maltoheptaose has been researched along with isomaltose in 4 studies
Studies (maltoheptaose) | Trials (maltoheptaose) | Recent Studies (post-2010) (maltoheptaose) | Studies (isomaltose) | Trials (isomaltose) | Recent Studies (post-2010) (isomaltose) |
---|---|---|---|---|---|
114 | 0 | 39 | 373 | 47 | 131 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 3 (75.00) | 18.2507 |
2000's | 1 (25.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Ford, C; Reilly, PJ; Sierks, MR; Svensson, B | 2 |
Fang, TY; Ford, C | 1 |
Frandsen, TP; Lehmbeck, J; Nielsen, BR | 1 |
4 other study(ies) available for maltoheptaose and isomaltose
Article | Year |
---|---|
Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori.
Topics: Amino Acid Sequence; Aspartic Acid; Aspergillus; Base Sequence; Binding Sites; Catalysis; DNA Restriction Enzymes; Glucan 1,4-alpha-Glucosidase; Glucans; Glutamates; Glutamic Acid; Hydrogen-Ion Concentration; Isomaltose; Kinetics; Maltose; Molecular Sequence Data; Mutation; Sequence Homology, Nucleic Acid; Structure-Activity Relationship; Thermodynamics | 1990 |
Functional roles and subsite locations of Leu177, Trp178 and Asn182 of Aspergillus awamori glucoamylase determined by site-directed mutagenesis.
Topics: Amino Acid Sequence; Aspergillus; Base Sequence; Binding Sites; Carbohydrate Sequence; Catalysis; Glucan 1,4-alpha-Glucosidase; Glucans; Isomaltose; Leucine; Maltose; Models, Chemical; Molecular Sequence Data; Mutagenesis, Site-Directed; Sequence Homology, Amino Acid; Structure-Activity Relationship; Substrate Specificity; Tryptophan | 1993 |
Protein engineering of Aspergillus awamori glucoamylase to increase its pH optimum.
Topics: Aspergillus; Catalysis; Glucan 1,4-alpha-Glucosidase; Glucans; Glucose; Hydrogen Bonding; Hydrogen-Ion Concentration; Hydrolysis; Isoelectric Point; Isomaltose; Kinetics; Maltose; Models, Molecular; Mutagenesis, Site-Directed; Recombinant Proteins | 1998 |
Cloning, heterologous expression, and enzymatic characterization of a thermostable glucoamylase from Talaromyces emersonii.
Topics: Aspergillus niger; Cloning, Molecular; Enzyme Stability; Gene Expression; Glucan 1,4-alpha-Glucosidase; Glucans; Hydrogen-Ion Concentration; Isomaltose; Kinetics; Maltose; Molecular Sequence Data; Recombinant Fusion Proteins; Substrate Specificity; Talaromyces; Temperature | 2002 |