Polyacrylamide gel electrophoresis (in the presence of urea) and gel permeation chromatography were employed to assess the profile of hydrolysis of caseins and the activity of enzymes contributed by the flowers of the plant Cynara cardunculus on bovine caseins, after previous precipitation with ammonium sulfate or in a plain crude aqueous extract. Results indicated that the qualitative degradation profile of bovine caseins by plant enzymes (cardosins) remains essentially unchanged upon extraction, and quantitative analysis showed that the precipitated fractions had a higher coagulant-to-proteolytic activity ratio; hence, the results showed that inexpensive precipitation with ammonium sulfate can successfully be used as a purification method in the production of that plant coagulant in standardized form.
|Number of pages||6|
|Journal||Journal of Food Science|
|Publication status||Published - 2002|
- Milk proteins