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Idendification of sulphur-rich proteins which resist rumen degradation and are hydrolysed rapidly by intestinal proteases

Published online by Cambridge University Press:  09 March 2007

Kerrie R. Hancock
Affiliation:
Plant Molecular Genetics Laboratory, New Zealand Pastoral Agriculture Resarch Institute, Palmerston North, New Zealand
Paul M. Ealing
Affiliation:
Plant Molecular Genetics Laboratory, New Zealand Pastoral Agriculture Resarch Institute, Palmerston North, New Zealand
Derek W.R. White
Affiliation:
Plant Molecular Genetics Laboratory, New Zealand Pastoral Agriculture Resarch Institute, Palmerston North, New Zealand
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Abstract

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Several proteins with high proportions of S-containing essential amino acids were incubated in sheep rumen fluid in vitro and their rate of digestion was examined by sodium dodecyl sulphate-polyacrylamide-gel electrophoresis. The S-rich proteins rice prolamin (10 kDa), maize zein (10 kDa) and the 3·2 kDa pumpkin (Cucurbita maxima L.) trypsin inhibitor-1 (CMTI-1) were highly resistant to rumen fluid degradation, relative to control proteins of known degradation rate (casein, bovine serum albumin (BSA) and pea (Pisum sativum) albumin-1 (PA1)). Comparison of PA1 and a recombinant N-terminal epitope-tagged PA1 indicated that addition of the epitope caused a slight increase in resistance to rumen degradation. The proteins were also incubated with a mixture of trypsin (EC 3·4·21·4) and chymotrypsin (EC 3·4·21.1). PA1, BSA and casein were hydrolysed less rapidly than rice prolamin, maize zein and CMTI-1. Digestion by these intestinal proteases appeared to be complete. Thus, the prolamin, zein and CMTI-1 proteins are suitable candidates for expression as foreign proteins in pasture plants to increase throughput and uptake of essential amino acids in sheep.

Type
Suiphur-rich Proteins Which resist dagaration in the rumen
Copyright
Copyright © The Nutrition Society 1994

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