Evidence map›Paper›PMID 41245189›Full record

ArticleFood science & nutrition2025

Enzymatic Hydrolysis With Pepsin Enhanced the Nutrient Compositions of Unfractionated Soy Protein Hydrolysate and Its Cell Viability and Nitric Oxide Activities.

Oluwafemi Ayodeji Idowu, Chutha Takahashi Yupanqui

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Article in Food science & nutrition, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

2 authors.

Oluwafemi Ayodeji IdowuFunctional Food and Nutrition Program, Center of Excellence in Functional Foods and Gastronomy, Faculty of Agro-Industry Prince of Songkla University Hat Yai Songkhla Thailand.ORCID https://orcid.org/0000-0003-2791-7460
Chutha Takahashi YupanquiFunctional Food and Nutrition Program, Center of Excellence in Functional Foods and Gastronomy, Faculty of Agro-Industry Prince of Songkla University Hat Yai Songkhla Thailand.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The crude soy protein isolate (SPI), a by-product of soybean processing, is a valuable source of plant proteins but is limited by poor digestibility, low solubility, and restricted functionality due to its high molecular weight. Enzymatic hydrolysis offers an effective way to overcome these limitations. This study aimed to develop soy protein hydrolysate (SPH) using pepsin and evaluate its nutrient composition, antioxidant, and anti-inflammatory activities. SPI was pre-incubated and hydrolyzed with pepsin at an enzyme-to-substrate ratio of 1.5% (w/w) for 4 h. The molecular weights of SPI and SPH were determined by SDS-PAGE. The nutrient composition, antioxidant (DPPH, FRAP, ORAC), cell viability, and the inhibitory effect of the SPH on nitric oxide-mediated inflammation were evaluated using RAW-264.7 cells. SDS-PAGE analysis revealed that SPH had lower molecular weight peptides (< 20 kDa) compared to crude SPI (> 65 kDa). The hydrolysate showed a high protein recovery yield (89.70%) and consisted of 71.18% protein, 13.66% carbohydrates, 13.14% dietary fiber, 10.79% ash, 2.45% moisture, 1.92% fat, sodium (5496.63 mg), calcium (85.53 mg), and iron (6.54 mg), providing 356.64 kcal/100 g energy. Amino acid profiling indicated 45.36% essential and 54.70% non-essential amino acids, with glutamate being predominant (18.35%). SPH exhibited significant (

Indexed as

amino acid compositionanti‐inflammationantioxidantenzyme hydrolysispepsinsoy protein hydrolysate

Identifiers

PMID41245189
PMCPMC12618858

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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.