ISSN:
1573-6776
Source:
Springer Online Journal Archives 1860-2000
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Summary The values of Km, Ea, and Ki (for product inhibition) of glucoamylase covalently bound to the waste mycelium were determined as 7.9mM, 71.4 kJ/mol, and 3.2 M resp. using maltose as the substrate. The bound enzyme is not subject to diffusion limitation in the range of the concentration used.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00139285