Results 141 to 150 of about 1,002,705 (170)
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International Journal of Biological Macromolecules
In practical applications, the gelatinisation temperature of starch is high. Most current glycogen branching enzymes (GBEs, EC 2.4.1.18) exhibit optimum activity at moderate or low temperatures and quickly lose their activity at higher temperatures, limiting the application of GBEs in starch modification.
Jie Long
exaly +3 more sources
In practical applications, the gelatinisation temperature of starch is high. Most current glycogen branching enzymes (GBEs, EC 2.4.1.18) exhibit optimum activity at moderate or low temperatures and quickly lose their activity at higher temperatures, limiting the application of GBEs in starch modification.
Jie Long
exaly +3 more sources
Vibrio vulnificus glycogen branching enzyme preferentially transfers very short chains: N1 domain determines the chain length transferred [PDF]
FEBS Letters, 2015 The glycogen branching enzyme from Vibrio vulnificus (VvGBE) transfers short side chains (DP 3–5) significantly greater than any other bacterial glycogen branching enzyme (GBE).
Jong-Tae Park, Sunghoon Park
exaly +2 more sources
Factors influencing glycogen branching enzyme activity in mouse liver [PDF]
, 2022 Glycogen is the storage polysaccharide in a spectrum of organisms ranging from yeast to humans. Glycogen has a highly branched structure somewhat resembling a tree or shrub, with the branch points formed by glucose molecules being joined by α 1,6 ...
Fuller, Scott
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Biochimica Et Biophysica Acta - General Subjects, 2013 Background: Glycogen and starch branching enzymes catalyze the formation of alpha(1 -> 6) linkages in storage polysaccharides by rearrangement of preexisting alpha-glucans.
D'Hulst C +2 more
exaly +2 more sources
Glycogen branching enzyme in Lafora myoclonus epilepsy
Biochemical Medicine, 1982Abstract Glycogen branching enzymes (EC 2.4.1.18) in extracts of cerebral cortex from a patient with Lafora myoclonus epilepsy and several normal subjects were compared in terms of activity and physical properties of the proteins. Branching-enzyme activity in Lafora cortex tissue was significantly higher than in controls. Gel-exclusion chromatography
C P, Zimmerman, A M, Gold
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International Journal of Biological Macromolecules, 2022
Glycogen-like particles (GLPs) were built up from sucrose by applying de novo one-pot enzymatic process of amylosucrase (ASase; 6 U·mL-1) and glycogen branching enzymes (GBEs; 0.001 and 0.005 U·mL-1). Due to different chain-length transferring patterns of GBEs, structurally differentiated GLPs were synthesized.
Daeyeon, Lee +5 more
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Glycogen-like particles (GLPs) were built up from sucrose by applying de novo one-pot enzymatic process of amylosucrase (ASase; 6 U·mL-1) and glycogen branching enzymes (GBEs; 0.001 and 0.005 U·mL-1). Due to different chain-length transferring patterns of GBEs, structurally differentiated GLPs were synthesized.
Daeyeon, Lee +5 more
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Apparent absence of glycogen branching enzyme activity in phosphofructokinase deficiency
Journal of Inherited Metabolic Disease, 1991SummaryA 30‐year‐old woman with clinical features and biochemical findings of muscle phosphofructokinase deficiency was found to have a very low level of α‐1,4‐glucan:α‐1,4‐glucan‐6‐transglucosylase (branching enzyme, EC 2.4.1.18) activity in muscle. In contrast, branching enzyme activity in the leukocytes was in the range of control values.
V, Barash +3 more
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Alteration of mitochondrial function in the livers of mice with glycogen branching enzyme deficiency
Biochimie, 2021Glycogen storage disease type IV (GSD IV) is caused by mutations in the glycogen branching enzyme gene (GBE1) that lead to the accumulation of aberrant glycogen in affected tissues, mostly in the liver. To determine whether dysfunctional glycogen metabolism in GSD IV affects other components of cellular bioenergetics, we studied mitochondrial function ...
Dominika Malinska +5 more
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Structure-function relationships of glycogen branching enzymes
, 2011 The new findings described in the thesis of Marta Palomo (which led to a patent application) are particularly valuable for understanding how glycogen is made and are important for developing new types of branched α -glucan polymers.
Palomo Reixach, Marta +1 more
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Mode of Action of Glycogen Branching Enzyme from Neurospora crassa
The Journal of Biochemistry, 1990Neurospora crassa branching enzyme [EC 2.4.1.18] acted on potato amylopectin or amylose to convert them to highly branched glycogen-type molecules which consisted of unit chains of six glucose units. The enzyme also acted on the amylopectin beta-limit dextrin, indicating that the enzyme acted on internal glucose chains as well as outer chains.
A, Matsumoto, T, Nakajima, K, Matsuda
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