Volume 46, Issue 8 e16753
ORIGINAL ARTICLE

Characterization of tuna dark muscle protein isolate

Trong Bach Nguyen

Corresponding Author

Trong Bach Nguyen

Faculty of Food Technology, Nha Trang University, Nha Trang, Vietnam

Correspondence

Trong Bach Nguyen, Faculty of Food Technology, Nha Trang University, No 2 Nguyen Dinh Chieu, Nha Trang 57000, Vietnam.

Email: [email protected]

Contribution: Conceptualization, Data curation, Formal analysis, Funding acquisition, ​Investigation, Project administration, Resources, Writing - original draft, Writing - review & editing

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Laurine Mule Mueni

Laurine Mule Mueni

Faculty of Food Technology, Nha Trang University, Nha Trang, Vietnam

Contribution: Data curation, ​Investigation, Validation

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Tran Nu Thanh Viet Bui

Tran Nu Thanh Viet Bui

Faculty of Food Technology, Nha Trang University, Nha Trang, Vietnam

Contribution: ​Investigation, Resources, Writing - original draft

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Huynh Nguyen Duy Bao

Huynh Nguyen Duy Bao

Faculty of Food Technology, Nha Trang University, Nha Trang, Vietnam

Contribution: Conceptualization, Methodology, Supervision

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Nguyen Thi Kim Cuc

Nguyen Thi Kim Cuc

Institute of Biotechnology and Environment, Nha Trang University, Nha Trang, Vietnam

Contribution: Data curation, ​Investigation

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Taco Nicolai

Taco Nicolai

IMMM UMR-CNRS 6283, Le Mans Université, Le Mans Cedex 9, France

Contribution: Conceptualization, Supervision, Writing - review & editing

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First published: 18 May 2022

Abstract

Fish protein isolate (FPI) was extracted from tuna dark muscle (TDM) using the pH-shift method that improves significantly its sensory quality and nutritional value. The amino-acid composition of the FPI was close to that of TDM, but the total protein content was higher. The solubility of FPI in water was higher than 85% at pH ≥ 6 and pH ≤ 3, but it dropped to about 10% at pH values close to the isoelectric point pI ≈ 5.0. The soluble FPI was present in the form of aggregates that were characterized by light-scattering. The microstructure of FPI solutions on larger length scales was probed by confocal microscopy, large protein flocs formed at pH close to pI. SDS-PAGE indicated that a significant fraction of myosin heavy chains was broken down into smaller chains. The viscosity decreased with decreasing of pH, which correlated with the decreasing size of the aggregates.

Novelty Impact Statement

Tuna dark muscle (TDM) represents a significant fraction of industrially processed tuna and it is currently considered a low value by-product because of its poor sensory qualities, but TDM has a high protein content that does not suffer from sensory defects if it is extracted by dispersing TDM at pH 12 and precipitating the dissolved protein at pH 5.5. The protein isolate is highly soluble (> 85%) in water at pH > 6 and pH < 3, where it is present in the form of small aggregates with average radii between 90 and 250 nm, depending on the pH. The characterization of the composition of TDM protein isolate and its properties in water show that it is a viable product for use in industrial applications.

CONFLICTS OF INTEREST

The authors declared no conflicts of interest.

DATA AVAILABILITY STATEMENT

The data that support the findings of this study are available from the corresponding author upon reasonable request.

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