Fractionation and angiotensin I-converting enzyme (ACE) inhibitory activity of gelatin hydrolysates from by-products of Alaska pollock surimi

Chan Ho Park; Hyung Jun Kim; Kyung Tae Kang; Jae W. Park; Jin Soo Kim

doi:10.5657/fas.2009.12.2.079

Fractionation and angiotensin I-converting enzyme (ACE) inhibitory activity of gelatin hydrolysates from by-products of Alaska pollock surimi

Chan Ho Park, Hyung Jun Kim, Kyung Tae Kang, Jae W. Park, Jin Soo Kim

Department of Food Technology

Research output: Contribution to journal › Article › peer-review

11 Citations (Scopus)

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.

Original language	English
Pages (from-to)	79-85
Number of pages	7
Journal	Fisheries and Aquatic Sciences
Volume	12
Issue number	2
DOIs	https://doi.org/10.5657/fas.2009.12.2.079
Publication status	Published - 2009 Jun

Keywords

Alaska pollock
Alaska pollock by-products
Fish gelatin
Fish gelatin hydrolysate
Refiner discharge

ASJC Scopus subject areas

Oceanography
Biochemistry
Aquatic Science
Molecular Biology

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10.5657/fas.2009.12.2.079

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title = "Fractionation and angiotensin I-converting enzyme (ACE) inhibitory activity of gelatin hydrolysates from by-products of Alaska pollock surimi",

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.",

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AU - Park, Jae W.

AU - Kim, Jin Soo

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AB - 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.

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Fractionation and angiotensin I-converting enzyme (ACE) inhibitory activity of gelatin hydrolysates from by-products of Alaska pollock surimi

Abstract

Keywords

ASJC Scopus subject areas

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