Facile synthesis of glucose-1-phosphate from starch by Thermus caldophilus GK24 α-glucan phosphorylase

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dc.contributor.authorJungDon Bae-
dc.contributor.authorDuckHee Lee-
dc.contributor.authorDooIl Kim-
dc.contributor.authorSoo Jin Cho-
dc.contributor.authorJung Eun Park-
dc.contributor.authorSukhoon Koh-
dc.contributor.authorJoong Su Kim-
dc.contributor.authorBo Hyun Park-
dc.contributor.authorYongseok Choi-
dc.contributor.authorH J Shin-
dc.contributor.authorS I Hong-
dc.contributor.authorDae Sil Lee-
dc.date.accessioned2017-04-19T09:03:30Z-
dc.date.available2017-04-19T09:03:30Z-
dc.date.issued2005-
dc.identifier.issn00329592-
dc.identifier.uri10.1016/j.procbio.2005.05.007ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/7125-
dc.description.abstractThe glgP gene encoding α-glucan phosphorylase (α-GP) from the thermopile Thermus caldophilus GK24 has been identified, cloned, and overexpressed in Escherichia coli and used to synthesize d-glucose-1-phospate (G1P) from an inexpensive starch. The enzyme, purified 6.5-fold, was isolated in 31% yield from the transformed E. coli, and gave a single band. The purified enzyme may exist as a homohexamer with an apparent molecular mass of a 550 kDa molecule, consisting of 90 kDa per subunit. The optimal pH and temperature were 7.0 and 70°C in the α-GP reaction with starch producing G1P. Soluble starch (amylopectin, amylose) turned out to be a better substrate giving a higher yield of G1P than α-1,6-branched α-1,4-glucans (glycogen, potato starch, etc.). As a result, G1P was obtained in a good yield (47%, w/w) from the reaction containing 5% (w/v) soluble starch in 0.7 M potassium phosphate at pH 7.0. T. caldophilus α-GP shows a high tolerance (up to 0.7 M) of potassium phosphate and plays a critical role in shifting the reaction equilibrium in favor of G1P synthesis. The G1P product can be purified simply by ethanol precipitation, after removing the unreacted starch and inorganic phosphate by activated charcoal and magnesium acetate precipitation. It is concluded that T. caldophilus α-GP readily utilized in large scale synthesis of G1P.-
dc.publisherElsevier-
dc.titleFacile synthesis of glucose-1-phosphate from starch by Thermus caldophilus GK24 α-glucan phosphorylase-
dc.title.alternativeFacile synthesis of glucose-1-phosphate from starch by Thermus caldophilus GK24 α-glucan phosphorylase-
dc.typeArticle-
dc.citation.titleProcess Biochemistry-
dc.citation.number12-
dc.citation.endPage3713-
dc.citation.startPage3707-
dc.citation.volume40-
dc.contributor.affiliatedAuthorJoong Su Kim-
dc.contributor.alternativeName배정돈-
dc.contributor.alternativeName이덕희-
dc.contributor.alternativeName김두일-
dc.contributor.alternativeName조수진-
dc.contributor.alternativeName박정은-
dc.contributor.alternativeName고석훈-
dc.contributor.alternativeName김중수-
dc.contributor.alternativeName박보현-
dc.contributor.alternativeName최용석-
dc.contributor.alternativeName신현재-
dc.contributor.alternativeName홍석인-
dc.contributor.alternativeName이대실-
dc.identifier.bibliographicCitationProcess Biochemistry, vol. 40, no. 12, pp. 3707-3713-
dc.identifier.doi10.1016/j.procbio.2005.05.007-
dc.subject.keywordα-Glucan phosphorylase-
dc.subject.keywordEnzymatic synthesis-
dc.subject.keywordGlucose-1-phosphate-
dc.subject.keywordGlycogen-
dc.subject.keywordStarch-
dc.subject.keywordThermus caldophilus-
dc.subject.localα-Glucan phosphorylase-
dc.subject.localEnzymatic synthesis-
dc.subject.localGlucose-1-phosphate-
dc.subject.localGlycogen-
dc.subject.localStarch-
dc.subject.localThermus caldophilus-
dc.description.journalClassY-
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Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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