Results 121 to 130 of about 7,085 (182)
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Biotechnology Advances, 2006
Fungi are employed to produce industrially important glucoamylases. Most glucoamylases are glycosylated. Glycosylation enhances the enzyme stability. Glucoamylases contain both starch binding and catalytic binding domains, the former being responsible for activity on raw (insoluble) starch.
Dariush, Norouzian +3 more
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Fungi are employed to produce industrially important glucoamylases. Most glucoamylases are glycosylated. Glycosylation enhances the enzyme stability. Glucoamylases contain both starch binding and catalytic binding domains, the former being responsible for activity on raw (insoluble) starch.
Dariush, Norouzian +3 more
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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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Glucoamylases: structural and biotechnological aspects
Applied Microbiology and Biotechnology, 2010Glucoamylases, one of the main types of enzymes involved in starch hydrolysis, are exo-acting enzymes that release consecutive glucose units from the non-reducing ends of starch molecules. Glucoamylases are microbial enzymes, present in bacteria, archaea, and fungi but not in plants and animals.
Julia, Marín-Navarro, Julio, Polaina
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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
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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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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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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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