Non-equivalence of D- and L-trehalose in stabilising alkaline phosphatase against freeze-drying and thermal stress. Is chiral recognition involved?
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.
Haines
Alan H
AH
Centre for Carbohydrate Chemistry, School of Chemical Sciences and Pharmacy, University of East Anglia, Norwich, UKNR4 7TJ. a.haines@uea.ac.uk
D000469:Alkaline Phosphatase / Q000737:chemistry* / Q000378:metabolism*; D004795:Enzyme Stability / Q000187:drug effects; D005612:Freeze Drying; D006358:Hot Temperature; D009596:Nitrophenols / Q000378:metabolism; D013237:Stereoisomerism; D014199:Trehalose / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*
D009596:Nitrophenols; D014199:Trehalose; D000469:Alkaline Phosphatase; C024836:4-nitrophenol