I'm looking for an assay for peptide racemization. A broad-spectrum exopeptidase like carboxypeptidase Y would be great, and I did find a reference (unavailable to my institution, so I can't read much of it) where it is shown to cleave L- but not D- esters, so that suggests it might be suitable for peptides.
I have only worked with a relatively small group of exopeptidases - specifically the oxytocinase subfamily of M1 amino peptidases, but they seem to fail to effectively cleave off D-amino acids (see attached paper, Figure 1). I would imagine that any member of the M1 family would behave similarly.
Dear Michael
Usually proteases don't cleave D-amino acids, in fact it is a common way to protect peptides from protease attack, in this way proteases are enantioselective for L-amino acids. Even so, its selectivity can be enhanced by addition of some compounds as you can find in this reference.
Jaap Broos, Johan F. J. Engbersen, Willem Verboom and David N. Reinhoudt. Inversion of enantioselectivity of serine proteases. Recueil des Travaux Chimiques des Pays-Bas. Volume 114, Issue 4-5, pages 255–257, 1995
http://onlinelibrary.wiley.com/doi/10.1002/recl.19951140421/abstract
I hope it can be usefull
Best regards
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