New thermostable D-methionine amidase from Brevibacillus borstelensis BCS-1 and its application for D-phenylalanine production

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dc.contributor.authorDae Heoun Baek-
dc.contributor.authorJae Jun Song-
dc.contributor.authorSeung Goo Lee-
dc.contributor.authorSeok Joon Kwon-
dc.contributor.authorY Asano-
dc.contributor.authorMoon Hee Sung-
dc.date.accessioned2017-04-19T08:59:30Z-
dc.date.available2017-04-19T08:59:30Z-
dc.date.issued2003-
dc.identifier.issn0141-0229-
dc.identifier.uri10.1016/S0141-0229(02)00268-5ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/6001-
dc.description.abstractA 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.publisherElsevier-
dc.titleNew thermostable D-methionine amidase from Brevibacillus borstelensis BCS-1 and its application for D-phenylalanine production-
dc.title.alternativeNew thermostable D-methionine amidase from Brevibacillus borstelensis BCS-1 and its application for D-phenylalanine production-
dc.typeArticle-
dc.citation.titleEnzyme and Microbial Technology-
dc.citation.number1-
dc.citation.endPage139-
dc.citation.startPage131-
dc.citation.volume32-
dc.contributor.affiliatedAuthorDae Heoun Baek-
dc.contributor.affiliatedAuthorJae Jun Song-
dc.contributor.affiliatedAuthorSeung Goo Lee-
dc.contributor.affiliatedAuthorSeok Joon Kwon-
dc.contributor.alternativeName백대헌-
dc.contributor.alternativeName송재준-
dc.contributor.alternativeName이승구-
dc.contributor.alternativeName권석준-
dc.contributor.alternativeNameAsano-
dc.contributor.alternativeName성문희-
dc.identifier.bibliographicCitationEnzyme and Microbial Technology, vol. 32, no. 1, pp. 131-139-
dc.identifier.doi10.1016/S0141-0229(02)00268-5-
dc.subject.keywordBrevibacillus borstelensis BCS-1-
dc.subject.keywordD-Phenylalanine production-
dc.subject.keywordThermophilic bacterium-
dc.subject.keywordThermostable D-methionine amidase-
dc.subject.localBrevibacillus borstelensis BCS-1-
dc.subject.localD-Phenylalanine production-
dc.subject.localThermophilic bacteria-
dc.subject.localthermophilic bacterium-
dc.subject.localThermophilic bacterium-
dc.subject.localThermostable D-methionine amidase-
dc.description.journalClassY-
Appears in Collections:
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
Synthetic Biology and Bioengineering Research Institute > 1. Journal Articles
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