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

Chan Ho Park | Zendy; Hyung Jun Kim | Zendy; Kyung-Tae Kang | Zendy; Jae-W. Park | Zendy; JinSoo Kim | Zendy

Open Access

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

Author(s) -

Chan Ho Park,

Hyung Jun Kim,

Kyung-Tae Kang,

Jae-W. Park,

JinSoo Kim

Publication year - 2009

Publication title -

fisheries and aquatic sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.39

H-Index - 15

eISSN - 2234-1757

pISSN - 2234-1749

DOI - 10.5657/fas.2009.12.2.079

Subject(s) - gelatin , fractionation , hydrolysate , pronase , chemistry , angiotensin converting enzyme , enzyme , inhibitory postsynaptic potential , chromatography , enzyme assay , food science , biochemistry , biology , endocrinology , trypsin , hydrolysis , blood pressure

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 (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.

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