pH-shifting extraction reveals conformation-dependent flavor binding to sea cucumber collagen proteins.

Xinran Li, Enhui Ma, Qiang Geng, Jian Jiao, Songyi Lin

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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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5 authors.

Xinran LiSKL of Marine Food Processing & Safety Control, National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China.

Enhui MaSKL of Marine Food Processing & Safety Control, National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China.

Qiang GengSKL of Marine Food Processing & Safety Control, National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China.

Jian JiaoBeijing Tong Ren Tang Health (Dalian) Seafoods Co., Ltd., Dalian 116045, China.

Songyi LinSKL of Marine Food Processing & Safety Control, National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sea cucumber collagen fibers (SCCF) are important nutritional and functional resources in aquatic foods, yet their interactions with flavor compounds remain insufficiently understood. This study innovatively applied pH-shifting extraction to isolate sea cucumber collagen fiber proteins extracted at alkaline (ALP), neutral (NP), and acidic pH (ACP), revealing conformation-dependent mechanisms in flavor binding. Key amino acids (Glu, Gly, Phe) were identified as crucial for structural stability and binding potential. Multi-spectroscopic analyses demonstrated that flavor interaction induced significant conformational changes: a reduction in α-helix and β-sheet content, with an increase in β-turns and random coils. FL and FTIR spectra confirmed that hydrogen bonding and hydrophobic interactions were the dominant forces driving complex formation. The molecular weight distribution and amino acid composition of the proteins varied substantially with extraction pH, directly influencing their distinct flavor-binding capacities. These findings provide a novel strategy for optimizing flavor retention in seafood by tailoring protein extraction conditions.

Indexed as

Amino acid compositionConformational changesFlavor-protein interactionpH-shiftingSea cucumber alkaline protein

Identifiers

PMID42232498

DOI10.1016/j.fochx.2026.104012

PMCPMC13223797

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LicenceCC BY-NC-ND

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