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Assessment of the biological activity of fish muscle protein hydrolysates using in vitro model systems

期刊

FOOD CHEMISTRY
卷 359, 期 -, 页码 -

出版社

ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2021.129852

关键词

Fish protein hydrolysates; Enzymatic hydrolysis; In vitro; Bioactivity

资金

  1. Department of Agriculture, Food and the Marine (FIRM project) [17 F 260]
  2. Science Foundation Ireland (SFI)
  3. Department of Agriculture, Food and Marine on behalf of the Government of Ireland [16/RC/3835 VistaMilk]

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The paper reviews the production of protein hydrolysates from fish muscle, primarily through enzymatic hydrolysis, and their potential bioactivities including anti-obesity, immunomodulatory, antioxidant, ACE-inhibitory, antimicrobial, and anti-cancer properties. Small molecular weight FPHs demonstrate higher bioactivity due to increased absorption through the gastrointestinal tract. The relationship between amino acid composition and sequence of FPH and peptides and their in vitro bioactivity is also discussed.
The generation of biologically active fish protein hydrolysates (FPH) is a useful technique to produce valueadded products with potential application in the functional food and nutraceutical industries. Fish muscle is an attractive substrate for the production of protein hydrolysates due to its rich protein content, containing 15-25% of total fish protein. This paper reviews the production of protein hydrolysates from fish muscle, most commonly via enzymatic hydrolysis, and their subsequent bioactivities including anti-obesity, immunomodulatory, antioxidant, angiotensin I-converting enzyme (ACE)-inhibitory, anti-microbial, and anti-cancer activities as measured by in vitro testing methods. Disease prevention with FPH potentially offers a safe and natural alternative to synthetic drugs. Small molecular weight (MW) FPHs generally exhibit favourable bioactivity than large MW fractions via enhanced absorption through the gastrointestinal tract. This review also discusses the relationship between amino acid (AA) composition and AA sequence of FPH and peptides and their exhibited in vitro bioactivity.

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