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Amino Acids

, Volume 47, Issue 9, pp 1805–1815 | Cite as

Use of the guanidination reaction for determining reactive lysine, bioavailable lysine and gut endogenous lysine

  • Shane M. RutherfurdEmail author
Review Article
Part of the following topical collections:
  1. Homoarginine, Arginine and Relatives

Abstract

Determining the bioavailability of lysine in foods and feedstuffs is important since lysine is often the first limiting indispensable amino acid in diets for intensively farmed livestock (pigs and poultry) and also in many cereal-based diets consumed by humans. When foods or feedstuffs are heat processed, lysine can undergo Maillard reactions to produce nutritionally unavailable products. The guanidination reaction, the reaction of O-methylisourea with the side chain amino group of lysine that produces homoarginine, has been used to determine the unmodified lysine (reactive lysine) in processed foods and feedstuffs and also true ileal digestible reactive lysine (bioavailable lysine). The advantages of the guanidination method in comparison with other reactive lysine methods such as the fluorodinitrobenzene, trinitrobenzenesulphonic acid and dye-binding methods are that it is very specific for reactive lysine and also that the method is relatively straightforward to conduct. The specificity of the guanidination reaction for the lysine side chain amino group is particularly important, since ileal digesta will contain N-terminal groups in the form of free amino acids and peptides. The main disadvantage is that complete conversion of lysine to homoarginine is required, yet it is not straightforward to test for complete guanidination in processed foods and feedstuffs. Another disadvantage is that the guanidination reaction conditions may vary for different food types and sometimes within the same food type. Consequently, food-specific guanidination reaction conditions may be required and more work is needed to optimise the reaction conditions across different foods and feedstuffs.

Keywords

Homoarginine Lysine Guanidination Reactive Bioavailable 

Notes

Conflict of interest

The author declares that there is no conflict of interest.

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Copyright information

© Springer-Verlag Wien 2015

Authors and Affiliations

  1. 1.Riddet InstituteMassey UniversityPalmerston NorthNew Zealand

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