DC Field | Value | Language |
---|---|---|
dc.contributor.author | Cho, Byung-Kwan | ko |
dc.contributor.author | Seo, Joo-Hyun | ko |
dc.contributor.author | Kim, Juhan | ko |
dc.contributor.author | Lee, Chang-Soo | ko |
dc.contributor.author | Kim, Byung-Gee | ko |
dc.date.accessioned | 2013-03-08T07:59:21Z | - |
dc.date.available | 2013-03-08T07:59:21Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2006-07 | - |
dc.identifier.citation | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, v.11, no.4, pp.299 - 305 | - |
dc.identifier.issn | 1226-8372 | - |
dc.identifier.uri | http://hdl.handle.net/10203/92539 | - |
dc.description.abstract | Aromatic L-amino acid transaminase is an enzyme that is able to transfer the amino group from L-glutamate to unnatural aromatic a-keto acids to generate alpha-ketog luta rate and unnatural aromatic L-amino acids, respectively. Enrichment culture was used to isolate thermophilic Bacillus sp. T30 expressing this enzyme for use in the synthesis of unnatural L-amino acids. The asymmetric syntheses of L-homophenylalanine and L-phenylglycine resulted in conversion yields of > 95% and > 93% from 150 mM 2-oxo-4-phenylbutyrate and phenylglyoxylate, respectively, using L-glutamate as an amino donor at 60 degrees C. Synthesized L-homophenylalanine and L-phenylglycine were optically pure (> 99% enantiomeric excess) and continuously pre-cipitated in the reaction solution due to their low solubility at the given reaction pH. While the solubility of the (Aeto acid substrates is dependent on temperature, the solubility of the unnatural L-amino acid products is dependent on the reaction pH. As the solubility difference between substrate and product at the given reaction pH is therefore larger at higher temperature, the thermophilic transaminase was successfully used to shift the reaction equilibrium toward rapid product formation. | - |
dc.language | English | - |
dc.publisher | KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING | - |
dc.subject | PURE (S)-AMINO ACIDS | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | THERMAL INACTIVATION | - |
dc.subject | L-HOMOPHENYLALANINE | - |
dc.subject | COUPLING REACTIONS | - |
dc.subject | AMINOTRANSFERASE | - |
dc.subject | PHENYLALANINE | - |
dc.subject | PATHWAY | - |
dc.subject | ENZYMES | - |
dc.title | Asymmetric synthesis of unnatural L-amino acids using thermophilic aromatic L-amino acid transaminase | - |
dc.type | Article | - |
dc.identifier.wosid | 000240267100005 | - |
dc.identifier.scopusid | 2-s2.0-33748505018 | - |
dc.type.rims | ART | - |
dc.citation.volume | 11 | - |
dc.citation.issue | 4 | - |
dc.citation.beginningpage | 299 | - |
dc.citation.endingpage | 305 | - |
dc.citation.publicationname | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING | - |
dc.contributor.localauthor | Cho, Byung-Kwan | - |
dc.contributor.nonIdAuthor | Seo, Joo-Hyun | - |
dc.contributor.nonIdAuthor | Kim, Juhan | - |
dc.contributor.nonIdAuthor | Lee, Chang-Soo | - |
dc.contributor.nonIdAuthor | Kim, Byung-Gee | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | thermophilic enzyme | - |
dc.subject.keywordAuthor | transaminase | - |
dc.subject.keywordAuthor | unnatural amino acids | - |
dc.subject.keywordAuthor | asymmetric synthesis | - |
dc.subject.keywordAuthor | equilibrium-shift | - |
dc.subject.keywordAuthor | enrichment culture | - |
dc.subject.keywordPlus | PURE (S)-AMINO ACIDS | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | THERMAL INACTIVATION | - |
dc.subject.keywordPlus | L-HOMOPHENYLALANINE | - |
dc.subject.keywordPlus | COUPLING REACTIONS | - |
dc.subject.keywordPlus | AMINOTRANSFERASE | - |
dc.subject.keywordPlus | PHENYLALANINE | - |
dc.subject.keywordPlus | PATHWAY | - |
dc.subject.keywordPlus | ENZYMES | - |
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