Hydrolysis of 7S and 11S soy proteins by commercial proteases
1988
Kang, Y.J. (Cheju National Univ., Cheju (Korea R.). Dept. of Food Science) | Rhee, K.C. (Texas A and M Univ., Texas (USA). Food Protein R and D Center) | Park, Y.H. (National Fisheries Univ., of Pusan, Pusan (Korea R.). Dept. of Food Science and Technology)
Selected kinetic parameters and degree of hydrolysis(DH) were measured using commercial proteases(trypsin, alcalase and pronase) to study the affinity of these enzymes to 7S and 11S soy proteins. Electrophoretic patterns of the hydrolysates were also investigated. In general, the order of affinity between the proteins and the proteases was 11S PRF(protein-rich fraction) and 7S PRF for unheated proteins, and 7S PRF and 11S PRF for preheated proteins. Substrate inhibition was present at a substrate concentration of l.5% or higher when preheated protein was used as the substrate. The maximum DH values of alcalase were obtained from 7S PRF (60%) and 11S PRF(80%) at 1 hr hydrolysis, respectively. Trypsin hydrolysis did not affect 11S soy protein but the acidic subunits in contrast to alcalase and pronase hydrolyses which changed almost all subunits. Alcalase hydrolysis induced distinct changes on 2S soy protein
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