Non-equivalence of d- and l-trehalose in stabilising alkaline phosphatase against freeze-drying and thermal stress. Is chiral recognition involved?

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

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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: 15 Jul 2022 00:24
URI: https://ueaeprints.uea.ac.uk/id/eprint/86106
DOI: 10.1039/b514473f

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