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Protein-Based Functional Colloids and Their Potential Applications in Foods
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Protein-Based Functional Colloids and Their Potential Applications in Foods

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Physics and (Bio)Chemistry".

Deadline for manuscript submissions: 20 May 2024 | Viewed by 4445

Special Issue Editors

Dr. Hongdong Song

E-Mail Website
Guest Editor
School of Health Sciences and Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China
Interests: food protein/peptide-based colloids; peptide self-assembly; nanocarrier; bioactive peptides; molecular nutrition; absorption and distribution; cereal chemistry
Prof. Dr. Lei Dai

E-Mail Website
Guest Editor
College of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, China
Interests: emulsions; plant-based food; delivery system; nanoparticle; intelligent biopolymer food packaging; functional food; digestive properties; protein corona
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The use of food-derived proteins for developing novel functional colloids has grown extensively in recent years due to sustainability, ethical and health reasons. There has been increasing interest over the years in protein-based functional colloids and utilizing these colloids in food systems has been a target for many researchers. Different types of protein-based colloidal systems with unique properties, including micro- or nanoparticles, emulsions, foams, gels, and films, have been reported. Some existing challenges needed to be addressed, including those associated with a deep understanding of protein molecular structure and its relationship with colloid formation characteristics; protein interactions with other components; controlled formation of desirable protein-based colloids; stability in vitro and in vivo; and the targeted delivery of protein-based functional colloids.

In this Special Issue of Foods, we are encouraging the submission of manuscripts focused on the study of protein or peptide-based functional colloids, such as micro- or nanoparticles, emulsions, foams, gels and films. We welcome papers related to the fabrication, characterization, in vitro and in vivo stability, target delivery and applications of protein or peptide-based functional colloids. This Special Issue aims to gather the latest and novel research and advances in the field.

Dr. Hongdong Song
Prof. Dr. Lei Dai
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. Foods 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 2900 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

  • protein colloids
  • protein or peptide self-assembly
  • micro- or nanoparticles
  • pickering emulsions
  • gels
  • films
  • encapsulation
  • target delivery
  • digestion

Published Papers (3 papers)

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Research

13 pages, 2024 KiB  
Article
Caffeic Acid Phenethyl Ester Encapsulated in Self-Assemble Rice Peptides Nanoparticles: Storage Stability, In Vitro Release, and Their Interaction Mechanisms
by Xinyue Wang, Siyi Feng and Hongdong Song
Foods 2024, 13(5), 755; https://doi.org/10.3390/foods13050755 - 29 Feb 2024
Viewed by 545
Abstract
Caffeic acid phenethyl ester (CAPE) is an important active component of propolis with many bioactivities. However, its efficiency and practical application are restricted due to its poor aqueous solubility and storage stability. In this study, a nanocarrier was fabricated to encapsulate CAPE using [...] Read more.
Caffeic acid phenethyl ester (CAPE) is an important active component of propolis with many bioactivities. However, its efficiency and practical application are restricted due to its poor aqueous solubility and storage stability. In this study, a nanocarrier was fabricated to encapsulate CAPE using self-assembled rice peptides obtained by controllable enzymolysis. The physicochemical properties, encapsulation efficiency, and loading capacity of rice peptides nanoparticles (RPNs) were characterized. The storage stability, in vitro release, and interaction mechanisms between CAPE and RPNs were investigated. The results showed that RPNs, mainly assembled by disulfide bonds and hydrogen bonds, possessed an effective diameter of around 210 nm and a high encapsulation efficiency (77.77%) and loading capacity (3.89%). Importantly, the water solubility of CAPE was increased by 45 times after RPNs encapsulation. Moreover, RPNs encapsulation also significantly increased CAPE stability, about 1.4-fold higher than that of unencapsulated CAPE after 18-day storage. An in vitro release study demonstrated that RPNs could delay the release of CAPE, implying a better CAPE protection against extreme environments during digestion. Hydrogen bond and van der Waals force are the predominant interaction forces between RPNs and CAPE. Therefore, the newly developed nanoparticle is a potential delivery system that could effectively improve the aqueous solubility and stability of CAPE. Full article
(This article belongs to the Special Issue Protein-Based Functional Colloids and Their Potential Applications in Foods)
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17 pages, 3672 KiB  
Article
Different Characteristics of Annealed Rice Kernels and Flour and Their Effects on the Quality of Rice Noodles
by Ziwen Zhang, Mengshan Shang, Xiaoyu Chen, Lei Dai, Na Ji, Yang Qin, Yanfei Wang, Liu Xiong, Qingjie Sun and Fengwei Xie
Foods 2023, 12(9), 1914; https://doi.org/10.3390/foods12091914 - 07 May 2023
Cited by 1 | Viewed by 1886
Abstract
In this study, the characteristics of indica rice kernels (IRK) and flour (IRF) annealed in different conditions were evaluated, and the quality of rice noodles made with these IRK and IRF was determined. Native IRK and IRF were annealed in deionized water at [...] Read more.
In this study, the characteristics of indica rice kernels (IRK) and flour (IRF) annealed in different conditions were evaluated, and the quality of rice noodles made with these IRK and IRF was determined. Native IRK and IRF were annealed in deionized water at a kernel or flour to water ratio of 1:3 (w/v) and temperatures of 50, 55, 60, and 65 °C for 12 and 24 h. Annealing increased the paste viscosity of IRK while decreasing that of IRF. Both annealed IRK and IRF exhibited increases in the gelatinization enthalpy change and relative crystallinity. Annealed IRK gel showed higher hardness, and annealed IRF gel displayed greater springiness. Unlike native rice noodles, annealed IRK noodles exhibited denser pores, while annealed IRF noodles exhibited a looser microstructure. With increasing annealing temperature and time, both annealed IRK and IRF noodles showed enhanced tensile properties. Rice noodles made from IRF annealed at 65 °C for 12 h exhibited a fracture strain of 2.7 times that of native rice noodles. In brief, IRK and IRF exhibited different degrees of susceptibility to annealing. Annealing had more significant effects on IRF than IRK. This study highlights the possibility of using annealed IRK and IRF in rice noodles. Full article
(This article belongs to the Special Issue Protein-Based Functional Colloids and Their Potential Applications in Foods)
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14 pages, 4067 KiB  
Article
Study on the Interaction Mechanism of Theaflavin with Whey Protein: Multi-Spectroscopy Analysis and Molecular Docking
by Jia Xu, Yi Huang, Yang Wei, Xinchu Weng and Xinlin Wei
Foods 2023, 12(8), 1637; https://doi.org/10.3390/foods12081637 - 13 Apr 2023
Cited by 3 | Viewed by 1537
Abstract
The interaction mechanism of whey proteins with theaflavin (TF1) in black tea was analyzed using multi-spectroscopy analysis and molecular docking simulations. The influence of TF1 on the structure of bovine serum albumin (BSA), β-lactoglobulin (β-Lg), and α-lactoalbumin (α-La) was examined in this work [...] Read more.
The interaction mechanism of whey proteins with theaflavin (TF1) in black tea was analyzed using multi-spectroscopy analysis and molecular docking simulations. The influence of TF1 on the structure of bovine serum albumin (BSA), β-lactoglobulin (β-Lg), and α-lactoalbumin (α-La) was examined in this work using the interaction of TF1 with these proteins. Fluorescence and ultraviolet-visible (UV-vis) absorption spectroscopy revealed that TF1 could interact with BSA, β-Lg and α-La through a static quenching mechanism. Furthermore, circular dichroism (CD) experiments revealed that TF1 altered the secondary structure of BSA, β-Lg and α-La. Molecular docking demonstrated that the interaction of TF1 with BSA/β-Lg/α-La was dominated by hydrogen bonding and hydrophobic interaction. The binding energies were −10.1 kcal mol−1, −8.4 kcal mol−1 and −10.4 kcal mol−1, respectively. The results provide a theoretical basis for investigating the mechanism of interaction between tea pigments and protein. Moreover, the findings offered technical support for the future development of functional foods that combine tea active ingredients with milk protein. Future research will focus on the effects of food processing methods and different food systems on the interaction between TF1 and whey protein, as well as the physicochemical stability, functional characteristics, and bioavailability of the complexes in vitro or in vivo. Full article
(This article belongs to the Special Issue Protein-Based Functional Colloids and Their Potential Applications in Foods)
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