Partial purification and properties of proteases from defatted soybean flour.
- 1 January 1979
- journal article
- research article
- Published by Center for Academic Publications Japan in Journal of Nutritional Science and Vitaminology
- Vol. 25 (4) , 333-342
- https://doi.org/10.3177/jnsv.25.333
Abstract
Four chromatographically different proteases were partially purified from defatted soybean flour and their pH optima were around 5.0-5.6 using casein as the substrate. These soybean proteases were designated S1, S2, S3 and S4 according to their order of elution from a DEAE-cellulose column. Each gave a single peak of caseinolytic activity on a Sephadex G-200 column chromatogram and corresponded to MW of about 50,000(S1), 35,000(S2), 60,000(S3) and 200,000(S4). The proteases could hydrolyze casein and poly-Glu. .alpha.-Casein was more rapidly hydrolyzed than .beta.-casein, but the esters or dipeptide could not be hydrolyzed. Aliquots of 10-3 M Hg2+, Cu2+ and Zn2+ inhibited the caseinolytic activities by 70-90%, while other cations, Mn2+, Mg2+, Ca2+ and Ni2+, at the same concentration did not. Proteases S1, S2, S3 and S4 from defatted soybean flour can apparently be classified as acid proteases.This publication has 6 references indexed in Scilit:
- [14] PapainPublished by Elsevier ,1970
- Association of lysosomal activity with aleurone grains in plant seedsArchives of Biochemistry and Biophysics, 1968
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- Estimation of the molecular weights of proteins by Sephadex gel-filtrationBiochemical Journal, 1964
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- Separation of α- and β-CaseinJournal of the American Chemical Society, 1944