| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 71174 | Journal of Molecular Catalysis B: Enzymatic | 2007 | 5 Pages |
A novel cross-linked enzyme aggregates (CLEA) concept called combi-CLEA has been described. It is based upon the fact that CLEA can be made from heterogeneous populations of proteins/enzymes. Porcine pancreatic acetone powder crude extract was used for preparing CLEA in such a way that lipase, α-amylase, phospholipase A2 activities were retained upto 100%. The lipase present in the CLEA showed greater thermal stability at 50 °C as compared to free enzyme. For lipase and phospholipase A2, Vmax/Km showed no significant change upon combi-CLEA formation but decreased significantly for α-amylase activity from 190 to 114 min−1. The lipase activity and α-amylase activity in CLEA were completely retained upto three cycles of use. The scanning electron microscopic (SEM) studies showed that morphology of CLEA changed upon inactivation by reuses.
