Torben P. Frandsen
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View article: Conversion of the maltogenic α-amylase Novamyl into a CGTase
Conversion of the maltogenic α-amylase Novamyl into a CGTase Open
Novamyl is a thermostable five-domain maltogenic alpha-amylase that shows sequence and structural homology with the cyclodextrin glycosyltransferases (CGTases). Comparing X-ray crystal structures of Novamyl and CGTases, two major differenc…
View article: Purification, Enzymatic Characterization, and Nucleotide Sequence of a High-Isoelectric-Point α-Glucosidase from Barley Malt
Purification, Enzymatic Characterization, and Nucleotide Sequence of a High-Isoelectric-Point α-Glucosidase from Barley Malt Open
High-isoelectric-point (pI) α-glucosidase was purified 7,300-fold from an extract of barley (Hordeum vulgare) malt by ammonium sulfate fractionation, ion-exchange, and butyl-Sepharose chromatography. The enzyme had high activity toward mal…
View article: Glucoamylase mutants in the conserved active-site segment Trp170-Tyr175 located at a distance from the site of catalysis
Glucoamylase mutants in the conserved active-site segment Trp170-Tyr175 located at a distance from the site of catalysis Open
To mimic the structure of the 1.8-fold more active (k(cat)) Rhizopus oryzae glucoamylase (GA), Aspergillus niger GA was subjected to site-directed mutagenesis in the Trp170-Tyr175 segment of the third of the six well-conserved alpha-->alph…
View article: Chemical mapping of the active site of the glucoamylase of <i>Aspergillus niger</i>
Chemical mapping of the active site of the glucoamylase of <i>Aspergillus niger</i> Open
A recently developed technique for the probing of the combining sites of lectins and antibodies, to establish the structure of the epitope that is involved in the binding of an oligosaccharide, is used to study the binding of methyl α-isom…
View article: Production, purification and characterization of the catalytic domain of glucoamylase from <i>Aspergillus niger</i>
Production, purification and characterization of the catalytic domain of glucoamylase from <i>Aspergillus niger</i> Open
The catalytic domain of glucoamylases G1 and G2 from Aspergillus niger is produced in vitro in high yield by limited proteolysis using either subtilisin Novo or subtilisin Carlsberg. Purification by affinity chromatography on an acarbose-S…