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 ID | 13453 |
| Article Category | Article |
| Authors | Hancock Kerrie R., Ealing, Paul M. and White, Derek W.R. |
| Journal Title | The British Journal of Nutrition: an international journal of nutritional science |
| Journal Citation | 72 (6), pp. 855-863 |
| Number of Pages | 9 |
| Year | 1994 |
| Publisher | Cambridge University Press |
| Place of Publication | United Kingdom |
| ISSN | 0007-1145 |
| 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. |
| Keywords | Rumen proteolysis; Ruminant nutrition; Sulphur-rich proteins |
| ANZSRC Field of Research 2020 | 300103. Agricultural molecular engineering of nucleic acids and proteins |
| Public Notes | Files associated with this item cannot be displayed due to copyright restrictions. |
| PubMed ID | 7827006 |
| Byline Affiliations | New Zealand Pastoral Agriculture Research Institute, New Zealand |
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