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Chemical Modifications and Interactions of Food Macromolecules: Mechanisms and Impacts on Quality

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Food Chemistry".

Deadline for manuscript submissions: 28 February 2026 | Viewed by 219

Special Issue Editors


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Guest Editor
The College of Food Science, Shenyang Agricultural University, Shenyang, China
Interests: food protein; food lipids; food chemistry; active ingredients; natural products

E-Mail Website
Guest Editor
The College of Food Science, Shenyang Agricultural University, Shenyang, China
Interests: antioxidants; functional food; food safety; HPLC-MS; glycation

Special Issue Information

Dear Colleagues,

Food macromolecules such as proteins, polysaccharides, and lipids are fundamental determinants of the structural, functional, and nutritional characteristics of food systems. Their intrinsic properties can be significantly altered by chemical modifications, whether occurring naturally during processing and storage or induced through targeted technological interventions. Such modifications, together with the complex interactions among different classes of macromolecules and bioactive compounds, critically influence food texture, stability, digestibility, and sensory attributes. Elucidating the mechanisms of these modifications and interactions is essential for advancing scientific understanding of food chemistry and for guiding the design of foods with improved quality, safety, and functionality.

This Special Issue, entitled “Chemical Modifications and Interactions of Food Macromolecules: Mechanisms and Impacts on Quality”, seeks to compile original research articles, reviews, and communications that address fundamental and applied aspects of macromolecular chemistry in foods. Contributions may encompass, but are not limited to, studies on chemical and enzymatic modifications of food macromolecules; the Maillard reaction and protein–polyphenol interactions; mechanisms of oxidation and cross-linking; molecular assembly and gelation behavior; and the resulting effects on physicochemical properties, stability, bioavailability, and sensory quality. Submissions focusing on advanced analytical methods, innovative processing technologies, and novel applications of modified macromolecules in the development of functional and sustainable foods are particularly welcome.

Prof. Dr. Ling Liu
Dr. Yixiao Shen
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 250 words) can be sent to the Editorial Office for assessment.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • lipid
  • protein
  • molecular interactions
  • food safety
  • food stability

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Published Papers (1 paper)

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Research

24 pages, 2320 KB  
Article
Alkaline Reaction Pathways of Phenolic Compounds with β-Lactoglobulin Peptides: Polymerization and Covalent Adduct Formation
by Alina Bock, Sarah Rottner, Daniel Güterbock, Ulrike Steinhäuser, Sascha Rohn and Helena Kieserling
Molecules 2025, 30(23), 4584; https://doi.org/10.3390/molecules30234584 - 28 Nov 2025
Viewed by 86
Abstract
A common strategy for a protein’s functionality modification is the covalent binding of phenolic compounds (PCs) under alkaline conditions. Whether intentionally applied or arising during food processing and storage, such reactions are highly relevant, as alkaline pH promotes oxidation, covalent adduct formation, and [...] Read more.
A common strategy for a protein’s functionality modification is the covalent binding of phenolic compounds (PCs) under alkaline conditions. Whether intentionally applied or arising during food processing and storage, such reactions are highly relevant, as alkaline pH promotes oxidation, covalent adduct formation, and polymerization, thereby altering both PC and protein properties. However, the interplay of these reactions and the impact of PC structure remain insufficiently understood. This study aimed at characterizing covalent binding products of structurally related PCs with tryptic peptides of the model protein β-lactoglobulin (β-Lg) at pH 9. Emphasis was given on substitution patterns and steric effects influencing polymerization and peptide adduct building. Hydroxycinnamic acid and flavonoid derivatives differing in hydroxyl substitution and carrying polar (glycosidic) groups were selected. Incubation products were characterized by HPLC–DAD and high-resolution mass spectrometry. Results showed that both mono- and dihydroxy PC undergo oxidation under alkaline conditions, but with distinct reactivity. Monohydroxy PCs form only limited peptide adducts due to resonance stabilization and steric hindrance. In contrast, dihydroxy PCs displayed a higher reactivity, producing more polymerization products and covalent adducts. Their enhanced reactivity is linked to the ability of quinone formation with reduced electrostatic repulsion, while additional polar substituents promote interactions with polar amino acids. At the same time, these substituents impose steric constraints on PC polymerization, modulating oligomer size and thereby influencing peptide binding. Overall, the findings highlight structural determinants of PC reactivity and provide mechanistic insight into the balance between polymerization and covalent peptide modification under alkaline conditions. Full article
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