We have located links that may give you full text access.
Improved stability of immobilized lipases via modification with polyethylenimine and glutaraldehyde.
Enzyme and Microbial Technology 2017 November
Phospholipase Lecitase Ultra (LU) and lipase from Thermomyces lanuginosus (TLL) have been immobilized under conditions that favor either enzyme crowding or enzyme dispersion. Highly loaded LU was more stable than low loaded biocatalyst under all studied conditions. Using TLL, the results depended on the inactivation conditions, e.g., crowding was positive at pH 5 and negative at pH 7. Then, all preparations were treated with glutaraldehyde (Glu), polyethyleneimine (PEI) or sequentially with Glu and PEI. These treatments may permit to stabilize the physically immobilized lipases by avoiding enzyme desorption via intermolecular crosslinking. Moreover, immobilizing a second enzyme on the lipase-glutaraldehyde-PEI has been proposed as a strategy without risks of PEI desorption by incubation in high ion strength solutions. The treatments altered the enzyme activity slightly but produced significant enzyme stabilization. This enzyme stabilization was more significant when using the highly loaded preparations, where intermolecular crosslinking was easier to obtain. SDS-PAGE analyses confirmed that crowded enzyme preparations were intermolecular crosslinked using Glu plus PEI, but some molecules still remained non-crosslinked. In general, PEI treatment was the most effective in increasing enzyme stability, while glutaraldehyde had a milder stabilization effect.
Full text links
Related Resources
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app
All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.
By using this service, you agree to our terms of use and privacy policy.
Your Privacy Choices
You can now claim free CME credits for this literature searchClaim now
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app