Evidence map›Paper›PMID 41454612›Full record

ArticleJournal of food science2026

Enzymatic Hydrolysis and Characterization of Protein Concentrate Obtained From Mechanically Separated Meat of Nile Tilapia (Oreochromis niloticus).

Poliana Dos Santos Mendes, Flávia Aparecida Reitz Cardoso, Maria Fernanda Giugiolli, Gabriela Wolhmuth, Maria Isabel Campos Oliveira, Vitória de Freitas Fante, Jéssica Novelo Nascimento Brenag, Evandro Bona, Patrícia Casarin, Adriana Aparecida Droval Arcain

Abstract read
In one paragraph

Article in Journal of food science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Poliana Dos Santos MendesPostgraduate Program of Food Technology (PPGTA), Federal University of Technology-Paraná (UTFPR), Campo Mourão, Brazil.
Flávia Aparecida Reitz CardosoPostgraduate Program of Food Technology (PPGTA), Federal University of Technology-Paraná (UTFPR), Campo Mourão, Brazil.ORCID https://orcid.org/0000-0002-0432-9191
Maria Fernanda GiugiolliDepartment of Food Engineering and Chemical Engineering, Federal University of Technology-Paraná (UTFPR), Campo Mourão, Brazil.
Gabriela WolhmuthPostgraduate Program of Food Technology (PPGTA), Federal University of Technology-Paraná (UTFPR), Campo Mourão, Brazil.
Maria Isabel Campos OliveiraDepartment of Food Engineering and Chemical Engineering, Federal University of Technology-Paraná (UTFPR), Campo Mourão, Brazil.
Vitória de Freitas FanteDepartment of Food Engineering and Chemical Engineering, Federal University of Technology-Paraná (UTFPR), Campo Mourão, Brazil.
Jéssica Novelo Nascimento BrenagPostgraduate Program of Food Technology (PPGTA), Federal University of Technology-Paraná (UTFPR), Campo Mourão, Brazil.
Evandro BonaPostgraduate Program of Food Technology (PPGTA), Federal University of Technology-Paraná (UTFPR), Campo Mourão, Brazil.
Patrícia CasarinPostgraduate Program of Food Technology (PPGTA), Federal University of Technology-Paraná (UTFPR), Campo Mourão, Brazil.
Adriana Aparecida Droval ArcainPostgraduate Program of Food Technology (PPGTA), Federal University of Technology-Paraná (UTFPR), Campo Mourão, Brazil.

Funding

Conselho Nacional de Desenvolvimento Científico e Tecnológico 302078/2023-1
6 · The paper itself

Abstract

The valorization of mechanically separated meat (MSM) from Nile tilapia through enzymatic hydrolysis can convert an underutilized co-product into functional ingredients; however, a practical balance between the degree of hydrolysis (DH) and techno-functional performance remains underexplored. This study aimed to optimize hydrolysis conditions and clearly define the treatments, enzyme (alcalase or papain), concentration (0.3975%-1.1025%), and time (0.385%-4.615 h), and to characterize the resulting fish protein hydrolysates (FPHs) in terms of solubility and emulsifying properties. A central composite rotatable design was used to evaluate the specified factors. Responses included solubility at pH 5.0, 7.0, and 9.0, emulsifying activity index (EAI), emulsion stability index (ESI), and qualitative FTIR. The optimized condition with alcalase (1.1025%, 4.615 h) yielded a DH of 13.80%, while the design-center condition yielded 2.06%, accompanied by improved solubility at neutral/alkaline pH and higher EAI/ESI. Papain tended to generate higher DH ranges in certain conditions but exhibited lower solubility near its isoelectric point (pI). Principal component analysis captured enzyme-dependent patterns linking DH and solubility. Collectively, the results indicate that tuning enzyme specificity, dose, and time enables the production of tailored FPH with balanced functionality, making it potentially suitable for use as clean-label emulsifiers or for protein enrichment, thereby supporting circular economy strategies by upcycling MSM. Because in-depth structural assays (e.g., peptide profiling, amino acid composition, zeta potential) were beyond the scope, we identify them as future steps to strengthen structure-function interpretation and validation in real food matrices. Standardized reporting of units (% DH) and clear treatment definitions can facilitate comparability across studies and accelerate the translation of findings.

Indexed as

CichlidsFish ProteinsMeatAnimalsEmulsionsFood HandlingHydrogen-Ion ConcentrationHydrolysisPapainProtein HydrolysatesSolubilitySubtilisinsEmulsionsFish ProteinsPapainProtein HydrolysatesSubtilisinsalcalasedegree of hydrolysisemulsifying propertiesfish protein hydrolysatemechanically separated meatpapain

Identifiers

PMID41454612
PMCPMC12743232

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.