DC Field | Value | Language |
---|---|---|
dc.contributor.author | Park, J.H. | ko |
dc.contributor.author | Kim, G.J. | ko |
dc.contributor.author | Kim, Hak-Sung | ko |
dc.date.accessioned | 2009-12-07T06:51:48Z | - |
dc.date.available | 2009-12-07T06:51:48Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2000 | - |
dc.identifier.citation | BIOTECHNOLOGY PROGRESS, v.16, no.4, pp.564 - 570 | - |
dc.identifier.issn | 8756-7938 | - |
dc.identifier.uri | http://hdl.handle.net/10203/14302 | - |
dc.description.abstract | We developed a fully enzymatic process employing D-hydantoinase and N-carbamoylase for the production of D-amino aid from 5'-monosubstituted hydantoin. For the comparison of the reaction systems using two sequential enzymes, D-hydantoinase of Bacillus stearothermophilus SD1 and N-carbamoyl-D-amino acid amidohydrolase (N-carbamoylase) of Agrobacterium tumefaciens NRRL B11291 were separately expressed in each host cell and coexpressed in the same host cell. A high level and constitutive expression of both enzymes in Escherichia coli in a soluble form was achieved using a promoter derived from B. stearothermophilus SD1. The expression levels of both enzymes ranged from 17% to 23% of the total soluble protein, depending on the expression system. In the case of employing separately expressed enzymes, the product yield of D-hydroxyphenylglycine from D,L-p-hydroxyphenylhydantoin and productivity were 71% and 2.57 mM/g-cell/h in 15 h, respectively. The accumulation of N-carbamoyl-D-hydroxyphenylglycine was significant over the reaction time. On the other hand, use of coexpressed enzymes resulted in 98% product yield of D-hydroxyphenylglycine in 15 h, minimizing the level of intermediates in the reaction mixture. The productivity of coexpressed whole cell reaction was estimated to be 6.47 mM/g-cell/h in 15 h. The coexpressed system was tested for an elevated concentration of D,L-p-hydroxyphenylhydantoin, and efficient production can be achieved. | - |
dc.language | English | - |
dc.language.iso | en_US | en |
dc.publisher | AMER CHEMICAL SOC | - |
dc.subject | THERMOSTABLE D-HYDANTOINASE | - |
dc.subject | HETEROGENEOUS REACTION SYSTEM | - |
dc.subject | D-P-HYDROXYPHENYLGLYCINE | - |
dc.subject | IN-VITRO | - |
dc.subject | AMIDOHYDROLASE | - |
dc.subject | PROTEIN | - |
dc.subject | CONVERSION | - |
dc.subject | EXPRESSION | - |
dc.subject | EVOLUTION | - |
dc.subject | STRAINS | - |
dc.title | Production of D-amino acid using whole cells of recombinant Escherichia coli with separately and coexpressed D-hydantoinase and N-carbamoylase | - |
dc.type | Article | - |
dc.identifier.wosid | 000088710200007 | - |
dc.identifier.scopusid | 2-s2.0-0034233319 | - |
dc.type.rims | ART | - |
dc.citation.volume | 16 | - |
dc.citation.issue | 4 | - |
dc.citation.beginningpage | 564 | - |
dc.citation.endingpage | 570 | - |
dc.citation.publicationname | BIOTECHNOLOGY PROGRESS | - |
dc.identifier.doi | 10.1021/bp0000611 | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Kim, Hak-Sung | - |
dc.contributor.nonIdAuthor | Park, J.H. | - |
dc.contributor.nonIdAuthor | Kim, G.J. | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | THERMOSTABLE D-HYDANTOINASE | - |
dc.subject.keywordPlus | HETEROGENEOUS REACTION SYSTEM | - |
dc.subject.keywordPlus | D-P-HYDROXYPHENYLGLYCINE | - |
dc.subject.keywordPlus | IN-VITRO | - |
dc.subject.keywordPlus | AMIDOHYDROLASE | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | CONVERSION | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | EVOLUTION | - |
dc.subject.keywordPlus | STRAINS | - |
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