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Electrophoretograms of peas and skim milk proteins hydrolyzed in vitro with pepsin ec 3.4.23.1 and rennin ec 3.4.23.4


, : Electrophoretograms of peas and skim milk proteins hydrolyzed in vitro with pepsin ec 3.4.23.1 and rennin ec 3.4.23.4. Journal of Agricultural and Food Chemistry 31(2): 297-300

Three protein products, pea protein isolate [PPI], pea protein concentrate [PPC] and reconstituted skim milk [SM], were hydrolyzed in vitro with commercial pepsin and renin for 0.25-22 h. The peptide bond hydrolysis was determined by reaction with 2,4,6-trinitrobenzenesulfonic acid. The order of hydrolysis of the 3 proteins by pepsin was PPI > PPC > SM and by rennin was SM > PPI > PPC. In general, the pea protein isolate and pea protein concentrate proteins appeared to be more susceptible to pepsin and skim milk proteins, as expected, appeared to be more susceptible to rennin. The sodium dodecyl sulfate-polyacrylamide gel electrophoretic patterns of PPI and PPC showed that proteins having a MW between 70,000-300,000 were preferentially hydrolyzed, although several protein bands were still present after 22 h of hydrolysis, suggesting the presence of resistant proteins or peptides. The preferentially hydrolyzed proteins were probably acidic proteins or subunits and their relative ease of hydrolysis may be related to their chemical composition and/or structure.

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Bhatty, R.S.; Patel, P.R., 1983: Electrophoretograms of peas and skim milk proteins hydrolyzed in vitro with pepsin and rennin. 3 protein products, pea protein isolate (PPI), pea protein concentrate (PPC) and reconstituted skim milk (SM), were hydrolysed in vitro with commercial pepsin and chymosin for 0.25-22 h. The peptide bond hydrolysis was determined by reaction with...

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