|
type |
Journal Article |
authors |
Nahálka J |
title |
Physiological aggregation of maltodextrin phosphorylase from Pyrococcus furiosus and its application in a process of batch starch degradation to alpha-D-glucose-1-phosphate |
journal |
J Ind Microbiol Biotechnol |
Activity |
2.4.1.1 |
Family |
2.4.1.1 |
sel |
selected |
ui |
18087736 |
year |
(2008) |
volume |
35 |
number |
4 |
pages |
219-23 |
| |
abstract |
Maltodextrin phosphorylase from Pyrococcus furiosus (PF1535) was fused with the cellulose-binding domain of Clostridium cellulovorans serving as an aggregation module. After molecular cloning of the corresponding gene fusion construct and controlled expression in Escherichia coli BL21, 83% of total maltodextrin phosphorylase activity (0.24 U/mg of dry cell weight) was displayed in active inclusion bodies. These active inclusion bodies were easily isolated by nonionic detergent treatment and directly used for maltodextrin conversion to alpha-D-glucose-1-phosphate in a repetitive batch mode. Only 10% of enzyme activity was lost after ten conversion cycles at optimum conditions. |
last changed |
2018/05/24 13:46 |
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