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Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21Enzymology and Structure of the GH13_31 Glucan 1,6- -Glucosidase That Confers Isomaltooligosaccharide Utilization in the Probiotic Lactobacillus acidophilus NCFMOligosaccharide and substrate binding in the starch debranching enzyme barley limit dextrinaseCrystal structure of barley limit dextrinase-limit dextrinase inhibitor (LD-LDI) complex reveals insights into mechanism and diversity of cereal type inhibitors.Structure and function of α-glucan debranching enzymes.An Extracellular Cell-Attached Pullulanase Confers Branched α-Glucan Utilization in Human Gut Lactobacillus acidophilus.Structural biology of starch-degrading enzymes and their regulation.Recent insight into oligosaccharide uptake and metabolism in probiotic bacteriaRecent insight in α-glucan metabolism in probiotic bacteriaFunctional Roles of Starch Binding Domains and Surface Binding Sites in Enzymes Involved in Starch BiosynthesisA Snapshot into the Metabolism of Isomalto-oligosaccharides in Probiotic BacteriaSurface Binding Sites (SBSs), Mechanism and Regulation of Enzymes Degrading Amylopectin and α-Limit DextrinsEfficient secretory expression of functional barley limit dextrinase inhibitor by high cell-density fermentation of Pichia pastorisA carbohydrate-binding family 48 module enables feruloyl esterase action on polymeric arabinoxylanRoles of the N-terminal domain and remote substrate binding subsites in activity of the debranching barley limit dextrinase
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P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Marie S Møller
@ast
Marie S Møller
@en
Marie S Møller
@es
Marie S Møller
@nl
type
label
Marie S Møller
@ast
Marie S Møller
@en
Marie S Møller
@es
Marie S Møller
@nl
prefLabel
Marie S Møller
@ast
Marie S Møller
@en
Marie S Møller
@es
Marie S Møller
@nl
P106
P31
P496
0000-0001-9017-3367