In this research enzymatic hydrolysis of grain bran proteins concentrate (RBPC) and soybean Proteins (SBP) as control were studied with 3 commercial enzymes (Alcalase? Papain and acommercial 3-enzyme cocktail formulated with of just one 1. of Alcalase? for SBP and RBPC was 12.69 and 12.50?% respectively. On the other hand papain enzyme was demonstrated most affordable DH% in three substrates that 1.56 and 1.24?% for SBP and RBPC had been respectively.The hydrolysis from the protein fraction performed the three enzymes on both substrates was followed in NBR13 SDS-PAGE. SBP and RBPC showed nearly complete digestion with Alcalase? enzyme after 60?mins. 3-enzyme cocktail enzyme hydrolyzed better the RBPC compared to Cerovive the SBP. Papain enzyme got less influence on both substrates than various other 2 enzymes. It had been discovered that Alcalase? provides highest capacity for hydrolysis in comparison to various other enzyme arrangements. The quality value proteins hydrolysates made by Alcalase? could be utilized as worth added ingredients in lots of food formulations. Cerovive Also they are suitable for a wide range of commercial food applications and in addition for aesthetic and personal maintenance systems. deionized drinking water. The pH of homogenate was altered to pH?12 and pH?10 with 2?N NaOH and was incubated at area temperatures centrifuged 30?min in 2300?g within a Beckman centrifuge (Model JS.5 Beckman USA). The supernatant was altered to pH?4.5 and centrifuged 20 again?min in 2300?g the supernatant was discarded as well as the precipitate was freeze-dried and known as protein focus (Kumagai et al. 2006). Defatted soybean proteins (Sigma) with 52?% protein was used as control. Protease selection Commercial enzymes used in this work were Alcalase? (produced from a strain of glycerol 0.2 DTT and 0.02%bromophenol blue at pH?6.8 heated 5?min in a boiling water bath. Samples were analyzed in a vertical electrophoresis unit (SE 260 Hoefer San Francisco CA) using a 1.5?mm polyacrylamide gel slab (17?%) for separating protein bands. Electrophoresis was conducted at a constant current (30?mA per gel). The separated protein bands were stained with a solution made up of 7?% acetic acid 0.5 Coomassie Brilliant Blue R-250 and 40?% methanol. The excess stain was removed with a solution made up of 40?% methanol and 7?% acetic acid and Cerovive then the gel recorded with an electronic scanner (Umax Power Look 2100 UMAX Technologies Fremont CA). Results The results of proximate composition of defatted rice-bran and rice bran protein concentrate are showed in Table ?Table11. Table 1 Proximate compositions of defatted rice bran and rice bran protein concentrate The results of the hydrolysis experiments are given in Table ?Table22 and Fig. ?Fig.1.1. There was significant differences between treatments (P?0.05).The highest and lowest DH% for RBPC was 12.69 and 1.21 for Alcalase? and papain respectively. Based on fig1 that it shows the DH% of 2 substrate with 3 commercial enzymes in over time both substrates showed an increasing trend over time and the maximum was at 60?min. Table 2 Effect of different enzymes on degree hydrolysis of RBPC and SBP substrate at 60?min Fig. 1 Degree of hydrolysis over time of 2 substrate with 3 commercial enzymes a rice bran protein concentrate b defatted soybean protein In Figs ?Figs22 and ?and3 3 the digestion of the protein fraction of the two Cerovive substrates by the 3 commercial enzymes was observed over time in SDS-PAGE. Both RBPC and SBP showed almost complete hydrolysis after 60?min when Alcalase? was used. The Fig. ?Fig.33 shows that the RBPC product had 11 component of protein and the molecular size of them were between 69.47 and 15.08?kDa. Fig. 2 SDS-PAGE showing hydrolysis over 60?min of Soybean protein with 3 commercial enzymes sampled at different times a?=?Soybean hydrolyzed with Alcalase b?=?Soybean hydrolyzed with 3-enzymes cocktail c?=?Soybean … Fig. 3 SDS-PAGE showing hydrolysis over 60?min of rice bran protein with 3 commercial enzymes sampled at different times a?=?rice bran protein hydrolyzed with Alcalase? b?=?rice bran protein hydrolyzed with 3-enzymes … Discussion In our research Alcalase?had stronger capability for hydrolysis compared to other enzyme. Silpradit et al. (2010) obtained the 14.5 DH% for rice bran protein hydrolysates with optimum condition (60C Enzyme/Substrate at Cerovive 1?% 340 incubation time) (Silpradit et al. 2010). At the end of 60?min of processing time Alcalase?hydrolyzed more than others.