Results 81 to 90 of about 6,563 (137)
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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
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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
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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
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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
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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
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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
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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 ...
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Journal of applied biochemistry, 1984
Glucoamylase (alpha-1,4-glucan glucohydrolase, EC 3.2.1.3) from fungal sources is one of the microbial glycoproteins that has received considerable attention particularly because it is used in the commercial production of dextrose. Several investigators have isolated glucoamylase from various fungal sources.
P, Manjunath +2 more
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Glucoamylase (alpha-1,4-glucan glucohydrolase, EC 3.2.1.3) from fungal sources is one of the microbial glycoproteins that has received considerable attention particularly because it is used in the commercial production of dextrose. Several investigators have isolated glucoamylase from various fungal sources.
P, Manjunath +2 more
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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.
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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.
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Glucoamylase Research: An Overview
Starch - Stärke, 1995AbstractThis paper reviews the main features of glucoamylase research describing essentially more recent developments on microorganisms, production and properties of glucoamylases. It is an important industrial enzyme and is widely used in starch saccharification, brewing and distilling industry.
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