نتایج جستجو برای: cyclodextrin glucosyl transferase cgtase

تعداد نتایج: 37729  

Journal: :Food Hydrocolloids 2021

Abstract The action of the enzyme CGTase on corn and potato starch was studied to understand influence structure cyclodextrin (CD) production. Native hydrolysed materials were analysed using multiple characterisation methods enabling coverage over more than six orders magnitude in length-scale. production CD greater for but relative abundance between different molecules conserved. Structural di...

Journal: :Infection and immunity 1974
D M Spinell R J Gibbons

Growth of Streptococcus mutans 6715 in a medium containing trace amounts of sucrose or dextran promotes cell-associated glucosyl transferase activity and increases the dextran-binding capacity of the organisms.

Journal: :Journal of molecular biology 1996
K Sorimachi A J Jacks M F Le Gal-Coëffet G Williamson D B Archer M P Williamson

The solution structure of the granular starch binding domain (SBD) of glucoamylase 1 from Aspergillus niger has been determined by heteronuclear multidimensional nuclear magnetic resonance spectroscopy and simulated annealing. A total of 1092 nuclear Overhauser enhancement-derived 1H-1H distance constraints, 137 dihedral constraints and 86 hydrogen bond constraints were incorporated into an X-P...

Journal: :Journal of biochemistry and molecular biology 2003
Jarunee Kaulpiboon Piamsook Pongsawasdi

The isoform 1 of cyclodextrin glycosyltransferase (CGTase, EC 2.4.1.19) from Paenibacillus sp. A11 was purified by a preparative gel electrophoresis. The importance of histidine, tryptophan, tyrosine, and carboxylic amino acids for isoform 1 activity is suggested by the modification of the isoform 1 with various group-specific reagents. Activity loss, when incubated with diethylpyrocarbonate (D...

Journal: :Plant physiology 1974
J C Linden W Tanner O Kandler

A glucosyl and a glucosyl-glucan transferase activity from spinach (Spinacia oleracea L. var. Matador) leaves have been partially purified and characterized. The latter activity (fraction 1 after diethylaminoethylcellulose chromatography) is responsible for the transfer of glucosyl as well as of maltosyl, maltotriosyl, and higher homologous residues to glucose giving rise to maltose and the cor...

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