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Acetylation of peptides inhibits their degradation by rumen micro-organisms

Published online by Cambridge University Press:  09 March 2007

R. J. Wallace
R. J. Wallace
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
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Abstract

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Proteins and peptides were acetylated using acetic anhydride in order to block their N-terminal amino groups and thereby to prevent their hydrolysis by rumen microbial aminopeptidases. The effects of acetylation on peptide breakdown and ammonia production were determined by incubating unmodified and acetylated substrates with sheep rumen micro-organisms in vitro. Ammonia production from casein and lactalbumin was affected little by acetylation, but acetylation of the corresponding enzymic hydrolysates caused ammonia production to be more than halved after 3.6 h incubation. Estimation of peptides remaining in rumen fluid showed that the decreased ammonia production was a consequence of peptides being hydrolysed more slowly. Acetylated Ala-Ala, Ala-Ala-Ala (Ala3), Leu-Gly-Gly, Phe-Gly-Gly and Val-Gly-Ser-Glu survived incubation with rumen fluid in vitro for 6 h, whereas almost none of the corresponding unmodified peptides was present at 6 h. The protection afforded to larger pure peptides was less reliable: for example, 72% of acetylated bradykinin was hydrolysed after 1 h. N-Acetyl Ala3 had only a minor inhibitory effect on the breakdown of Ala3 and Ala4, suggesting that although acetyl peptides were broken down more slowly than unmodified peptides they did not inhibit peptidase activity.

Keywords

Rumen peptide breakdownProtection by acetylationSheep
Type
Protein Digestion and Metabolism
Information
British Journal of Nutrition , Volume 68 , Issue 2 , September 1992 , pp. 365 - 372
Copyright
Copyright © The Nutrition Society 1992

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