A comparative study on digestible characteristics of denatured proteins by molecular sieve HPLC
Lee, J.Y.; Park, J.L.
Korean Journal of Dairy Science 12(3): 267-276
In order to compare the digestible characteristics of native and denatured proteins, ß-lactoglobulin, alpha-lactalbumin and bovine serum albumin were denatured by heat treatment, heat treatment in fructose and alkali treatment, individually. The native and the denatured proteins were hydrolysed by the sole immobilized pepsin, and digested by the immobilized trypsin, chymotrypsin and pronase successively and then the peptides produced by digestion were separated by molecular sieve HPLC. The results obtained were summarized as follows: 1. In molecular sieve HPLC diagrams, the native ß-lactoglobulin, alpha-lactalbumin and bovine serum albumin were appeared a single peak, but their retention times were different individually. 2. Denaturations of ß-lactoglobulin, alpha-lactalbumin and bovine serum albumin by heat treatment, by heat and fructose treatment, and by alkali treatment, changed the elution time and the number of their eluted protein peak individually. 3. Digestion of native and denatured proteins on immobilized enzyme system prolonged the elution time, and increased the number of eluted peptide groups produced by hydrolysis of them. But according to the types of treatment and the kinds of protein, changes of the number of peak and of the degree of released time were appeared individually various different tendencies.