:The aim of this study was to produce enzymatic hydrolysis of α-LA, β-LG and BSA with alcalase for the possible application of hypoallergenic foods toward cow's milk allergenic infant. The molecular weights of most of the peptides in hydrolysates from α-LA, β-LG and BSA by alcalase were below 3,000 dalton. Antigenesity of α-LA, β-LG and BSA hydrolysates to rabbit anti-α-LA antiserum, β-LG antiserum and BSA antiserum were remarkably decreased by more than 10 -3 at 20% inhibitionrate. Antigenesity of polyvalent antigenic peptide in α-LA, β-LG and BSA hydrolysates to specific rabbit anti-α-LA antiserum, β-LG antiserum and BSA antiserum was determined by PCS test using guina-pig.Hydrolysates of α-LA, β-LG and BSA with less than 3,000 dalton did not show polyvalent antigenic reaction against rabbit antiserum. Hydrolysates of α-LA, β-LG and BSA could be a source for the manufacturing of hypoallergenic food.
: Degrees of hydrolysis by alkaline protease produced from Serratia marcescens S3-R1 is 3.95-6.30% of whey proteins during 5, 15, 30, 60, 90, 120,180, 240 min incubation at 40 °C. Proteolytic pattern of the whey proteins showed that various low molecular weight peptides were generated during the incubation periods. The biological function of in Raw 264.7 cells treated with whey protein hydrolytic peptides, anti-inflammatory effect showed exhibit in the expression of pro-inflammatory cytokines such as TNF-α, IL-6, COX-2 and iNOS by PCR analysis. COX-2 and iNOS gene expression inhibited in Raw 264.7 cells on whey protein hydrolysates below 3,000 dalton. The protease from Serratia marcescens S3-R1 showed a potential in production of low molecular weight whey protein hydrolysates which could be used for industrial application.
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