Immobilization of Zymomonas mobilis and amyloglucosidase for ethanol production from sago starch [PDF]
Immobilization of amyloglucosidase (AMG) and Zymomonas mobilis cells was studied in order to produce ethanol from sago starch economically. Among various immobilization methods tested, a coimmobilized system using chitin and sodium alginate appeared most
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Clinical Experiments with a Toothpaste Containing Amyloglucosidase and Glucose Oxidase
Caries Research, 2009A toothpaste containing sodium fluoride and enzymes activating the antibacterial lactoperoxidase-thiocyanate system was tested in a model with sucrose-induced plaque formation. The dentifrice did not reduce the acidogenicity of dental plaque in vivo in the present study, neither did it reduce plaque formation in a test panel.
J, Afseth, G, Rølla
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A DEX gene conferring production of extracellular amyloglucosidase on yeast
Gene, 1985A DEX gene from Saccharomyces diastaticus (strain BRG536 alpha DEX1) has been cloned in the hybrid vector pJDB207. The gene is included within a 3.6-kb fragment and confers production of extracellular amylo-alpha-1,4-glucosidase (AMG) and, thereby the ability to hydrolyse starch or dextrins on Dex- strains of Saccharomyces cerevisiae.
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Kinetics and performance of a co-immobilised system of amyloglucosidase andZymomonas mobilis
Biotechnology and Bioengineering, 1999High operational stability and productivity of co-immobilised systems are important aspects for their successful application in industrial processes. A dynamic model is required to describe artificially co-immobilised systems because the time needed to reach steady state normally exceeds the operational life span of these systems.
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Australine, a pyrrolizidine alkaloid that inhibits amyloglucosidase and glycoprotein processing
Biochemistry, 1989Australine [(1R,2R,3R,7S,7aR)-3-(hydroxymethyl)-1,2,7-trihydroxypyrrolizid ine] is a polyhydroxylated pyrrolizidine alkaloid that was isolated from the seeds of the Australian tree Castanospermum australe and characterized by NMR and X-ray diffraction analysis [Molyneux et al. (1988) J. Nat. Prod. (in press)].
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Isolation and purification of amyloglucosidase from Halobacterium sodomense
Biomedical Chromatography, 1993AbstractAmyloglucosidase from Halobacterium sodomense was purified by a combination of hydrophobic interaction chromatography and immobilized metal ion affinity chromatography at analytical and preparative scale with 75% recovery. The enzyme was found to be a dimer of two different subunits with molecular weights of 72,000 and 82,000 D, respectively ...
G, Chaga, J, Porath, T, Illéni
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Preparation and characterization of amyloglucosidase adsorbed on activated charcoal
Journal of Molecular Catalysis B: Enzymatic, 2000Amyloglucosidase (AMG) [α-1, 4-d-glucan glucohydrolase (E.C.3.2.1.3)] is an exo-enzyme, which is used in the hydrolysis of starch to glucose in industries. To increase the efficiency and profitability of this process, AMG was immobilized on activated charcoal by physical adsorption without the aid of any cross-linking agent, characterized by hydrolysis
A.S. Rani, M.L.M. Das, S. Satyanarayana
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Method for Determination of Acid Amyloglucosidase in Isolated Islets of the Pancreas
Enzymologia biologica et clinica, 2017A method has been developed for the assay of acid amyloglucosidase activity in isolated pancreatic islets with glycogen as substrate. The effects of the type and concentration of buffer, pH, incubation time, and concentration of tissue and substrate on the rate of enzyme hydrolysis are described. One unit of acid amyloglucosidase activity is defined as
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Porous high amylose rice starch modified by amyloglucosidase and maltogenic α-amylase
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