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

Article


Hancock Kerrie R., Ealing, Paul M. and White, Derek W.R.. 1994. "Identification of sulphur-rich proteins which resist rumen degradation and are hydrolysed rapidly by intestinal proteases." The British Journal of Nutrition: an international journal of nutritional science. 72 (6), pp. 855-863. https://doi.org/10.1079/BJN19940090
Article Title

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

ERA Journal ID13453
Article CategoryArticle
AuthorsHancock Kerrie R., Ealing, Paul M. and White, Derek W.R.
Journal TitleThe British Journal of Nutrition: an international journal of nutritional science
Journal Citation72 (6), pp. 855-863
Number of Pages9
Year1994
PublisherCambridge University Press
Place of PublicationUnited Kingdom
ISSN0007-1145
1475-2662
Digital Object Identifier (DOI)https://doi.org/10.1079/BJN19940090
Web Address (URL)https://www.cambridge.org/core/journals/british-journal-of-nutrition/article/idendification-of-sulphurrich-proteins-which-resist-rumen-degradation-and-are-hydrolysed-rapidly-by-intestinal-proteases/396B03F161FAB2D2880643B49275A292
Abstract

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 (EC3.4.21.1). 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.

KeywordsRumen proteolysis; Ruminant nutrition; Sulphur-rich proteins
ANZSRC Field of Research 2020300103. Agricultural molecular engineering of nucleic acids and proteins
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PubMed ID7827006
Byline AffiliationsNew Zealand Pastoral Agriculture Research Institute, New Zealand
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