DC Field | Value | Language |
---|---|---|
dc.contributor.author | Dae Heoun Baek | - |
dc.contributor.author | Jae Jun Song | - |
dc.contributor.author | Seung Goo Lee | - |
dc.contributor.author | Seok Joon Kwon | - |
dc.contributor.author | Y Asano | - |
dc.contributor.author | Moon Hee Sung | - |
dc.date.accessioned | 2017-04-19T08:59:30Z | - |
dc.date.available | 2017-04-19T08:59:30Z | - |
dc.date.issued | 2003 | - |
dc.identifier.issn | 0141-0229 | - |
dc.identifier.uri | 10.1016/S0141-0229(02)00268-5 | ko |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/6001 | - |
dc.description.abstract | A new thermostable D-methionine amidase was found in a cell-free extract of Brevibacillus borstelensis BCS-1. After five steps of purification, the specific activity increased approximately 207-fold and the purity was more than 98%. The molecular weight of the enzyme was estimated to be 199kDa by gel permeation chromatography and 30kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, which indicates that the thermostable D-methionine amidase was a homo-hexamer consisting of a single subunit. The purified enzyme was stable up to 65°C within a broad pH range from 6.5 to 10.0, and its maximum activity was measured at pH 9.5 and 70°C. The enzyme activity increased about five-fold with the addition of Co2+, yet was strongly inhibited by Hg2+, 2-mercaptoethanol, dithiothreitol, and ethylenediaminetetracetic acid. The thermostable D-methionine amidase exhibited a high amidase activity and D-stereospecificity toward D-amino acid amides and esters, yet did not hydrolyze D-peptides. The catalytic efficiencies (kcat/Km, mM-1s-1) of the enzyme for D-methioninamide and D-alaninamide were 3086 and 21.5, respectively, and the enantiomeric excess (ee) and enantiomeric ratio of D-phenylalanine produced from DL-phenylalaninamide were 97.1 and 196%, respectively. | - |
dc.publisher | Elsevier | - |
dc.title | New thermostable D-methionine amidase from Brevibacillus borstelensis BCS-1 and its application for D-phenylalanine production | - |
dc.title.alternative | New thermostable D-methionine amidase from Brevibacillus borstelensis BCS-1 and its application for D-phenylalanine production | - |
dc.type | Article | - |
dc.citation.title | Enzyme and Microbial Technology | - |
dc.citation.number | 1 | - |
dc.citation.endPage | 139 | - |
dc.citation.startPage | 131 | - |
dc.citation.volume | 32 | - |
dc.contributor.affiliatedAuthor | Dae Heoun Baek | - |
dc.contributor.affiliatedAuthor | Jae Jun Song | - |
dc.contributor.affiliatedAuthor | Seung Goo Lee | - |
dc.contributor.affiliatedAuthor | Seok Joon Kwon | - |
dc.contributor.alternativeName | 백대헌 | - |
dc.contributor.alternativeName | 송재준 | - |
dc.contributor.alternativeName | 이승구 | - |
dc.contributor.alternativeName | 권석준 | - |
dc.contributor.alternativeName | Asano | - |
dc.contributor.alternativeName | 성문희 | - |
dc.identifier.bibliographicCitation | Enzyme and Microbial Technology, vol. 32, no. 1, pp. 131-139 | - |
dc.identifier.doi | 10.1016/S0141-0229(02)00268-5 | - |
dc.subject.keyword | Brevibacillus borstelensis BCS-1 | - |
dc.subject.keyword | D-Phenylalanine production | - |
dc.subject.keyword | Thermophilic bacterium | - |
dc.subject.keyword | Thermostable D-methionine amidase | - |
dc.subject.local | Brevibacillus borstelensis BCS-1 | - |
dc.subject.local | D-Phenylalanine production | - |
dc.subject.local | Thermophilic bacteria | - |
dc.subject.local | thermophilic bacterium | - |
dc.subject.local | Thermophilic bacterium | - |
dc.subject.local | Thermostable D-methionine amidase | - |
dc.description.journalClass | Y | - |
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