An approach to improve ACE-inhibitory activity of casein hydrolysates with plastein reaction catalyzed by Alcalase |
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Authors: | Xin-Huai Zhao Ya-Yun Li |
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Affiliation: | (1) Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, 150030 Harbin, People’s Republic of China |
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Abstract: | The preparation method of casein hydrolysates with high ACE-inhibitory activity was studied by Alcalase-catalyzed hydrolysis
coupled with plastein reaction. Casein hydrolysates with an IC50 value of about 47 μg mL−1 were first prepared by hydrolysis of casein with Alcalase and then modified with plastein reaction catalyzed by the same
enzyme. The impacts of four reaction conditions on plastein reaction of casein hydrolysates were studied, and then optimal
conditions were determined using response surface methodology with the decrease of free amino groups in the reaction mixture
as response. When the concentration of casein hydrolysates was fixed at 35% by weight, the maximum decrease of free amino
groups in the reaction mixture of 181.8 μmol g−1 proteins was obtained. The optimum conditions for the above decrease were found to be an E/S ratio of 7.7 kU g−1 proteins, reaction temperature of 42.7 °C and reaction time of 6 h. Analysis results showed that ACE-inhibitory activity
of casein hydrolysates prepared could be improved significantly by plastein reaction. When casein hydrolysates were modified
by plastein reaction, with a decrease of free amino groups in the mixture of about 154.7 μmol g−1 proteins and 181.8 μmol g−1 proteins, their IC50 values could be decreased to 0.6 and 0.5 μg mL−1. |
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Keywords: | Casein Hydrolysis ACE-inhibitory activity Plastein reaction Alcalase |
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