Results 171 to 180 of about 9,014 (216)
Production and purification of a granular-starch-binding domain of glucoamylase 1 fromAspergillus niger [PDF]
FEBS Letters, 1990 A domain of glucoamylase 1 from Aspergillus niger which binds to granular starch was produced by proteolytic digestion and purified to apparent homogeneity by extraction with corn starch followed by anion-exchange chromatography and gel filtration.
Gary Williamson
exaly +2 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Microbial glucoamylases: characteristics and applications
Critical Reviews in Biotechnology, 2009Glucoamylase is one of the oldest and widely used biocatalysts in food industry. The major application of glucoamylase is the saccharification of partially processed starch/dextrin to glucose, which is an essential substrate for numerous fermentation processes and a range of food and beverage industries.
Pardeep, Kumar, T, Satyanarayana
openaire +2 more sources
Properties of human intestinal glucoamylase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1973Abstract 1. 1. Human intestinal glucoamylase has been purified almost to homogeneity by polyacrylamide disc electrophoresis. At least two isoenzymes were found with identical catalytic properties. 2. 2. Linear oligosaccharides ( N = 9 ) containing glucose residues linked α(1 → 4) have the greatest affinity for the active site.
J J, Kelly, D H, Alpers
openaire +2 more sources
Immobilization of glucoamylase on porous glass
Acta Biotechnologica, 1988AbstractThe kinetic properties of glucoamylase immobilized on silanized porous glass in saccharification of starch solutions were examined as well as the influence of the working condition on its operational stability.
E. Miller, H. Sucher
openaire +1 more source
Purification of glucoamylase fromAspergillus terreus
World Journal of Microbiology & Biotechnology, 1990Glucoamylase from a rice bran culture ofAspergillus terreus was purified by chromatography on DEAE-cellulose and concanavatin A-Sepharose. A homogenous monomer resulted after SDS-PAGE electrophoresis. The enzyme was a glycoprotein, molecular weight, 86,000 with 7.5% (w/w) carbohydrate content.
S, Ali, Z, Hossain, S, Mahmood, R, Alam
openaire +2 more sources
Glucoamylase Covalently Coupled to Porous Glass
Applied Biochemistry and Biotechnology, 1982Glucoamylase (EC 3.2.1.3) was immobilized to alkylamine porous glass with glutaraldehyde. The choice and pretreatment of carrier and conditions for immobilization have been investigated. The immobilized enzyme contained about 4.0-8.0% protein and its activity was about 1000-1700 U/g.
L, Gaoxiang +3 more
openaire +2 more sources
Journal of Fermentation and Bioengineering, 1992
Affinity chromatography using an immobilized glucoamylase inhibitors (GAIs) column promises glucoamylase(GA)-free unpasteurized sake by means of complete adsorption of the GA in unpasteurized sake on the column. In consequence of the adsorption taking place at a maximum flow rate (SV=90 h −1 ) at 4°C, even in the presence of 2% (w/v) glucose and 20% (v/
Yoji Hata +5 more
openaire +1 more source
Affinity chromatography using an immobilized glucoamylase inhibitors (GAIs) column promises glucoamylase(GA)-free unpasteurized sake by means of complete adsorption of the GA in unpasteurized sake on the column. In consequence of the adsorption taking place at a maximum flow rate (SV=90 h −1 ) at 4°C, even in the presence of 2% (w/v) glucose and 20% (v/
Yoji Hata +5 more
openaire +1 more source
Glucoamylase absorption and desorption process
Journal of Biomaterials Science, Polymer Edition, 1996This paper reports the study of glucoamylase absorption and desorption processes on spherical particles constituting acrylic supports. The kinetic (reaction order, half-life of the reaction, reaction rate constant), and thermodynamic parameters (activation energy, pre-exponential factor) of the glucoamylase immobilization reaction dynamics inside the ...
openaire +2 more sources
A thermophilic glucoamylase fromCephalosporium eichhorniae
Current Microbiology, 1978A novel exocellular glucoamylase produced by a thermophilic fungus,Cephalosporium eichhorniae, was purified by a combination of membrane filtration and Sephadex chromatography. The enzyme was a glycoprotein, 28% carbohydrate by weight. It was composed of a single polypeptide chain with a molecular weight of 26,850.
openaire +2 more sources
Glucoamylases from Saccharomyces Diastaticus
Critical Reviews in Biotechnology, 1987(1987). Glucoamylases from Saccharomyces Diastaticus. Critical Reviews in Biotechnology: Vol. 5, No. 2, pp. 95-104.
openaire +2 more sources