Results 151 to 160 of about 82,389 (203)

Glucose - 6 - phosphate isomerase

Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1981
Glucose-6-phosphate isomerase (EC 5 . 3 .1 .9) is a dimeric enzyme of molecular mass 132000 which catalyses the interconversion of D-glucose-6-phosphate and D-fructose- 6-phosphate. The crystal structure of the enzyme from pig muscle has been determined at a nominal resolution of 2.6 A. The structure is of the a/B type.
A, Achari, S E, Marshall, H, Muirhead, R H, Palmieri, E A, Noltmann   +4 more
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Thermoinactivation mechanism of glucose isomerase

Applied Biochemistry and Biotechnology, 2007
In this article, the mechanisms of thermoinactivation of glucose isomerase (GI) from Streptomyces rubiginosus (in soluble and immobilized forms) were investigated, particularly the contributions of thiol oxidation of the enzyme's cysteine residue and a "Maillard-like" reaction between the enzyme and sugars in high fructose corn syrup (HFCS). Soluble GI
Leng Hong, Lim, Bradley A, Saville
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Glucose sensor with immobilized glucose oxidase-glucose isomerase membrane

Journal of Molecular Catalysis, 1981
Abstract A glucose sensor, i.e., an oxygen detection electrode with immobilized glucose oxidase, has been studied by several researchers as a novel analytical technique which can simplify tedious steps in conventional methods of glucose determination. In a glucose sensor of such construction, any glocuse oxidase inhibition will impair the performance
Shinichiro Gondo, Tomeo Osaki, Michio Morishita   +2 more
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Substrate protection of immobilized glucose isomerase

Biotechnology and Bioengineering, 1987
AbstractUsing commercial immobilized glucose isomerase (SWETASE®, Nagase Co.), the effect of substrate protection on enzyme deactivation has been studied in a batch manner. The data analysis was carried out based on Briggs‐Haldane kinetics in which enzyme deactivation accompanying the protection of substrates was also considered.
K C, Chen, J Y, Wu
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Immobilization of glucose isomerase

Zeitschrift für allgemeine Mikrobiologie, 1982
AbstractThe immobilization of glucose isomerase (D‐xylose ketol isomerase, EC 5.3.1.5) by covalently bonding to various carriers and by adsorption to ion exchange resins was attempted in order to obtain a stable immobilized enzyme which can be used for continuous isomerization of glucose in a column.Of the covalent bonding methods, the colloidal silica‐
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Polyhedral Instability of Glucose Isomerase Crystals

Crystal Growth & Design, 2008
The problem of polyhedral (in)stability for the crystallization of macromolecules is discussed. We present both qualitative and quantitative data on the transition of face morphology in response to surface concentration gradients for the case of glucose isomerase.
Sleutel, Mike, Willaert, Ronnie, Wyns, Lode, Maes, Dominique   +3 more
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Thermostable glucose isomerases

Trends in Food Science & Technology, 1993
Abstract During the past two decades, the use of immobilized glucose isomerase for the production of high-fructose corn syrup has evolved into a highly optimized industrial process. The desire for higher process temperatures has stimulated the screening of extreme thermophilic organisms for more thermostable glucose isomerases; protein engineering ...
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Glucose-isomerase in Barley Malt

Nature, 1960
WORK in this Institute on the enzymatic breakdown of starch has included above all the qualitative and quantitative determination of products resulting from this breakdown1. We have observed that in every case fructose occurred beside the glucose derivatives already in the barley malt extract2.
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Production of glucose isomerase by genus Streptomyces

Zeitschrift für allgemeine Mikrobiologie, 1982
AbstractScreening for glucose isomerases was done using 46 species and 63 strains of Streptomyces type cultures. Glucose isomerase was found in a wide range of these species. The intracellular glucose isomerase of S. olivochromogenes showed the highest fructose conversion ratio.
M, Suekane, H, Iizuka
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Safety evaluation of Streptomyces murinus glucose isomerase

Toxicology Letters, 1987
A glucose isomerase enzyme, obtained from Streptomyces murinus, was produced by a fermentation process and subjected to a series of tests to investigate its safety in use and manufacture. It was not mutagenic (Ames test, using liquid culture) nor did it provoke chromosomal damage (rat bone marrow cytogenetics test).
R. Ashby, R.K. Hjortkjaer, M. Stavnsbjerg, H. Gurtler, P.B. Pedersen, J. Bootman, G. Hudson-Walker, J.M. Tesh, C.R. Willoughby, H. West, J.P. Finn   +10 more
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