Kinetics of formation of maltose and isomaltose through condensation of glucose by glucoamylase
โ Scribed by Shuji Adachi; Yasuo Ueda; Kenji Hashimoto
- Publisher
- John Wiley and Sons
- Year
- 1984
- Tongue
- English
- Weight
- 553 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0006-3592
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๐ SIMILAR VOLUMES
Kinetic results on the glucoamylase-catalysed hydrolysis of maltose and maltotriose, and glucose polymerization into maltose and isomaltose up to 450 g/L total sugar concentration are presented. Whereas the enzyme has a faster hydrolytic and synthetic activity on ~(1'4) than on a-(I -6) linkages, at
The binding of maltose, isomaltose, and D-glucono-1,5-lactone to the glucoamylase [E.C.3.2.1.3] from Aspergillus niger was monitored by the fluorescence-intensity change (delta F) based on the tryptophan residues of the enzyme, and the binding parameters (Kd and delta Fmax) were evaluated from the d
Arabinose, fructose, galactose, myo-inositol, lyxose, mannose, ribose, and xylose were incubated individually and with glucose in the presence of Aspergillus niger glucoamylase at pH 4.5 and 45ยฐC. Glucoamy- lase condenses galactose, glucose, and mannose individually into disaccharides. It also produ