0000000000087787

AUTHOR

Jong-hyun Jung

0000-0002-0599-0985

showing 2 related works from this author

GH57 amylopullulanase from Desulfurococcus amylolyticus JCM 9188 can make highly branched cyclodextrin via its transglycosylation activity.

2018

Abstract Desulfurococcus amylolyticus is an anaerobic and hyperthermophilic crenarchaeon that can use various carbohydrates as energy sources. We found a gene encoding a glycoside hydrolase family 57 amylolytic enzymes (DApu) in a putative carbohydrate utilization gene cluster in the genome of D. amylolyticus . This gene has an open reading frame of 1,878 bp and consists of 626 amino acids with a molecular mass of 71 kDa. Recombinant DApu (rDApu) completely hydrolyzed pullulan to maltotriose by attacking α-1,6-glycosidic linkages, and was able to produce glucose and maltose from soluble starch and amylopectin. Although rDApu showed no activity toward α-cyclodextrin (CD) and β-CD, maltooctao…

0301 basic medicineGlycosylationGlycoside HydrolasesArchaeal ProteinsBioengineeringApplied Microbiology and BiotechnologyBiochemistrySubstrate Specificity03 medical and health scienceschemistry.chemical_compoundHydrolysisOpen Reading FramesGene clusterEnzyme StabilityMaltotrioseGlycoside hydrolaseCloning MolecularMaltoseGlucansCyclodextrins030102 biochemistry & molecular biologyDesulfurococcaceaePullulanMaltoseMolecular Weight030104 developmental biologychemistryBiochemistryAmylopectinEnergy sourceTrisaccharidesBiotechnologyEnzyme and microbial technology
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Acceptor Specificity of Amylosucrase from Deinococcus radiopugnans and Its Application for Synthesis of Rutin Derivatives

2016

The transglycosylation activity of amylosucrase (ASase) has received significant attention owing to its use of an inexpensive donor, sucrose, and broad acceptor specificity, including glycone and aglycone compounds. The transglycosylation reaction of recombinant ASase from Deinococcus radiopugnans (DRpAS) was investigated using various phenolic compounds, and quercetin-3-O-rutinoside (rutin) was found to be the most suitable acceptor molecule used by DRpAS. Two amino acid residues in DRpAS variants (DRpAS Q299K and DRpAS Q299R), assumed to be involved in acceptor binding, were constructed by site-directed mutagenesis. Intriguingly, DRpAS Q299K and DRpAS Q299R produced 10-fold and 4-fold hig…

0106 biological sciences0301 basic medicineGlycosylationGlycosylationStereochemistryRutinAmino Acid Motifs01 natural sciencesApplied Microbiology and BiotechnologySubstrate Specificity03 medical and health sciencesRutinchemistry.chemical_compoundAmylosucraseGlucosyltransferasesBacterial Proteins010608 biotechnologyDeinococcusBinding siteBinding SitesbiologyGeneral Medicinebiology.organism_classificationAcceptorMolecular Docking SimulationKinetics030104 developmental biologyAglyconechemistryGlucosyltransferasesbiology.proteinDeinococcusBiotechnologyJournal of Microbiology and Biotechnology
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