Rupendra Mukerjea
Iowa State University
30 Papers
318 Citations
Rupendra Mukerjea is an academic researcher from Iowa State University. The author has contributed to research in topics: Starch & Starch synthase. The author has an hindex of 14, co-authored 30 publications.
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Papers
Separation and quantitative determination of nanogram quantities of maltodextrins and isomaltodextrins by thin-layer chromatography
John F. Robyt,Rupendra Mukerjea +1 more
TL;DR: In this article, the TLC separation of maltodextrins and isomaltodextrin containing 1-20 glucose residues was performed by using densitometric scanning of a TLC plate with a linear relationship for 50 to 2000 ng of glucose.
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Dextransucrase and the mechanism for dextran biosynthesis.
TL;DR: It is shown how the three conserved amino acids at the active sites of glucansucrases participate in the polymerization of dextran and related glucans from a single active site by the addition of the D-glucose moiety of sucrose to the reducing-ends of the covalently linked glucan chains in a two catalytic-site, insertion mechanism.
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Biosynthesis of dextrans with different molecular weights by selecting the concentration of Leuconostoc mesenteroides B-512FMC dextransucrase, the sucrose concentration, and the temperature
TL;DR: The results of the study show that the molecular weights of the synthesized dextrans were inversely proportional to the concentration of the enzyme and directly proportional toThe concentration of sucrose and the temperature.
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Simplified and improved methylation analysis of saccharides, using a modified procedure and thin-layer chromatography
TL;DR: Methylation analysis used in determining the positions of glycosidic linkages in oligo- and poly-saccharides has been greatly simplified by eliminating two of the usual reactions, reduction and acetylation of the methylated monosaccharide residues.
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Starch biosynthesis: mechanism for the elongation of starch chains.
TL;DR: Starch granules from eight diverse plant sources all had active starch synthases and branching enzymes inside the granules, and evidence indicated that the synthase forms a high-energy covalent complex with D-glucose and the growing starch chain, and that the D- glucopyranosyl group is added to the reducing end of thegrowing starch chain by a two-site insertion mechanism.
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