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Fig. 2 The hydrolyzed protein concentrations in control (a) and CFU pretreatment enzymolysis (b) at different substrate concentrations during enzymolysis time of 75 min

Figure 2 The hydrolyzed protein concentrations in control (a) and CFU pretreatment enzymolysis (b) at different substrate concentrations during enzymolysis time of 75 min

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Fig. 1 Schematic diagram of CFU pretreatment
Fig. 1 Schematic diagram of CFU pretreatment
Note: Different letters in the same column indicate significant differences at P<0.05. Hydrolysates were diluted 15x prior to determination of ACE inhibitory activity. (CFU condition: temperature 30+2 °C, pulsed on-time 4 s and off- time 3 s, pretreatment time 20 min and circulation pump speed of 200 rpm, ultrasound concentration 50 g/L.) The enzymolysis processes of wheat gluten protein in control and CFU pretreatment enzymolysis at different substrate con- centrations during an enzymolysis time of 75 min were showed in Fig. 2. It could be seen that the hydrolyzed protein concentrations in both control and ultrasound hydrolysis in- creased with increasing hydrolysis time. It could also be ob- served that the rate of increase was quite slow for the lower substrate concentrations (10, 20 g/L). However, for high sub- strate concentrations (30—50 g/L), the hydrolyzed protein con- centrations continued to increase quite linearly throughout the 75 min of hydrolysis. Increasing hydrolyzed protein concen- trations with increasing substrate concentration is in conso- nance with the report by Qu et al. [6] which showed that hydrolyzed protein concentrations of wheat germ increased as the substrate concentration increased from 1.5 to 24.0 g/ L. The hydrolysis process of WG at different substrate con- centrations was also in agreement with the results from the study of cheese [19]. The result implied that CFU pretreatment could increase the hydrolyzed protein concentrations at high substrate concentrations of WG compared to control, and mainly represented at the beginning of the enzymolysis period.
Note: Different letters in the same column indicate significant differences at P<0.05. Hydrolysates were diluted 15x prior to determination of ACE inhibitory activity. (CFU condition: temperature 30+2 °C, pulsed on-time 4 s and off- time 3 s, pretreatment time 20 min and circulation pump speed of 200 rpm, ultrasound concentration 50 g/L.) The enzymolysis processes of wheat gluten protein in control and CFU pretreatment enzymolysis at different substrate con- centrations during an enzymolysis time of 75 min were showed in Fig. 2. It could be seen that the hydrolyzed protein concentrations in both control and ultrasound hydrolysis in- creased with increasing hydrolysis time. It could also be ob- served that the rate of increase was quite slow for the lower substrate concentrations (10, 20 g/L). However, for high sub- strate concentrations (30—50 g/L), the hydrolyzed protein con- centrations continued to increase quite linearly throughout the 75 min of hydrolysis. Increasing hydrolyzed protein concen- trations with increasing substrate concentration is in conso- nance with the report by Qu et al. [6] which showed that hydrolyzed protein concentrations of wheat germ increased as the substrate concentration increased from 1.5 to 24.0 g/ L. The hydrolysis process of WG at different substrate con- centrations was also in agreement with the results from the study of cheese [19]. The result implied that CFU pretreatment could increase the hydrolyzed protein concentrations at high substrate concentrations of WG compared to control, and mainly represented at the beginning of the enzymolysis period.
Table 2 Effects of CFU-pretreatment on the initial reaction for different concentrations for the enzymatic hydrolysis of WG Note: Different letters in the same column indicate significant differences at P<0.05
Table 2 Effects of CFU-pretreatment on the initial reaction for different concentrations for the enzymatic hydrolysis of WG Note: Different letters in the same column indicate significant differences at P<0.05
Fig. 3 Effects of CFU pretreatment on kinetic parameters for the enzymatic hydrolysis of WG
Fig. 3 Effects of CFU pretreatment on kinetic parameters for the enzymatic hydrolysis of WG
Table 4 Particle analysis of samples Note: Different letters in the same column indicate significant differences at P<0.05 As shown in Fig. 5, surface morphology of CFU pre- treatment WG had less folded than control (without CFU pretreatment). It showed that compared with control, di- ameters of protein particles was significantly enlarged (Table 4). The roughness R, and R, were increased after CFU pretreatment. It was revealed that the CFU pretreat- ment caused the reunion of protein molecules and a dra- matic change of surface roughness. CFU pretreatment
Table 4 Particle analysis of samples Note: Different letters in the same column indicate significant differences at P<0.05 As shown in Fig. 5, surface morphology of CFU pre- treatment WG had less folded than control (without CFU pretreatment). It showed that compared with control, di- ameters of protein particles was significantly enlarged (Table 4). The roughness R, and R, were increased after CFU pretreatment. It was revealed that the CFU pretreat- ment caused the reunion of protein molecules and a dra- matic change of surface roughness. CFU pretreatment
biomechanical properties of CFU pretreated (Fig. 6b and d). Figure 6f showed that, the adhesion values of CFU pretreatment samples distributed at 0.2-86.6 pN. It was showed a wider dispersion than the control. Compared with the control, the Young’s modulus was lower and distributed at 0.0-5.1 MPa. Additionally some very low Young’s modulus regions were also appeared and its values focus on 0.9-1.8 Kpa. The changes revealed that ultrasound damaged the homoge- neous reticular structure and changed the biomechani- cal map. Fourier transform infrared (FTIR) analysis was conducted to further investigate the difference between secondary structure of WG with and without CFU pretreatment. It was observed that the contents of the secondary structure elements by ana- yzing the Amide I band of WG which had been resolved by deconvolution and secondary derivation and Gaussian curve fitting. The different Amide I regions were assigned to protein secondary structures according to previous reports, B-sheet, which contained intermolecular B-sheet of protein aggrega- tion (1605-1615 cm‘), intra-molecular B-sheet (1615— 1640 cm‘), anti-parallel 8-sheet (1690-1700 cm '), random coil (1640-1650 cm '), «x-helix (1650-1660 cm‘'), B-turn (1675-1690 cm ') [30-32]. A category-based analysis of the peak shape of infrared spectrum was conducted as Table 5. According to the previous research of adhesion by AFM, the adhesion of biopolymers surfaces was related to the hydrophilic properties [29]. Since the informa- tion about adhesion was obtained just when the tip lifts the sample on mica and returns to its initial position. Mica was a kind of hydrophilic mineral, so we specu- lated that the high adhesion divisions possessed a high hydrophilic property in this paper, while the low adhe- sion division represented a high hydrophobic property. The low adhesion divisions in Fig. 6b mean the hydro- phobic regions of the WG were enriched together dur- ing CFU pretreatment. The enrichment and exposure of hydrophobic regions of the protein were beneficial to the increase of ACE inhibition activity [6, 7]. With respect to the changes of Young’s modulus map in Fig. 6d, the lower Young’s modulus of CFU pretreat- ment samples represent the surface of protein was more soft and easy to disintegrate than control. These chang- es led to the active components and amide bonds of WG to cleave easily by alcalase.
biomechanical properties of CFU pretreated (Fig. 6b and d). Figure 6f showed that, the adhesion values of CFU pretreatment samples distributed at 0.2-86.6 pN. It was showed a wider dispersion than the control. Compared with the control, the Young’s modulus was lower and distributed at 0.0-5.1 MPa. Additionally some very low Young’s modulus regions were also appeared and its values focus on 0.9-1.8 Kpa. The changes revealed that ultrasound damaged the homoge- neous reticular structure and changed the biomechani- cal map. Fourier transform infrared (FTIR) analysis was conducted to further investigate the difference between secondary structure of WG with and without CFU pretreatment. It was observed that the contents of the secondary structure elements by ana- yzing the Amide I band of WG which had been resolved by deconvolution and secondary derivation and Gaussian curve fitting. The different Amide I regions were assigned to protein secondary structures according to previous reports, B-sheet, which contained intermolecular B-sheet of protein aggrega- tion (1605-1615 cm‘), intra-molecular B-sheet (1615— 1640 cm‘), anti-parallel 8-sheet (1690-1700 cm '), random coil (1640-1650 cm '), «x-helix (1650-1660 cm‘'), B-turn (1675-1690 cm ') [30-32]. A category-based analysis of the peak shape of infrared spectrum was conducted as Table 5. According to the previous research of adhesion by AFM, the adhesion of biopolymers surfaces was related to the hydrophilic properties [29]. Since the informa- tion about adhesion was obtained just when the tip lifts the sample on mica and returns to its initial position. Mica was a kind of hydrophilic mineral, so we specu- lated that the high adhesion divisions possessed a high hydrophilic property in this paper, while the low adhe- sion division represented a high hydrophobic property. The low adhesion divisions in Fig. 6b mean the hydro- phobic regions of the WG were enriched together dur- ing CFU pretreatment. The enrichment and exposure of hydrophobic regions of the protein were beneficial to the increase of ACE inhibition activity [6, 7]. With respect to the changes of Young’s modulus map in Fig. 6d, the lower Young’s modulus of CFU pretreat- ment samples represent the surface of protein was more soft and easy to disintegrate than control. These chang- es led to the active components and amide bonds of WG to cleave easily by alcalase.
Note: “ Estimated as (secondary structure area/total amide I band area) x 100 %. Different letters in the same column indicate significant differences at P<0.05 Table 5 Secondary structure contents of control and CFU pretreatments
Note: “ Estimated as (secondary structure area/total amide I band area) x 100 %. Different letters in the same column indicate significant differences at P<0.05 Table 5 Secondary structure contents of control and CFU pretreatments
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Mechanical Pretreatment
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