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- W1976031053 abstract "The effects of different hydrolysis conditions on the angiotensin-I converting enzyme (ACE) inhibitory properties of giant red sea cucumber (Parastichopus californicus) collagen hydrolysates were investigated. Optimal conditions predicted by central composite rotatable design (CCDR) modeling for producing ACE inhibitory peptides were found to be 54.9°C, 1.76 h and an enzyme to substrate (E/S) ratio of 0.064. Compared with experiments performed under these optimal conditions, the predicted degree of hydrolysis (DH) and ACE inhibitory activities had error rates of 3 to 6%. Under optimum conditions, the molecular weights of collagen hydrolysates were less than 6.5 kDa. Lineweaver-Burk plots suggest that the collagen hydrolysates acted as competitive inhibitors with an inhibition constant (Ki) value of 0.706 mg/mL." @default.
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- W1976031053 date "2011-04-18" @default.
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- W1976031053 title "Optimization of Hydrolysis Conditions for the Production of the Angiotensin-I Converting Enzyme Inhibitory Peptides from Sea Cucumber Collagen Hydrolysates" @default.
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- W1976031053 doi "https://doi.org/10.1080/10498850.2011.560364" @default.
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