Breakdown of different peptides by Prevotella (Bacteroides) ruminicola and mixed microorganisms from the sheep rumen

R. J. Wallace, N. McKain, G. A. Broderick

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Several di-, tri-, and oligopeptides were incubated individually in vitro with rumen fluid from two sheep receiving a mixed grass hay/concentrate diet and with washed cells of Prevotella (formerly Bacteroides) ruminicola M384 and P. ruminicola B(1)4. The rates of breakdown of most peptides were similar in the rumen fluid from the two sheep. Acidic and proline-containing peptides tended to be more slowly degraded than neutral or basic peptides. The dipeptide at the N-terminus of higher peptides was observed as an early product of hydrolysis, confirming that a dipeptidyl aminopeptidase type of activity was present. The relative rates of breakdown of dipeptides by P. ruminicola were different from that of rumen fluid, but the hydrolysis of higher peptides followed a similar pattern, and dipeptides from the N-terminus were detected as early products.
Original languageEnglish
Pages (from-to)333-336
Number of pages4
JournalCurrent Microbiology
Volume26
Issue number6
Publication statusPublished - Jun 1993

Fingerprint

Prevotella ruminicola
Bacteroides
Rumen
Sheep
Dipeptides
Peptides
Hydrolysis
Prevotella
Oligopeptides
Aminopeptidases
Poaceae
Proline
Diet

Cite this

Breakdown of different peptides by Prevotella (Bacteroides) ruminicola and mixed microorganisms from the sheep rumen. / Wallace, R. J.; McKain, N.; Broderick, G. A.

In: Current Microbiology, Vol. 26, No. 6, 06.1993, p. 333-336.

Research output: Contribution to journalArticle

@article{b18ce385168f4c8587fe07c659000acc,
title = "Breakdown of different peptides by Prevotella (Bacteroides) ruminicola and mixed microorganisms from the sheep rumen",
abstract = "Several di-, tri-, and oligopeptides were incubated individually in vitro with rumen fluid from two sheep receiving a mixed grass hay/concentrate diet and with washed cells of Prevotella (formerly Bacteroides) ruminicola M384 and P. ruminicola B(1)4. The rates of breakdown of most peptides were similar in the rumen fluid from the two sheep. Acidic and proline-containing peptides tended to be more slowly degraded than neutral or basic peptides. The dipeptide at the N-terminus of higher peptides was observed as an early product of hydrolysis, confirming that a dipeptidyl aminopeptidase type of activity was present. The relative rates of breakdown of dipeptides by P. ruminicola were different from that of rumen fluid, but the hydrolysis of higher peptides followed a similar pattern, and dipeptides from the N-terminus were detected as early products.",
author = "Wallace, {R. J.} and N. McKain and Broderick, {G. A.}",
note = "Medline is the source for the MeSH terms of this document.",
year = "1993",
month = "6",
language = "English",
volume = "26",
pages = "333--336",
journal = "Current Microbiology",
issn = "0343-8651",
publisher = "Springer New York",
number = "6",

}

TY - JOUR

T1 - Breakdown of different peptides by Prevotella (Bacteroides) ruminicola and mixed microorganisms from the sheep rumen

AU - Wallace, R. J.

AU - McKain, N.

AU - Broderick, G. A.

N1 - Medline is the source for the MeSH terms of this document.

PY - 1993/6

Y1 - 1993/6

N2 - Several di-, tri-, and oligopeptides were incubated individually in vitro with rumen fluid from two sheep receiving a mixed grass hay/concentrate diet and with washed cells of Prevotella (formerly Bacteroides) ruminicola M384 and P. ruminicola B(1)4. The rates of breakdown of most peptides were similar in the rumen fluid from the two sheep. Acidic and proline-containing peptides tended to be more slowly degraded than neutral or basic peptides. The dipeptide at the N-terminus of higher peptides was observed as an early product of hydrolysis, confirming that a dipeptidyl aminopeptidase type of activity was present. The relative rates of breakdown of dipeptides by P. ruminicola were different from that of rumen fluid, but the hydrolysis of higher peptides followed a similar pattern, and dipeptides from the N-terminus were detected as early products.

AB - Several di-, tri-, and oligopeptides were incubated individually in vitro with rumen fluid from two sheep receiving a mixed grass hay/concentrate diet and with washed cells of Prevotella (formerly Bacteroides) ruminicola M384 and P. ruminicola B(1)4. The rates of breakdown of most peptides were similar in the rumen fluid from the two sheep. Acidic and proline-containing peptides tended to be more slowly degraded than neutral or basic peptides. The dipeptide at the N-terminus of higher peptides was observed as an early product of hydrolysis, confirming that a dipeptidyl aminopeptidase type of activity was present. The relative rates of breakdown of dipeptides by P. ruminicola were different from that of rumen fluid, but the hydrolysis of higher peptides followed a similar pattern, and dipeptides from the N-terminus were detected as early products.

UR - http://www.scopus.com/inward/record.url?scp=0027196329&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0027196329

VL - 26

SP - 333

EP - 336

JO - Current Microbiology

JF - Current Microbiology

SN - 0343-8651

IS - 6

ER -