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

김형준|강경태|김진수|박재원|박찬호
한국수산과학회 (The Korean Society of Fisheries and Aquatic Science)|2009.06|Fisheries and Aquatic Sciences|제12권 제2호|pp. 79-85

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참고문헌

키워드

Alaska pollockRefiner dischargeFish gelatinFish gelatin hydrolysateAlaska pollock by-products
주제분류수산학

초록

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 IC50 (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) was observed with the 3-kDa filtrate.

Abstract

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 IC50 (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) was observed with the 3-kDa filtrate.

참고문헌 (21)

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