Haines, Alan H. (2006) Non-equivalence of d- and l-trehalose in stabilising alkaline phosphatase against freeze-drying and thermal stress. Is chiral recognition involved? Organic and Biomolecular Chemistry, 4 (4). pp. 702-706. ISSN 1477-0520
Full text not available from this repository. (Request a copy)Abstract
Comparison of the ability of the enantiomeric forms of trehalose to stabilise alkaline phosphatase towards dehydration and heat showed that natural d-trehalose is superior to l-trehalose, although both disaccharides provide some protection for the enzyme. The result of this novel experiment suggests a chiral differentiation between carbohydrate and protein and thus lends support for the water replacement hypothesis of solute-based stabilisation of biomolecules, but the non-crystallinity and the physical form of the l-isomer may also be a key factor.
Item Type: | Article |
---|---|
Uncontrolled Keywords: | biochemistry,physical and theoretical chemistry,organic chemistry ,/dk/atira/pure/subjectarea/asjc/1300/1303 |
Faculty \ School: | Faculty of Science > School of Chemistry |
Related URLs: | |
Depositing User: | LivePure Connector |
Date Deposited: | 14 Jul 2022 12:30 |
Last Modified: | 23 Oct 2022 03:52 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/86106 |
DOI: | 10.1039/b514473f |
Actions (login required)
![]() |
View Item |