Results 171 to 180 of about 5,714 (209)
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Rapid Colorimetric Method for the Microdetermination of Amyloglucosidase

Zentralblatt für Bakteriologie, Parasitenkunde, Infektionskrankheiten und Hygiene. Zweite Naturwissenschaftliche Abteilung: Allgemeine, Landwirtschaftliche und Technische Mikrobiologie, 1974
Summary A new simple method for amyloglucosidase activity has been suggested. It is based on the optical density measurements of the products of enzymic reactions.
R M, Attia, S A, Ali
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Lentiginosine, a dihydroxyindolizidine alkaloid that inhibits amyloglucosidase

Biochemistry, 1990
Lentiginosine, a dihydroxyindolizidine alkaloid, was extracted from the leaves of Astragalus lentiginosus with hot methanol and was purified to homogeneity by ion-exchange, thin-layer, and radial chromatography. A second dihydroxyindolizidine, the 2-epimer of lentiginosine, was also purified to apparent homogeneity from these extracts.
I, Pastuszak   +3 more
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Adsorption of amyloglucosidase on inorganic carriers

Biotechnology and Bioengineering, 1975
AbstractA simple method for immobilizing amyloglucosidase by adsorption on inorganic carriers is described. Amyloglucosidase was adsorbed on acid‐activated molecular sieve and on alumina. The immobilized enzyme preparations exhibited 50–100% of the initial activity and possessed high temperature stability.
B. Solomon, Y. Levin
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Amyloglucosidase immobilized on acrylic supports

Acta Biotechnologica, 1994
AbstractThis paper deals with the study of the behaviour of Amyloglucosidase covalently immobilized on acrylic supports in the maltodextrin hydrolysis process. The specific catalytic activity of the different immobilized Amyloglucosidase preparations critically depends on their protein content.
S. Maxim, A. Flondor, I. Bunia
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Action of amyloglucosidase on oxidised amylose

Carbohydrate Research, 1979
The Michaelis constant and maximal velocity of alpha-amylase-free amyloglucosidase decrease with increasing periodate oxidation of amylose. These kinetic features have been explained on the basis of competitive inhibition by the oxidised non-reducing end of the (1 leads to 4)-alpha-D-glucan chain with the active centres of the enzyme.
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Kinetische Bestimmungsmethode für Amyloglucosidase

Fresenius' Zeitschrift für analytische Chemie, 1980
Durch Einwirkung der Amyloglucosidase auf 0,1 % Starke wird Glucose freigesetzt. Die Geschwindigkeit der Glucosebildung ist ein Mas fur die Enzymaktivitat. Sie kann direkt im Mesansatz mittels Glucosedehydrogenase/NAD bei 340 nm verfolgt werden. Bei Verwendung einer Testpackung lassen sich etwa 15 Analysen/h mit einer Standardabweichung von 2–3 ...
H. Bartels, G. Römmele, M. Böhmer
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6,7-Diepicastanospermine, a tetrahydroxyindolizidine alkaloid inhibitor of amyloglucosidase

Biochemistry, 1991
A tetrahydroxyindolizidine alkaloid, 6,7-diepicastanospermine, was isolated from the seeds of Castanospermum australe by extraction with methanol and purified to homogeneity using ion-exchange, preparative thin-layer, and radial chromatography. A very low yield of a pyrrolidine alkaloid, N-(hydroxyethyl)-2-(hydroxymethyl)-3-hydroxypyrrolidine, was also
R J, Molyneux   +5 more
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Immobilization of amyloglucosidase onto granular chicken bone

Applied Biochemistry and Biotechnology, 1992
Amyloglucosidase was immobilized onto granular chicken bone (BIOBONE) by noncovalent interactions. The amount of activity bound relative to an equal amount of free enzyme was 13.6 +/- 0.4%. The estimated specific activity for amyloglucosidase decreased from 75.3 +/- 0.8 to 43.5 +/- 9.6 U/mg protein upon immobilization.
D Y, Schafhauser, K B, Storey
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Substrate recognition by amyloglucosidase: evaluation of conformationally biased isomaltosides

Carbohydrate Research, 1993
Amyloglucosidase catalyzes the hydrolysis of methyl beta-maltoside (1) 30-50 times more rapidly than methyl alpha-isomaltoside (2). It is established that OH-6', OH-4', and OH-4 which are involved in key polar interactions with the enzyme in the case of isomaltoside.
M M, Palcic   +4 more
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Immobilization of amyloglucosidase using two forms of polyurethane polymer

Applied Biochemistry and Biotechnology, 1990
Amyloglucosidase was covalently immobilized using two hydrophilic prepolymers: Hypol FHP 2002 (creates foams) and Hypol FHP 8190H (creates gels). The foamable prepolymer was superior as a support for enzyme immobilization. The percent activity immobilized in the polyurethane foams was 25 +/- 1.5%.
K B, Storey   +2 more
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