Conjugation of sunflower meal protein hydrolysates with chlorogenic acid: Structural changes and functional properties.

Sarina Ma, Xili Dege, Zhenyuan Li, Karim Gafurov, Dilshoda Safarava, Qin Guo, Qiang Wang

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Article in Food chemistry: X, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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7 authors.

Sarina MaCollege of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot, China.

Xili DegeCollege of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot, China.

Zhenyuan LiInstitute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Beijing, China.

Karim GafurovBukhara State Technical University, Bukhara, 200100, Uzbekistan.

Dilshoda SafaravaBukhara State Technical University, Bukhara, 200100, Uzbekistan.

Qin GuoInstitute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Beijing, China.

Qiang WangInstitute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Beijing, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Appropriate modification of sunflower meal protein with polyphenols can greatly increase its functional properties and improve the utilization rate of by-product as a lower price protein source. The present work analyzed effects of covalent conjugation of chlorogenic acid (CGA) to sunflower meal protein hydrolysate (SMPH) on its structural and functional properties. Covalent modification at increasing CGA concentrations (0.2-1.0 mg/mL) caused color changes, reduced free amino, thiol, and tyrosine groups, as well as significantly increased particle size and polyphenol bound equivalents of SMPH. Enhanced random coil content indicated protein unfolding and structural disorder. Fluorescence intensity and surface hydrophobicity decreased, indicating that CGA and SMPH had interacted. Antioxidant activity and emulsifying capacity improved dose-dependently, with 1.0 mg/mL CGA yielding the highest ABTS·

Indexed as

Antioxidant capacityChlorogenic acidEmulsifying activityStructural changesSunflower protein hydrolysate

Identifiers

PMID42006645

DOI10.1016/j.fochx.2026.103800

PMCPMC13089077

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LicenceCC BY-NC-ND

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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.