Proline rich protein

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Proline-rich proteins (PRPs) is a class of intrinsically unstructured proteins[1] (IUP) containing several repeats of a short proline-rich sequence.

Many tannin-consuming animals secrete a tannin-binding protein (mucin) in their saliva. Tannin-binding capacity of salivary mucin is directly related to its proline content. Advantages in using salivary proline-rich proteins (PRPs) to inactivate tannins are :

  • PRPs inactivate tannins to a greater extent than do dietary proteins; this results in reduced fecal nitrogen losses,[2]
  • PRPs contain non specific nitrogen and nonessential amino acids; this makes them more convenient for an animal to exploit rather than using up valuable dietary protein.[3]

Example of this class of protein is IB5, a human parotid salivary protein known to bind with polyphenols (binding responsible for the astringency mouth feel). Other examples include Proline-Rich 12, Proline-Rich Protein 30, and Proline-Rich Protein 21.

References[]

  1. ^ Characterization, stoichiometry, and stability of salivary protein–tannin complexes by ESI-MS and ESI-MS/MS. Francis Canon, Franck Paté, Emmanuelle Meudec, Thérèse Marlin, Véronique Cheynier, Alexandre Giuliani and Pascale Sarni-Manchado, Analytical and Bioanalytical Chemistry, Volume 395, Number 8 / décembre 2009
  2. ^ René A. de Wijk, Jon F. Prinz, The role of friction in perceived oral texture, Food Quality and Preference 16 (2005) 121–129
  3. ^ "Tanins chemistry on www.users.muohio.edu" (PDF). Archived from the original (PDF) on 2013-08-26. Retrieved 2010-01-19.


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