Purification and biochemical characterization of pullulanase type I from Thermus caldophilus GK-24

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dc.contributor.authorC H Kim-
dc.contributor.authorO Nashiru-
dc.contributor.authorJung Hun Koh-
dc.description.abstractA thermostable pullulanase (pullulan 6-glucanohydrolase, EC has been purified to homogeneity from Thermus caldophilus GK-24 by chromatographic methods, including gel-filtration and ion-exchange chromatography. The specific activity of the enzyme was increased 431-fold with a recovery of 13.2%. The purified enzyme was a monomer, M(r) = 65 kDa as estimated by SDS-PAGE and gel filtration. The pI was 6.1. The enzyme was most active at pH 5.5. The activity was maximal at 75°C and stable up to 95°C for 30 min at pH 5.5. The enzyme was stable to incubation from pH 3.5 to pH 8.0 at 4°C for 24 h. The activity of the enzyme was stimulated by Mn2+ and Mg2+ ions. Ni2+, Ca2+, Co2+ ions and EDTA did not inhibit the enzyme activity. The enzyme hydrolyzed the α-1,6 linkages of amylopectin, glycogens, α,β-limited dextrin, and pullulan. The enzyme caused the complete hydrolysis of pullulan to maltotriose. The activity was inhibited by α-, β-, or γ-cyclodextrins. The N-terminal sequence [(Ala-Pro-Gln-(Asp or Tyr)-Asn-Leu-Leu-Xaa-Ile-Gly-Ala(Ser)l showed some similarity to those of bacterial pullulanases.-
dc.publisherOxford Univ Press-
dc.titlePurification and biochemical characterization of pullulanase type I from Thermus caldophilus GK-24-
dc.title.alternativePurification and biochemical characterization of pullulanase type I from Thermus caldophilus GK-24-
dc.citation.titleFEMS Microbiology Letters-
dc.contributor.affiliatedAuthorJung Hun Koh-
dc.identifier.bibliographicCitationFEMS Microbiology Letters, vol. 138, no. 2, pp. 147-152-
dc.subject.keywordThermus caldophilus GK-24-
dc.subject.keywordPullulanase type I-
dc.subject.keywordThermophilic bacteria-
dc.subject.localthermus caldophilus GK-24-
dc.subject.localthermus caldosphilus Gk24-
dc.subject.localThermus caldophilus GK-24-
dc.subject.localThermus caldophilus GK24-
dc.subject.localthermus caldophilus GK24-
dc.subject.localPullulanase type I-
dc.subject.localpullulanase type I-
dc.subject.localThermophilic bacteria-
dc.subject.localthermophilic bacterium-
dc.subject.localThermophilic bacterium-
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Synthetic Biology and Bioengineering Research Institute > Genome Editing Research Center > 1. Journal Articles
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