Breakdown of N-terminally modified peptides and an isopeptide by rumen microorganisms

R. J. Wallace, P. P. Frumholtz, N. D. Walker

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Treatment of Trypticase peptides with acetic anhydride, succinic anhydride, or maleic anhydride inhibited their breakdown to ammonia by rumen microorganisms by an average of 89% after 12 h of incubation in vitro. All three treatments gave similar protection. Acetylation also protected dipeptides containing lysine and methionine from degradation. However, more effective protection was obtained by linking lysine and methionine as N-epsilon-methionyl lysine.
Original languageEnglish
Pages (from-to)3147-3149
Number of pages3
JournalApplied and Environmental Microbiology
Volume59
Issue number9
Publication statusPublished - Sep 1993

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rumen microorganisms
Rumen
Methionine
peptide
Lysine
lysine
ammonia
microorganism
incubation
Maleic Anhydrides
peptides
Peptides
degradation
methionine
Dipeptides
Acetylation
Ammonia
dipeptides
anhydrides
acetylation

Cite this

Breakdown of N-terminally modified peptides and an isopeptide by rumen microorganisms. / Wallace, R. J.; Frumholtz, P. P.; Walker, N. D.

In: Applied and Environmental Microbiology, Vol. 59, No. 9, 09.1993, p. 3147-3149.

Research output: Contribution to journalArticle

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