
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| Veröffentlicht in: | Process biochemistry (1991) 2005-10, Vol.40 (10), p.3186-3189 |
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| container_title | Process biochemistry (1991) |
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| creator | Machado, Georgia D.C. Gomes, Marlito Antunes, O.A.C. Oestreicher, Enrique G. |
| description | An enzymic process of production of
d- and
l-phenylglycine is described. The unnatural amino acid
dl-phenylglycine was synthesized from benzaldehyde and its
dl-
N-acetyl derivative obtained. Hog kidney acylase I, an amidohydrolase, was used as catalyst to hydrolyse enantiospecifically with 100% conversion of
l-
N-acetylphenylglycine.
l-Phenylglycine was obtained with 36% isolated yield, with over 99% of enantiomeric excess. After acid hydrolysis using 48% HBr (v/v), unreacted
d-
N-acetylphenylglycine, yielded
d-phenylglycine in 26% isolated yield, with over 95% of enantiomeric excess. The present methodology constitutes a new preparative route to produce both enantiomers of phenylglycine and is suitable for industrial use. |
| doi_str_mv | 10.1016/j.procbio.2005.02.010 |
| format | Article |
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d- and
l-phenylglycine is described. The unnatural amino acid
dl-phenylglycine was synthesized from benzaldehyde and its
dl-
N-acetyl derivative obtained. Hog kidney acylase I, an amidohydrolase, was used as catalyst to hydrolyse enantiospecifically with 100% conversion of
l-
N-acetylphenylglycine.
l-Phenylglycine was obtained with 36% isolated yield, with over 99% of enantiomeric excess. After acid hydrolysis using 48% HBr (v/v), unreacted
d-
N-acetylphenylglycine, yielded
d-phenylglycine in 26% isolated yield, with over 95% of enantiomeric excess. The present methodology constitutes a new preparative route to produce both enantiomers of phenylglycine and is suitable for industrial use.</description><identifier>ISSN: 1359-5113</identifier><identifier>EISSN: 1873-3298</identifier><identifier>DOI: 10.1016/j.procbio.2005.02.010</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>Acylase I ; d-Phenylglycine ; dl- N-Acetylphenylglycine ; Enantiomeric resolution ; Ion exchange chromatography ; l-Phenylglycine</subject><ispartof>Process biochemistry (1991), 2005-10, Vol.40 (10), p.3186-3189</ispartof><rights>2005 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c408t-e597170a16d40aad9de2901d9eb1948bffaeb748ddb159e48132e1fe63be76f73</citedby><cites>FETCH-LOGICAL-c408t-e597170a16d40aad9de2901d9eb1948bffaeb748ddb159e48132e1fe63be76f73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1359511305001492$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids></links><search><creatorcontrib>Machado, Georgia D.C.</creatorcontrib><creatorcontrib>Gomes, Marlito</creatorcontrib><creatorcontrib>Antunes, O.A.C.</creatorcontrib><creatorcontrib>Oestreicher, Enrique G.</creatorcontrib><title>Enzymic resolution of dl-phenylglycine</title><title>Process biochemistry (1991)</title><description>An enzymic process of production of
d- and
l-phenylglycine is described. The unnatural amino acid
dl-phenylglycine was synthesized from benzaldehyde and its
dl-
N-acetyl derivative obtained. Hog kidney acylase I, an amidohydrolase, was used as catalyst to hydrolyse enantiospecifically with 100% conversion of
l-
N-acetylphenylglycine.
l-Phenylglycine was obtained with 36% isolated yield, with over 99% of enantiomeric excess. After acid hydrolysis using 48% HBr (v/v), unreacted
d-
N-acetylphenylglycine, yielded
d-phenylglycine in 26% isolated yield, with over 95% of enantiomeric excess. The present methodology constitutes a new preparative route to produce both enantiomers of phenylglycine and is suitable for industrial use.</description><subject>Acylase I</subject><subject>d-Phenylglycine</subject><subject>dl- N-Acetylphenylglycine</subject><subject>Enantiomeric resolution</subject><subject>Ion exchange chromatography</subject><subject>l-Phenylglycine</subject><issn>1359-5113</issn><issn>1873-3298</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNqFkMtOwzAQRS0EEqXwCUhddZcwY-dhrxCqykOqxAbWVmJPwFUaFztBCl9Pqnbf1czi3Cvdw9g9QoqAxcM23QdvaudTDpCnwFNAuGAzlKVIBFfycvpFrpIcUVyzmxi3AAIRYcaW6-5v3DmzCBR9O_TOdwvfLGyb7L-pG9uvdjSuo1t21VRtpLvTnbPP5_XH6jXZvL-8rZ42iclA9gnlqsQSKixsBlVllSWuAK2iGlUm66apqC4zaW2NuaJMouCEDRWiprJoSjFny2PvtOhnoNjrnYuG2rbqyA9Rc4Ul56jOg7IAkJxPYH4ETfAxBmr0PrhdFUaNoA_69Faf9OmDPg1cT_qm3OMxR9PcX0dBR-OoM2RdINNr692Zhn_F6nsW</recordid><startdate>20051001</startdate><enddate>20051001</enddate><creator>Machado, Georgia D.C.</creator><creator>Gomes, Marlito</creator><creator>Antunes, O.A.C.</creator><creator>Oestreicher, Enrique G.</creator><general>Elsevier Ltd</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7U5</scope><scope>8FD</scope><scope>F28</scope><scope>FR3</scope><scope>L7M</scope></search><sort><creationdate>20051001</creationdate><title>Enzymic resolution of dl-phenylglycine</title><author>Machado, Georgia D.C. ; Gomes, Marlito ; Antunes, O.A.C. ; Oestreicher, Enrique G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c408t-e597170a16d40aad9de2901d9eb1948bffaeb748ddb159e48132e1fe63be76f73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Acylase I</topic><topic>d-Phenylglycine</topic><topic>dl- N-Acetylphenylglycine</topic><topic>Enantiomeric resolution</topic><topic>Ion exchange chromatography</topic><topic>l-Phenylglycine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Machado, Georgia D.C.</creatorcontrib><creatorcontrib>Gomes, Marlito</creatorcontrib><creatorcontrib>Antunes, O.A.C.</creatorcontrib><creatorcontrib>Oestreicher, Enrique G.</creatorcontrib><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Process biochemistry (1991)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Machado, Georgia D.C.</au><au>Gomes, Marlito</au><au>Antunes, O.A.C.</au><au>Oestreicher, Enrique G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzymic resolution of dl-phenylglycine</atitle><jtitle>Process biochemistry (1991)</jtitle><date>2005-10-01</date><risdate>2005</risdate><volume>40</volume><issue>10</issue><spage>3186</spage><epage>3189</epage><pages>3186-3189</pages><issn>1359-5113</issn><eissn>1873-3298</eissn><abstract>An enzymic process of production of
d- and
l-phenylglycine is described. The unnatural amino acid
dl-phenylglycine was synthesized from benzaldehyde and its
dl-
N-acetyl derivative obtained. Hog kidney acylase I, an amidohydrolase, was used as catalyst to hydrolyse enantiospecifically with 100% conversion of
l-
N-acetylphenylglycine.
l-Phenylglycine was obtained with 36% isolated yield, with over 99% of enantiomeric excess. After acid hydrolysis using 48% HBr (v/v), unreacted
d-
N-acetylphenylglycine, yielded
d-phenylglycine in 26% isolated yield, with over 95% of enantiomeric excess. The present methodology constitutes a new preparative route to produce both enantiomers of phenylglycine and is suitable for industrial use.</abstract><pub>Elsevier Ltd</pub><doi>10.1016/j.procbio.2005.02.010</doi><tpages>4</tpages></addata></record> |
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| identifier | ISSN: 1359-5113 |
| ispartof | Process biochemistry (1991), 2005-10, Vol.40 (10), p.3186-3189 |
| issn | 1359-5113 1873-3298 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_29172219 |
| source | Elsevier ScienceDirect Journals |
| subjects | Acylase I d-Phenylglycine dl- N-Acetylphenylglycine Enantiomeric resolution Ion exchange chromatography l-Phenylglycine |
| title | Enzymic resolution of dl-phenylglycine |
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