Selective denaturation of milk coagulants in 5 M-urea
- 1 June 1977
- journal article
- research article
- Published by Cambridge University Press (CUP) in Journal of Dairy Research
- Vol. 44 (2) , 319-324
- https://doi.org/10.1017/s0022029900020240
Abstract
Summary: Porcine and bovine pepsins were very stable in 5·0 M-urea at pH 2·0 or 2·5 at 30 °C while chymosin and Mucor miehei and M. pusillus proteases were rapidly denatured under these conditions. These differences may provide the basis of a quantitative assay of the complement of individual milk clotting enzymes in a coagulant and a possible scheme is suggested.This publication has 6 references indexed in Scilit:
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- Determination of Rennin and Bovine Pepsins in Commercial Rennets and Abomasal JuicesJournal of Dairy Science, 1972
- Inactivation par l'urée de la présure et des pepsines bovines. Application possible à leur dosage en mélangeBiochimie, 1971
- Effects of some protein modifying agents on the properties of renninJournal of Dairy Research, 1969
- Denaturation of Rennin ; Effect on Activity and Molecular ConfigurationNature, 1965