Evidence map›Paper›PMID 42164335›Full record

ReviewFood chemistry: X2026

Emerging enzymatic modifications and AI-driven strategies for smart tailoring of taste characteristics in food-derived peptides: A review.

Haoyu Xiong, Ruixi Liu, Na Zhang, Soottawat Benjakul, Yuhao Zhang, Yu Fu

Abstract readReview
In one paragraph

Review in Food chemistry: X, 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

6 authors.

Haoyu XiongCollege of Food Science, Southwest University, Chongqing 400715, China.
Ruixi LiuCollege of Food Science, Southwest University, Chongqing 400715, China.
Na ZhangCollege of Food Engineering, Harbin University of Commerce, Harbin 150028, China.
Soottawat BenjakulInternational Center of Excellence in Seafood Science and Innovation, Faculty of Agro-Industry, Prince of Songkla University, Songkhla, Thailand.
Yuhao ZhangCollege of Food Science, Southwest University, Chongqing 400715, China.
Yu FuCollege of Food Science, Southwest University, Chongqing 400715, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Food-derived peptides hold promise for food applications but are often limited by bitterness. Emerging enzymatic modification offers a novel strategy to improve sensory properties. This review aims to summarize the structural characteristics and taste-active properties of peptides and further highlights recent advances in enzymatic approaches for reducing bitterness and enhancing umami, saltiness and kokumi, combined with AI-assisted prediction and enzyme engineering. Peptide taste is governed by amino-acid composition, molecular conformation, and environmental factors; enzymatic modification alters composition and spatial structure to improve solubility and receptor interactions, thereby mitigating bitterness and enhancing umami, saltiness, and kokumi. Despite limitations in enzyme availability, efficiency, and scalability, advances in enzyme discovery and engineering support precise taste modulation for food application. The integration of AI and computer-assisted technologies has significantly advanced the smart tailoring and industrial application of taste-active peptides. This review provides a theoretical reference for enzymatic modifications and smart tailoring of taste-active peptides.

Indexed as

AIDebitteringEnzymatic modificationStructure-taste relationshipTaste-active peptidesTaste modulationUmamiγ-Glutamylation

Identifiers

PMID42164335
PMCPMC13185919

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.