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Investigations on the Guanidination of Lysine in Proteins
Author(s) -
Imbeah Maleena,
Angkanaporn Kris,
Ravindran Velmurugu,
Bryden Wayne L.
Publication year - 1996
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/(sici)1097-0010(199610)72:2<213::aid-jsfa641>3.0.co;2-n
Subject(s) - chemistry , lysine , casein , reagent , food science , biochemistry , amino acid , organic chemistry
The present study was conducted to compare the efficacy of five different reaction conditions on the guanidination of lysine in casein and to establish optimum lysine: O ‐methylisourea (OMIU) for maximum guanidination of lysine in casein and soya bean meal. The results indicate that the presence of glycine–NaOH buffer is not required for guanidination of proteins at pH 10·5. A OMIU concentration of 0·4 M was found to be as effective as 0·6 M for guanidination. Both OMIU–hydrogen sulphate and free OMIU were equally effective reagents in terms of conversion of lysine to homoarginine. The use of OMIU–hydrogen sulphate for guanidination and the use of ethanol to recover guanidinated protein, however, resulted in the formation of crystalline sodium sulphate, a known purgative agent, in the guanidinated material, and therefore are not recommended if the guanidinated protein is to be used in animal trials. The molar ratio of lysine: OMIU required for efficient lysine conversion to homoarginine varied for different protein sources. Ratios required for maximum conversion for casein and soya bean meal were determined to be 1:10 and 1:16, respectively. A simple procedure developed for the large‐scale guanidination (5–10 kg batches) of proteins is also described. The results showed that guanidination of proteins can be easily scaled up from 20 g to 5–10 kg and that large‐scale guanidination is feasible and efficient.