Gel filtration studies of peptide metabolism by rumen microorganisms

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

Peptide metabolism by rumen microorganisms was investigated by gel filtration using Sephadex G-25 with water as eluant. Protein hydrolysates containing a mixture of peptides were used to calibrate the column. Total peptide in each fraction was estimated from its A206, and free peptide amino groups were analysed by fluorescamine, thus enabling the average peptide Mr to be calculated. Three different protein hydrolysates produced similar, nearly linear, relations between log Mr and elution volume for peptides between 300 and 2000 Da. Trypticase, a pancreatic hydrolysate of casein, was metabolised rapidly in rumen fluid in vitro. Hydrolysis appeared to be complete after 6 h, leaving a small residual peptide concentration which persisted up to 24 h, equivalent to about 15% of the original peptide concentration of 2 g litre−1. Residual peptides from casein hydrolysis were 0.05 g litre−1 at 24 h. Peptides accumulated in rumen fluid of sheep receiving dietary ionophores. Two hours after feeding, the accumulation with monensin appeared to be of peptides of a wide Mr range, while tetronasin caused an accumulation mainly of smaller, <570 Da, peptides. Treatment of Trypticase with acetic anhydride afforded 76% protection of its peptides from degradation to ammonia in a 6-h incubation. When Trypticase was fractionated by gel filtration then acetylated, none of the fractions was protected significantly better than others.
Original languageEnglish
Pages (from-to)177-184
Number of pages8
JournalJournal of the Science of Food and Agriculture
Volume58
Issue number2
DOIs
Publication statusPublished - 1992

Fingerprint

rumen microorganisms
Rumen
Gel Chromatography
gels
peptides
Peptides
metabolism
Protein Hydrolysates
protein hydrolysates
rumen fluids
Hydrolysis
hydrolysis
Fluorescamine
Monensin
casein hydrolysates
monensin
Ionophores
ionophores
Caseins
Ammonia

Cite this

Gel filtration studies of peptide metabolism by rumen microorganisms. / Wallace, R. John.

In: Journal of the Science of Food and Agriculture, Vol. 58, No. 2, 1992, p. 177-184.

Research output: Contribution to journalArticle

@article{33e71fb1670549e794b372ee7642d5a0,
title = "Gel filtration studies of peptide metabolism by rumen microorganisms",
abstract = "Peptide metabolism by rumen microorganisms was investigated by gel filtration using Sephadex G-25 with water as eluant. Protein hydrolysates containing a mixture of peptides were used to calibrate the column. Total peptide in each fraction was estimated from its A206, and free peptide amino groups were analysed by fluorescamine, thus enabling the average peptide Mr to be calculated. Three different protein hydrolysates produced similar, nearly linear, relations between log Mr and elution volume for peptides between 300 and 2000 Da. Trypticase, a pancreatic hydrolysate of casein, was metabolised rapidly in rumen fluid in vitro. Hydrolysis appeared to be complete after 6 h, leaving a small residual peptide concentration which persisted up to 24 h, equivalent to about 15{\%} of the original peptide concentration of 2 g litre−1. Residual peptides from casein hydrolysis were 0.05 g litre−1 at 24 h. Peptides accumulated in rumen fluid of sheep receiving dietary ionophores. Two hours after feeding, the accumulation with monensin appeared to be of peptides of a wide Mr range, while tetronasin caused an accumulation mainly of smaller, <570 Da, peptides. Treatment of Trypticase with acetic anhydride afforded 76{\%} protection of its peptides from degradation to ammonia in a 6-h incubation. When Trypticase was fractionated by gel filtration then acetylated, none of the fractions was protected significantly better than others.",
author = "Wallace, {R. John}",
note = "97",
year = "1992",
doi = "10.1002/jsfa.2740580204",
language = "English",
volume = "58",
pages = "177--184",
journal = "Journal of the Science of Food and Agriculture",
issn = "0022-5142",
publisher = "John Wiley and Sons Ltd",
number = "2",

}

TY - JOUR

T1 - Gel filtration studies of peptide metabolism by rumen microorganisms

AU - Wallace, R. John

N1 - 97

PY - 1992

Y1 - 1992

N2 - Peptide metabolism by rumen microorganisms was investigated by gel filtration using Sephadex G-25 with water as eluant. Protein hydrolysates containing a mixture of peptides were used to calibrate the column. Total peptide in each fraction was estimated from its A206, and free peptide amino groups were analysed by fluorescamine, thus enabling the average peptide Mr to be calculated. Three different protein hydrolysates produced similar, nearly linear, relations between log Mr and elution volume for peptides between 300 and 2000 Da. Trypticase, a pancreatic hydrolysate of casein, was metabolised rapidly in rumen fluid in vitro. Hydrolysis appeared to be complete after 6 h, leaving a small residual peptide concentration which persisted up to 24 h, equivalent to about 15% of the original peptide concentration of 2 g litre−1. Residual peptides from casein hydrolysis were 0.05 g litre−1 at 24 h. Peptides accumulated in rumen fluid of sheep receiving dietary ionophores. Two hours after feeding, the accumulation with monensin appeared to be of peptides of a wide Mr range, while tetronasin caused an accumulation mainly of smaller, <570 Da, peptides. Treatment of Trypticase with acetic anhydride afforded 76% protection of its peptides from degradation to ammonia in a 6-h incubation. When Trypticase was fractionated by gel filtration then acetylated, none of the fractions was protected significantly better than others.

AB - Peptide metabolism by rumen microorganisms was investigated by gel filtration using Sephadex G-25 with water as eluant. Protein hydrolysates containing a mixture of peptides were used to calibrate the column. Total peptide in each fraction was estimated from its A206, and free peptide amino groups were analysed by fluorescamine, thus enabling the average peptide Mr to be calculated. Three different protein hydrolysates produced similar, nearly linear, relations between log Mr and elution volume for peptides between 300 and 2000 Da. Trypticase, a pancreatic hydrolysate of casein, was metabolised rapidly in rumen fluid in vitro. Hydrolysis appeared to be complete after 6 h, leaving a small residual peptide concentration which persisted up to 24 h, equivalent to about 15% of the original peptide concentration of 2 g litre−1. Residual peptides from casein hydrolysis were 0.05 g litre−1 at 24 h. Peptides accumulated in rumen fluid of sheep receiving dietary ionophores. Two hours after feeding, the accumulation with monensin appeared to be of peptides of a wide Mr range, while tetronasin caused an accumulation mainly of smaller, <570 Da, peptides. Treatment of Trypticase with acetic anhydride afforded 76% protection of its peptides from degradation to ammonia in a 6-h incubation. When Trypticase was fractionated by gel filtration then acetylated, none of the fractions was protected significantly better than others.

U2 - 10.1002/jsfa.2740580204

DO - 10.1002/jsfa.2740580204

M3 - Article

VL - 58

SP - 177

EP - 184

JO - Journal of the Science of Food and Agriculture

JF - Journal of the Science of Food and Agriculture

SN - 0022-5142

IS - 2

ER -