Native soy protein isolate (SPI) was hydrolyzed with 4 different proteolytic enzymes, including bromelain, papain, Neutrase, and Flavourzyme. SPI hydrolysates with the degree of hydrolysis (DH) in range of 6 to 15% were prepared by each enzyme. The angiotensin 1 converting enzyme (ACE) inhibitory an...
Native soy protein isolate (SPI) was hydrolyzed with 4 different proteolytic enzymes, including bromelain, papain, Neutrase, and Flavourzyme. SPI hydrolysates with the degree of hydrolysis (DH) in range of 6 to 15% were prepared by each enzyme. The angiotensin 1 converting enzyme (ACE) inhibitory and the antioxidant activities of the SPI hydrolysates, such as superoxide dismutase-like activity and inhibition of the linoleic acid autoxidation, were evaluated. Overall, as the DH increased, all evaluated bioactivities of the SPI hydrolysates significantly increased. The significantly highest ACE inhibitory and antioxidant activities were found in hydrolysates made with papain and bromelain, respectively. SPI hydrolysates by Flavourzyme showed the significantly lowest activity in all tested bioactivities. The results suggested that ACE inhibitory and antioxidant activities of SPI hydrolysates were determined by the DH and by the enzyme used.
Native soy protein isolate (SPI) was hydrolyzed with 4 different proteolytic enzymes, including bromelain, papain, Neutrase, and Flavourzyme. SPI hydrolysates with the degree of hydrolysis (DH) in range of 6 to 15% were prepared by each enzyme. The angiotensin 1 converting enzyme (ACE) inhibitory and the antioxidant activities of the SPI hydrolysates, such as superoxide dismutase-like activity and inhibition of the linoleic acid autoxidation, were evaluated. Overall, as the DH increased, all evaluated bioactivities of the SPI hydrolysates significantly increased. The significantly highest ACE inhibitory and antioxidant activities were found in hydrolysates made with papain and bromelain, respectively. SPI hydrolysates by Flavourzyme showed the significantly lowest activity in all tested bioactivities. The results suggested that ACE inhibitory and antioxidant activities of SPI hydrolysates were determined by the DH and by the enzyme used.
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제안 방법
Therefore, in this study, soy protein isolate (SPI) was hydrolyzed with different proteolytic enzymes, including bromelain, papain, Neutrase, and Flavourzyme. SPI hydrolysates with the DH in range of 6 to 15% were prepared by each enzyme and the effects of the enzyme used and DH on the angiotensin I converting enzyme (ACE) inhibitory and antioxidant activities were evaluated.
This result could be due to the difference of the antioxidant properties measured to determine SOD-like activity and inhibition of linoleic acid autoxidation. To determine the overall antioxidant action, it was necessary to examine several methods, including the lipid peroxidation inhibitory, the reducing activity, the radical scavenging activity, and the peroxynitrite scavenging activity (2, 7). These several methods seem to be necessary in understanding how the properties have their antioxidant activity.
대상 데이터
1, from Aspergillus oryzae), were purchased from Novo Nordisk (Bagsvaerd, Denmark). Papain (EC 3.4.22.2) and bromelain (EC 3.4.22.32) were purchased from Sigma- Aldrich. All the other reagents were 야f analytical grade.
Louis, MO, USA). Two plant-derived and 2 microbi이ogical proteolytic enzymes were used to hydrolyze SPL Neutrase (EC 3.4.24.28, from Bacillus amyloliquefaciens^ 1.5 AU/g); Flavo니rzyme (EC 3.4.11.1, from Aspergillus oryzae), were purchased from Novo Nordisk (Bagsvaerd, Denmark). Papain (EC 3.
데이터처리
, Chicago, IL, USA). One-way analysis of variance (ANOVA) was used and mean comparison was performed by Duncan's m니tiple range test (/?<0.05).
이론/모형
ACE inhibitory activity was measured by the method of Cushman and Cheung (28) with modification. The reaction mixture contained 50 of 20 mM HHL as a substrate, 50 giL of ACE powder (20 munit) in a 150 mM sodium borate buffer (pH 8.
The mixed solution was incubated at 40℃ in a dark room for 5 days and the degree of oxidation was evaluated by measuring the thiobarbituric acid (TBA) value. The TBA value was measured using a modified version of the method of Ohkawa et al. (31). The inhibition of lipid peroxidation in percentage was calculated by following equation:
성능/효과
In conclusion, our findings suggest that in the ACE inhibitory and the antioxidant activities, such as SOD-like activity and inhibition of the lin이eie acid autoxidation, there were significant effects of enzyme used and DH. Overall, as the DH increased, all evaluated bioactivities of the SPI hydrolysates increased.
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