Fractionation and Angiotensin I-converting Enzyme (ACE) Inhibitory Activity of Gelatin Hydrolysates from by-products of Alaska Pollock Surimi

摘要

Gelatin hydrolysates with a high inhibitory activity against angiotensin I-converting enzyme (ACE) were fractionated from Alaska pollock surimi refiner discharge. The ACE-inhibitory activity, expressed as IC_(50) (mg/mL), was highest (0.49 mg/mL) in gelatin hydrolysates formed by sequential 2-hr treatments of Pronase and Flavourzyme. After fractionation through four different membrane filters with molecular weight cut-offs of 3, 5, 10, and 30 kDa, the highest ACE-inhibitory activity (0.21 mg/mL) wasobserved with the 3-kDa filtrate.