Proline rich protein

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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