Digestibility of extruded proteins and metabolic transit of N^sup [epsilon]^-carboxymethyllysine in rats

• Published in: Amino acids 2013-06, Vol.44 (6), p.1441
• Main Authors: Alamir, Issam, Niquet-leridon, Céline, Jacolot, Philippe, Rodriguez, Camille, Orosco, Martine, Anton, Pauline M, Tessier, Frédéric J
• Format: Article
• Language: English
• ISSN: 0939-4451; 1438-2199
• DOI: 10.1007/s00726-012-1427-3

Issue Title: Glycation Section Milk proteins are frequently used as supplements in fortified foods. However, processing produces chemical changes which likely affect the nutritional advantage. This study was intended to explore the possible difference in digestibility between extruded and non-extruded caseins and how the dietary N ^sup [straight epsilon]^-carboxymethyllysine (CML) is metabolised. Normal rats were randomized into either an extruded protein diet (EP) or the same with unextruded proteins (UEP), for two periods of 2 weeks at 7 to 9 and 11 to 13 weeks of age. However, no difference in protein digestibility was detected between the two diets, either in young or in adult animals, despite a 9.4-fold higher level of CML and an 8.5-fold higher level of lysinoalanine in the EP than in the UEP. No diet-related changes were observed in plasma CML, either protein bound or free. Amounts of 38 and 48 % of the orally absorbed CML were excreted in urine and faeces, respectively, in UEP-fed rats. Lower rates of excretion were found in the EP-fed rats (23 and 37 %, respectively). A second animal study using a single oral dose of free CML (400 [mu]g/rat) was set up to measure the systemic concentration of CML every hour from 0 to 4 h. It revealed that protein-bound CML was not affected by the oral dose of CML, and the highest free CML level found in the circulation was 600 ng/mL. Extruded proteins, therefore, appear to be well digested, and CML rapidly eliminated. Since its elimination is, however, incomplete, the question of its biodistribution and metabolism remains open.[PUBLICATION ABSTRACT]