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Start Over Author "Dong Hyun Jung" Journal enzyme and microbial technology
2 results on '"Dong Hyun Jung"'

1. An unusual chimeric amylosucrase generated by domain-swapping mutagenesis

Author

Sun-Young Park, Sang-Ho Yoo, Cheon-Seok Park, Young-Rok Kim, Dong-Ho Seo, Dong-Hyun Jung, and Jong-Hyun Jung

Subjects
0301 basic medicine, Recombinant Fusion Proteins, Bioengineering, Biology, Molecular Dynamics Simulation, 010402 general chemistry, medicine.disease_cause, Protein Engineering, 01 natural sciences, Applied Microbiology and Biotechnology, Biochemistry, law.invention, Substrate Specificity, 03 medical and health sciences, Amylosucrase, Bacterial Proteins, law, Enzyme Stability, medicine, Overlap extension polymerase chain reaction, Protein Structure, Quaternary, Escherichia coli, Thermostability, chemistry.chemical_classification, Mutagenesis, biology.organism_classification, Molecular biology, 0104 chemical sciences, Kinetics, 030104 developmental biology, Enzyme, chemistry, Glucosyltransferases, Recombinant DNA, biology.protein, Deinococcus, Deinococcus geothermalis, Neisseria, Biotechnology
Abstract

Amylosucrase (ASase; EC 2.4.1.4) synthesizes α-1,4-glucans using sucrose as a sole substrate. The aim of this study was to compare the enzymatic properties of four recombinant ASase genes to determine the underlying mechanisms thereof. Following cloning and expression in Escherichia coli, we determined that the ASase enzyme from Deinococcus geothermalis (DGAS) had the highest thermostability whereas ASase from Neisseria polysaccharea (NPAS) showed the greatest polymerization activity. Chimeric ASases were constructed using dgas and npas genes by overlap extension polymerase chain reaction. Two of the six chimeric ASases generated, NPAS-B' and DGAS-B, showed ASase activity using sucrose as the sole substrate. However, DGAS-B was not able to produce longer α-1,4-glucans; the highest degree of polymerization was

Published
2015

2. Bioinformatic and biochemical analysis of a novel maltose-forming α-amylase of the GH57 family in the hyperthermophilic archaeon Thermococcus sp. CL1

Author

Eun-Jung Jeon, James F. Holden, Cheon-Seok Park, Dong-Hyun Jung, Jong-Hyun Jung, and Dong-Ho Seo

Subjects
Archaeal Proteins, Molecular Sequence Data, Bioengineering, medicine.disease_cause, Applied Microbiology and Biotechnology, Biochemistry, Genes, Archaeal, Substrate Specificity, chemistry.chemical_compound, medicine, Glycoside hydrolase, Amylase, Amino Acid Sequence, Cloning, Molecular, Maltose, Escherichia coli, Peptide sequence, Phylogeny, chemistry.chemical_classification, biology, Sequence Homology, Amino Acid, Computational Biology, Glycosidic bond, biology.organism_classification, Hyperthermophile, Recombinant Proteins, Thermococcus, Kinetics, chemistry, biology.protein, alpha-Amylases, Biotechnology
Abstract

Maltose-forming α-amylase is a glycoside hydrolase family 57 (GH57) member that is unique because it displays dual hydrolysis activity toward α-1,4- and α-1,6-glycosidic linkages and only recognizes maltose. This enzyme was previously identified only in Pyrococcus sp. ST04 (PSMA); however, we recently found two homologs subgroups in Thermococcus species. One subgroup (subgroup A) showed relatively high amino acid sequence similarity to PSMA (>71%), while the other subgroup (subgroup B) showed lower homology with PSMA (

Published
2013

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