Food functionalities and bioactivities of protein isolates recovered from skipjack tuna roe by isoelectric solubilization and precipitation

Four roe protein isolates (RPIs) from skipjack tuna were prepared using isoelectric solubilization (pH 11 and 12) and precipitation (pH 4.5 and 5.5) (ISP) at different pH points to evaluate their physicochemical and functional properties and in vitro bioactivities. Moisture (

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Published in:Food science & nutrition 2020-04, Vol.8 (4), p.1874-1887
Main Authors: Cha, Jang Woo, Yoon, In Seong, Lee, Gyoon‐Woo, Kang, Sang In, Park, Sun Young, Kim, Jin‐Soo, Heu, Min Soo
Format: Article
Language:English
Subjects:
Amino acids
Angiotensin
Biological activity
Casein
Chemical precipitation
Fish
Food
food functionality
Glutamic acid
Hemoglobin
Katsuwonus pelamis
Leucine
Lipids
Original Research
pH effects
Phosphorus
physicochemical characterization
Potassium
Proteins
roe protein isolates
Scavenging
skipjack tuna
Sodium
Solubilization
Sulfur
Tuna
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description Four roe protein isolates (RPIs) from skipjack tuna were prepared using isoelectric solubilization (pH 11 and 12) and precipitation (pH 4.5 and 5.5) (ISP) at different pH points to evaluate their physicochemical and functional properties and in vitro bioactivities. Moisture (
doi_str_mv 10.1002/fsn3.1470
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Moisture (&lt;6.3%) and protein (71%–77%) content were maintained. Sulfur, sodium, phosphorus, and potassium were the major elements, and glutamic acid and leucine were the prevalent amino acids (12.2–12.8 and 9.6–9.8 g/100 g protein, respectively) in RPIs. RPI‐1 showed the highest buffering capacity at pH 7–12. RPIs and casein showed similar water‐holding capacities. At pH 12, RPI‐1(pH 11/4.5) showed the highest solubility, followed by RPI‐3(pH 12/4.5), RPI‐2(pH 11/5.5), and RPI‐4(pH 12/5.5) (p &lt; .05). Oil‐in‐water emulsifying activity indices of RPI‐1 and RPI‐3 significantly differed. At pH 2 and 7–12, pH‐shift treatment improved the food functionality of RPIs, which was superior to positive controls (casein and hemoglobin). RPI‐1 showed ABTS+ radical scavenging (102.7 μg/ml) and angiotensin‐converting enzyme inhibitory activities (44.0%). The physicochemical properties of skipjack tuna roe protein isolate (RPI) were determined, and the isolate was found to be useful as a protein source. These RPIs were superior to the positive controls in food functionalities and confirmed to be useful as raw materials in protein‐fortified foods. RPI also showed in vitro antioxidant and antihypertensive activities. Fish RPIs recovered using isoelectric solubilization, and precipitation can be used to supplement and enhance deficient nutrients in agricultural products. By partially replacing or adding RPI to traditional foods such as noodle, confectionery, and bakery‐ and surimi‐based products, agro‐seafood products with food functionality can be developed.</description><identifier>ISSN: 2048-7177</identifier><identifier>EISSN: 2048-7177</identifier><identifier>DOI: 10.1002/fsn3.1470</identifier><identifier>PMID: 32328253</identifier><language>eng</language><publisher>United States: John Wiley &amp; Sons, Inc</publisher><subject>Amino acids ; Angiotensin ; Biological activity ; Casein ; Chemical precipitation ; Fish ; Food ; food functionality ; Glutamic acid ; Hemoglobin ; Katsuwonus pelamis ; Leucine ; Lipids ; Original Research ; pH effects ; Phosphorus ; physicochemical characterization ; Potassium ; Proteins ; roe protein isolates ; Scavenging ; skipjack tuna ; Sodium ; Solubilization ; Sulfur ; Tuna</subject><ispartof>Food science &amp; nutrition, 2020-04, Vol.8 (4), p.1874-1887</ispartof><rights>2020 The Authors. published by Wiley Periodicals, Inc.</rights><rights>2020 The Authors. 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Moisture (&lt;6.3%) and protein (71%–77%) content were maintained. Sulfur, sodium, phosphorus, and potassium were the major elements, and glutamic acid and leucine were the prevalent amino acids (12.2–12.8 and 9.6–9.8 g/100 g protein, respectively) in RPIs. RPI‐1 showed the highest buffering capacity at pH 7–12. RPIs and casein showed similar water‐holding capacities. At pH 12, RPI‐1(pH 11/4.5) showed the highest solubility, followed by RPI‐3(pH 12/4.5), RPI‐2(pH 11/5.5), and RPI‐4(pH 12/5.5) (p &lt; .05). Oil‐in‐water emulsifying activity indices of RPI‐1 and RPI‐3 significantly differed. At pH 2 and 7–12, pH‐shift treatment improved the food functionality of RPIs, which was superior to positive controls (casein and hemoglobin). RPI‐1 showed ABTS+ radical scavenging (102.7 μg/ml) and angiotensin‐converting enzyme inhibitory activities (44.0%). 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nutrition</jtitle><addtitle>Food Sci Nutr</addtitle><date>2020-04</date><risdate>2020</risdate><volume>8</volume><issue>4</issue><spage>1874</spage><epage>1887</epage><pages>1874-1887</pages><issn>2048-7177</issn><eissn>2048-7177</eissn><abstract>Four roe protein isolates (RPIs) from skipjack tuna were prepared using isoelectric solubilization (pH 11 and 12) and precipitation (pH 4.5 and 5.5) (ISP) at different pH points to evaluate their physicochemical and functional properties and in vitro bioactivities. Moisture (&lt;6.3%) and protein (71%–77%) content were maintained. Sulfur, sodium, phosphorus, and potassium were the major elements, and glutamic acid and leucine were the prevalent amino acids (12.2–12.8 and 9.6–9.8 g/100 g protein, respectively) in RPIs. RPI‐1 showed the highest buffering capacity at pH 7–12. RPIs and casein showed similar water‐holding capacities. At pH 12, RPI‐1(pH 11/4.5) showed the highest solubility, followed by RPI‐3(pH 12/4.5), RPI‐2(pH 11/5.5), and RPI‐4(pH 12/5.5) (p &lt; .05). Oil‐in‐water emulsifying activity indices of RPI‐1 and RPI‐3 significantly differed. At pH 2 and 7–12, pH‐shift treatment improved the food functionality of RPIs, which was superior to positive controls (casein and hemoglobin). RPI‐1 showed ABTS+ radical scavenging (102.7 μg/ml) and angiotensin‐converting enzyme inhibitory activities (44.0%). The physicochemical properties of skipjack tuna roe protein isolate (RPI) were determined, and the isolate was found to be useful as a protein source. These RPIs were superior to the positive controls in food functionalities and confirmed to be useful as raw materials in protein‐fortified foods. RPI also showed in vitro antioxidant and antihypertensive activities. Fish RPIs recovered using isoelectric solubilization, and precipitation can be used to supplement and enhance deficient nutrients in agricultural products. By partially replacing or adding RPI to traditional foods such as noodle, confectionery, and bakery‐ and surimi‐based products, agro‐seafood products with food functionality can be developed.</abstract><cop>United States</cop><pub>John Wiley &amp; Sons, Inc</pub><pmid>32328253</pmid><doi>10.1002/fsn3.1470</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0001-7609-0303</orcidid><oa>free_for_read</oa></addata></record>
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subjects Amino acids
Angiotensin
Biological activity
Casein
Chemical precipitation
Fish
Food
food functionality
Glutamic acid
Hemoglobin
Katsuwonus pelamis
Leucine
Lipids
Original Research
pH effects
Phosphorus
physicochemical characterization
Potassium
Proteins
roe protein isolates
Scavenging
skipjack tuna
Sodium
Solubilization
Sulfur
Tuna
title Food functionalities and bioactivities of protein isolates recovered from skipjack tuna roe by isoelectric solubilization and precipitation
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