Search Results1-12 of  12

  • PARK Kwan Hwa ID: 9000000718154

    Research Center for New Bio-Materials in Agriculture and Department of Food Science and Technology, School of Agricultural Biotechnology, Seoul National University (2001 from CiNii)

    Articles in CiNii:1

    • The Multisubstrate Specificity and the Quaternary Structure of Cyclodextrin-/Pullulan-degrading Enzymes (2001)
  • PARK Kwan Hwa ID: 9000020819145

    Articles in CiNii:1

    • A rapid screening method for alkaline .BETA.-cyclodextrin glucanotransferase using phenolphthalein-methyl orange-containing-solid medium. (1989)
  • PARK Kwan-Hwa ID: 9000000479327

    Department of Marine Biomedical Science, Kunsan National University (2000 from CiNii)

    Articles in CiNii:1

    • ANNUALLY REPRODUCTIVE CYCLES OF GONADOTROPES, AND ENDOCRINE MATERIALS AND PLASMA COMPONENTS IN SPECIAL RELATION TO OOGENSIS IN RAINBOW TROUT, Oncorhynchus mykiss (2000)
  • PARK Kwan-Hwa ID: 9000001657409

    Center for Agricultural Biomaterials, and Department of Food Science and Biotechnology, School of Agricultural Biotechnology, Seoul National University (2006 from CiNii)

    Articles in CiNii:1

    • Function and Tertiary- and Quaternary-structure of Cyclodextrin-hydrolyzing Enzymes (CDase), a Group of Multisubstrate Specific Enzymes Belonging to the α-Amylase Family (2006)
  • PARK Kwan-Hwa ID: 9000004156940

    Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, School of Agricultural Biotechnology, Seoul National University (2007 from CiNii)

    Articles in CiNii:7

    • Engineering Thermus Maltogenic Amylase with Improved Thermostability : Probing the Role of the Conserved Calcium Binding Site in Cyclodextrin-degrading Enzymes (2005)
    • TreX from Sulfolobus solfataricus ATCC 35092 Displays Isoamylase and 4-α-Glucanotransferase Activities (2007)
    • Modulation of Substrate Preference of Thermus Maltogenic Amylase by Mutation of the Residues at the Interface of a Dimer (2007)
  • PARK Kwan-Hwa ID: 9000007041901

    Articles in CiNii:1

    • Antioxidative Effects of Glycosyl-ascorbic Acids Synthesized by Maltogenic Amylase to Reduce Lipid Oxidation and Volatiles Production in Cooked Chicken Meat (2004)
  • PARK Kwan-Hwa ID: 9000240031143

    Department of Foodservice Management and Nutrition, Sangmyung University (2013 from CiNii)

    Articles in CiNii:1

    • Characterization and application of an acidophilic and thermostable βNB-LPA3ETCglucosidase from Thermofilum pendens (2013)
  • Park Kwan Hwa ID: 9000269007177

    Department of FoodService Management and Nutrition, Sangmyung University (2014 from CiNii)

    Articles in CiNii:1

    • S2-9 Enzymes Involved in Glycogen Metabolism in Escherichia coli(Recent Progress of Carbohydrate Bioengineering) (2014)
  • Park Kwan-Hwa ID: 9000021895365

    Articles in CiNii:1

    • Synthesis of Branched Oligosaccharides from Starch by Two Amylases Cloned from Bacillus licheniformis. (1994)
  • Park Kwan-Hwa ID: 9000257965769

    Center for Agricultural Biomaterials, and Department of Food Science and Technology, School of Agricultural Biotechnology, Seoul National University (2005 from CiNii)

    Articles in CiNii:1

    • Engineering Thermus Maltogenic Amylase with Improved Thermostability: Probing the Role of the Conserved Calcium Binding Site in Cyclodextrin-degrading Enzymes (2005)
  • Park Kwan-Hwa ID: 9000258425165

    Center for Agricultural Biomaterials, Seoul National University|Department of Food Science & Biotechnology, School of Agricultural Biotechnology, Seoul National University (2007 from CiNii)

    Articles in CiNii:1

    • Novel Catalytic Properties of a Hyperthermophilic Amylolytic Enzyme from <I>Pyrococcus furiosus</I> and Its Application (2007)
  • Park Kwan-Hwa ID: 9000291602235

    Department of Food Science and Biotechnology, Seoul National University|Department of Foodservice Management and Nutrition, Sangmyung University (2015 from CiNii)

    Articles in CiNii:1

    • Roles of Enzymes in Glycogen Metabolism and Degradation in <i>Escherichia coli</i> (2015)
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