Evidence map›Paper›PMID 41430097›Full record

ArticleScientific reports2025

Hydrolysis kinetics amino acid profiling and antioxidant properties of enzymatic hydrolysates from desalted egg white.

Saowaluk Rungchang, Chayanid Sringarm, Sonthaya Numthuam, Naruemon Tosuk, Tipawan Thongsuk, Mahattanee Phinyo, Thunnalin Winuprasith, Sudarat Jiamyangyuen

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Circular Valorization of Yellowfin Tuna (Molecules (Basel, Switzerland) · 2026
    Article
  2. 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

8 authors.

Saowaluk RungchangDepartment of Agro-Industry, Faculty of Agriculture Natural Resources and Environment, Naresuan University, Phitsanulok, 65000, Thailand.
Chayanid SringarmDepartment of Agro-Industrial, Food, and Environmental Technology, Faculty of Applied Science, King Mongkut's University of Technology North Bangkok (KMUTNB), Bangkok, 10800, Thailand.
Sonthaya NumthuamDepartment of Agricultural Science, Faculty of Agriculture, Natural Resources and Environment, Naresuan University, Phitsanulok, 65000, Thailand.
Naruemon TosukDepartment of Agro-Industry, Faculty of Agriculture Natural Resources and Environment, Naresuan University, Phitsanulok, 65000, Thailand.
Tipawan ThongsukDepartment of Agro-Industry, Faculty of Agriculture Natural Resources and Environment, Naresuan University, Phitsanulok, 65000, Thailand.
Mahattanee PhinyoDepartment of Agricultural Science, Faculty of Agriculture, Natural Resources and Environment, Naresuan University, Phitsanulok, 65000, Thailand.
Thunnalin WinuprasithInstitute of Nutrition, Mahidol University, Nakhon Pathom, 73170, Thailand.
Sudarat JiamyangyuenDivision of Food Science and Technology, Faculty of Agro-Industry, Chiang Mai University, Chiang Mai, 50100, Thailand. sudarat.j@cmu.ac.th.

Funding

Naresuan University (NU) and National Science, Research and Innovation Fund (NSRF) R2568B049
6 · The paper itself

Abstract

Salted egg white is a nutrient-rich by-product that is usually discarded due to its high salt content. It has strong potential for value-added transformation through enzymatic hydrolysis. This study aimed to generate peptide-rich hydrolysates with antioxidant potential from desalted salted egg white using single and combined protease systems. Hydrolysis was carried out using three enzymatic systems: MSD (a dual endo- and exo-protease), Thermoase GL (a thermostable endo-protease), and a combination of both. The hydrolysis process was monitored at 0, 1, 3, and 6 h. The hydrolysates were characterized in terms of degree of hydrolysis (DH), amino acid release, kinetic parameters, synergy analysis and antioxidant activity. MSD exhibited the highest hydrolytic efficiency, releasing up to 338.46 ± 0.05 mg/g d.b. of free amino acids, while GL showed limited activity under the test conditions. The combined enzymes system enhanced peptide release, showing a synergy factor of 1.87 at 3 h. Kinetic modeling (zero-, first-and second-order) suggested that GL enhanced MSD-mediated hydrolysis by increasing substrate accessibility. Antioxidant assays revealed that MSD alone had the highest activity, with 84.14% 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging at 3 h and 31.20 nmol Trolox equivalents (TE)/mL ferric reducing antioxidant power (FRAP) at 1 h. These values were higher than those from GL and mixed treatments. Principal component analysis (PCA) revealed that amino acids such as phenylalanine, leucine, methionine, and tyrosine were key markers for distinguishing MSD and mixed enzyme hydrolysates from GL samples based on enzyme type and hydrolysis time. Overall, the results highlight the effectiveness of MSD in producing antioxidant-rich peptides and demonstrate that appropriate enzyme selection and combinations can yield functional hydrolysates from underutilized food by-products.

Indexed as

Amino AcidsAntioxidantsEgg WhiteProtein HydrolysatesAnimalsEndopeptidasesHydrolysisKineticsPeptide HydrolasesAmino AcidsAntioxidantsEndopeptidasesPeptide HydrolasesProtein HydrolysatesAmino acid profilingAntioxidant activityDesalted egg whiteEnzymatic hydrolysisEnzyme synergy

Identifiers

PMID41430097
PMCPMC12722750

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.