Compounds > maltoheptaose
Page last updated: 2024-09-05

maltoheptaose and isomaltose

maltoheptaose has been researched along with isomaltose in 4 studies

Compound Research Comparison

Studies
(maltoheptaose)		Trials
(maltoheptaose)		Recent Studies (post-2010)
(maltoheptaose)		Studies
(isomaltose)		Trials
(isomaltose)		Recent Studies (post-2010) (isomaltose)
11403937347131

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (75.00)18.2507
2000's1 (25.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Ford, C; Reilly, PJ; Sierks, MR; Svensson, B2
Fang, TY; Ford, C1
Frandsen, TP; Lehmbeck, J; Nielsen, BR1

Other Studies

4 other study(ies) available for maltoheptaose and isomaltose

ArticleYear
Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori.
    Protein engineering, 1990, Volume: 3, Issue:3

    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.
    Protein engineering, 1993, Volume: 6, Issue:1

    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.
    Protein engineering, 1998, Volume: 11, Issue:5

    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.
    Protein expression and purification, 2002, Volume: 26, Issue:1

    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