Food Gels: Gelling Process and Advanced Applications

A special issue of Gels (ISSN 2310-2861). This special issue belongs to the section "Gel Processing and Engineering".

Deadline for manuscript submissions: 30 September 2024 | Viewed by 1732

Special Issue Editors


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Guest Editor
College of Light Industry and Food Engineering, Nanjing Forestry University, Nanjing 210037, China
Interests: food protein hydrogels; edible films; food emulsions; protein oxidation
Special Issues, Collections and Topics in MDPI journals
Department of Food Science and Technology, School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing 210097, China
Interests: food emulsions; bioactive compounds delivery; multiple component interactions
Special Issues, Collections and Topics in MDPI journals
School of Food Science and Technology, Natural Food Macromolecule Research Center, Shaanxi University of Science and Technology, Xi'an 710016, China
Interests: protein structure and function; protein chemistry; meat science and technology; active packaging
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Food proteins play an important role in the food industry, especially in recent years, due to high demand in terms of quality and quantity. Many attempts have been made to explore the potential proteins originating from land and forests. These proteins could replace or partially replace traditional proteins exerting technical functionalities or nutrition.

However, the related research on the functional properties of these proteins serving as food stuff is not enough. It is essential to investigate their comprehensive properties and potential physicochemical changes in food processing, storage, and modification. In particular, the gelling properties of plant proteins play a major role in the food matrix and nutrients/bioactive carriers. Additionally, proteins from unique plants (e.g., ginkgo biloba, xanthoceras sorbifolium bunge, and almonds) are important supplements to food protein resources. To promote the practical applications of plant proteins in the food industry, improving their gelling properties or exploring food processing techniques to enhance the gels of the proteins is highly urgent.

This Special Issue aims to publish research results regarding edible/nutritive proteins from plants and related innovative processing techniques, or insight into the mechanism of the formation or understanding of enhanced plant protein-based gels, which can potentially contribute to the development of new food proteins and their utilization via gel forms.

Dr. Yaosong Wang
Dr. Weiwei Li
Dr. Yungang Cao
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 100 words) can be sent to the Editorial Office for announcement on this website.

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. Gels is an international peer-reviewed open access monthly 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 2600 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

  • plant proteins from unique plants
  • hydrogels and their gelling properties
  • physical, chemical, and enzymatic modification
  • protein extraction, storage, and oxidation
  • emerging techniques for enhanced gels

Published Papers (1 paper)

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Research

14 pages, 4785 KiB  
Article
L-Theanine Improves the Gelation of Ginkgo Seed Proteins at Different pH Levels
by Luyan Zhang, Huifang Ge, Jing Zhao, Changqi Liu and Yaosong Wang
Gels 2024, 10(2), 131; https://0-doi-org.brum.beds.ac.uk/10.3390/gels10020131 - 6 Feb 2024
Viewed by 1249
Abstract
L-theanine (L-Th), a non-protein amino acid naturally found in teas and certain plant leaves, has garnered considerable attention due to its health benefits and potential to modify proteins such as ginkgo seed proteins, which have poor gelling properties, thereby expanding their applications in [...] Read more.
L-theanine (L-Th), a non-protein amino acid naturally found in teas and certain plant leaves, has garnered considerable attention due to its health benefits and potential to modify proteins such as ginkgo seed proteins, which have poor gelling properties, thereby expanding their applications in the food industry. The objective of this study was to investigate the impact of varying concentrations of L-Th (0.0%, 0.5%, 1.0%, and 2.0%) on the gelling properties of ginkgo seed protein isolate (GSPI) at various pH levels (5.0, 6.0, and 7.0). The GSPI gels exhibited the highest strength at a pH of 5.0 (132.1 ± 5.6 g), followed by a pH of 6.0 (95.9 ± 3.9 g), while a weak gel was formed at a pH of 7.0 (29.5 ± 0.2 g). The incorporation of L-Th increased the hardness (58.5–231.6%) and springiness (3.0–9.5%) of the GSPI gels at a pH of 7.0 in a concentration-dependent manner. However, L-Th did not enhance the gel strength or water holding capacity at a pH of 5.0. The rheological characteristics of the GSPI sols were found to be closely related to the textural properties of L-Th-incorporated gels. To understand the underlying mechanism of L-Th’s effects, the physicochemical properties of the sols were analyzed. Specifically, L-Th promoted GSPI solubilization (up to 7.3%), reduced their hydrophobicity (up to 16.2%), reduced the particle size (up to 40.9%), and increased the ζ potential (up to 21%) of the sols. Overall, our findings suggest that L-Th holds promise as a functional ingredient for improving gel products. Full article
(This article belongs to the Special Issue Food Gels: Gelling Process and Advanced Applications)
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