Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
5.8
5.2
Journals
Foods
Special Issues
Proteins in Food Processing
share announcement

Proteins in Food Processing

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

Deadline for manuscript submissions: closed (31 August 2023) | Viewed by 13356

Special Issue Editors

Prof. Dr. Guanghua Zhao

E-Mail Website
Guest Editor
College of Food Science & Nutritional Engineering, China Agricultural University, Beijing 100083, China
Interests: protein structure and function; food nanomaterials; ferritin; protein self-assembly; iron nutrition
Dr. Chenyan lv

E-Mail Website
Guest Editor
College of Food Science & Nutritional Engineering, China Agricultural University, Beijing, China
Interests: protein applications in nutrition; interaction between protein and bioactive molecules

Special Issue Information

Dear Colleagues,

Proteins are main components in food, especially cereals, meat, eggs, milk, and fishery products. The properties and structures of protein are closely related to the food quality. Food processing including chemical and physical treatment may lead to changes in the protein structure and function. This Special Issue will look at the structure and function of proteins during food processing. It not only includes the purification and structural characterization of proteins and the interaction between proteins and other food components during food processing but also the functional properties of them. In addition, the effects of protein changes during food processing on food safety and nutritional evaluation of proteins will also be welcome. The proteins discussed should be closely related to the food-processing and food industry.

Prof. Dr. Guanghua Zhao
Dr. Chenyan lv
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 structure and function
  • nutrition
  • interactions
  • food safety

Published Papers (5 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

Jump to: Review

14 pages, 768 KiB  
Article
Meat Substitute Markets: A Comparative Analysis of Meat Analogs in Austria
by Christof Falkenberg, Alena Trexler, Christian Garaus and Siegfried Pöchtrager
Foods 2023, 12(11), 2211; https://doi.org/10.3390/foods12112211 - 31 May 2023
Cited by 1 | Viewed by 1793
Abstract
The consumption of meat substitutes has significantly grown over the last decade. To understand the extent to which plant-based meat alternatives can already substitute conventional meat in terms of price and nutritional value, detailed knowledge of current market offerings is essential. We conducted [...] Read more.
The consumption of meat substitutes has significantly grown over the last decade. To understand the extent to which plant-based meat alternatives can already substitute conventional meat in terms of price and nutritional value, detailed knowledge of current market offerings is essential. We conducted an analysis of 38 plant-based minced products and 36 plant-based sausage products in Austrian supermarkets. The data were obtained using standardized observation in Austrian supermarkets reflecting 90% of the current market, expanded further through secondary data, and analyzed the generated dataset using mean value comparison. To provide a broader perspective on the trends in these markets, we incorporate results from a comparative study conducted in Australia. Our results obtained through t-tests revealed that there is no statistically significant difference in the protein content of plant-based meat substitutes and conventional meat (at the 95% confidence interval), underscoring the potential of meat substitutes as an alternative source of protein. Offering comparable protein content but with significantly lower caloric intake (at the 1% significance level), plant-based substitutes may contribute to reducing obesity in industrialized countries. The findings also reveal that plant-based products continue to be priced significantly higher than conventional meat (at the 1% significance level). We found substantial differences in ingredients and other nutritional values of plant-based products between Austria and Australia, although the main protein sources are the same in both countries, with peas being included in 60 out of 74 and soy in 27 out of 74 Austrian products. Our article concludes with a discussion of the implications for scholars and policymakers and identifies new avenues for future research. Full article
(This article belongs to the Special Issue Proteins in Food Processing)
►▼ Show Figures

Figure 1

12 pages, 4151 KiB  
Article
Investigation of the Structure and Allergic Potential of Whey Protein by Both Heating Sterilization and Simulation with Molecular Dynamics
by Zhao Zhang, Ruida Ma, Yunpeng Xu, Lei Chi, Yue Li, Guangqing Mu and Xuemei Zhu
Foods 2022, 11(24), 4050; https://doi.org/10.3390/foods11244050 - 14 Dec 2022
Cited by 5 | Viewed by 1618
Abstract
As the main allergens in milk, whey proteins are heat-sensitive proteins and are widespread in dairy products and items in which milk proteins are involved as food additives. The present work sought to investigate the effect of heating sterilization on the allergenicity of [...] Read more.
As the main allergens in milk, whey proteins are heat-sensitive proteins and are widespread in dairy products and items in which milk proteins are involved as food additives. The present work sought to investigate the effect of heating sterilization on the allergenicity of α-lactalbumin (α-LA) and β-lactoglobulin (β-LG), the main composite and allergen in whey protein isolate (WPI), by combining molecular dynamics with experimental techniques for detecting the spatial structure and IgE binding capacity. The structure of WPI was basically destroyed at heat sterilization conditions of 95 °C for 5 min and 65 °C for 30 min by SDS-PAGE analysis and spectroscopic analysis. In addition, α-lactalbumin (α-LA) may be more sensitive to temperature, resulting in exposure to allergic epitopes and increasing the allergic potential, while the binding capacity of β-lactoglobulin (β-LG) to IgE was reduced under 65 °C for 30 min. By the radius of gyration (Rg) and root-mean-square deviation (RMSD) plots calculated in molecular dynamics simulations, α-LA was less structurally stable at 368 K, while β-LG remained stable at higher temperatures, indicating that α-LA was more thermally sensitive. In addition, we observed that the regions significantly affected by temperatures were associated with the capacity of allergic epitopes (α-LA 80–101 and β-LG 82–93, 105–121) to bind IgE through root-mean-standard fluctuation (RMSF) plots, which may influence the two major allergens. We inferred that these regions are susceptible to structural changes after sterilization, thus affecting the allergenicity of allergens. Full article
(This article belongs to the Special Issue Proteins in Food Processing)
►▼ Show Figures

Figure 1

15 pages, 3665 KiB  
Article
Microencapsulation of Carvacrol by Complex Coacervation of Walnut Meal Protein Isolate and Gum Arabic: Preparation, Characterization and Bio-Functional Activity
by Jishuai Sun, Yishen Cheng, Tuo Zhang and Jiachen Zang
Foods 2022, 11(21), 3382; https://doi.org/10.3390/foods11213382 - 27 Oct 2022
Cited by 7 | Viewed by 2301
Abstract
As a natural phenolic compound, carvacrol has attracted much attention due to its excellent antibacterial and antioxidant activities. However, its application is limited due to its instability, such as easy volatilization, easy oxidation, etc. Protein-polysaccharide interactions provide strategies for improving their stability issues. [...] Read more.
As a natural phenolic compound, carvacrol has attracted much attention due to its excellent antibacterial and antioxidant activities. However, its application is limited due to its instability, such as easy volatilization, easy oxidation, etc. Protein-polysaccharide interactions provide strategies for improving their stability issues. In this study, the plant-based carvacrol microcapsules via complex coacervation between walnut meal protein isolate (WMPI) and gum Arabic (GA) has been fabricated and characterized. The formation conditions of WMPI-GA coacervates were determined by some parameters, such as pH, zeta-potential, and turbidity. The optimum preparation conditions were achieved at pH 4.0 with a WMPI-to-GA ratio of 6:1 (w/w). The mean particle size, loading capacity (LC), and encapsulation efficiency (EE) of the microcapsules were 43.21 μm, 26.37%, and 89.87%, respectively. Fourier transform infrared spectroscopy (FT-IR) and fluorescence microscopy further confirmed the successful microencapsulation of carvacrol. The microencapsulation of carvacrol improved the thermal stability of the free carvacrol. The swelling capacity results indicated that it could resist gastric acid, and facilitate its intestinal absorption. Meanwhile, the carvacrol molecules trapped within the microcapsules could be continuously released in a concentration-dependent manner. Furthermore, the microcapsules presented good antioxidant activity and antibacterial activity against the Gram-negative (E. coli) and the Gram-positive (S. aureus) bacteria. These results indicated that the obtained carvacrol microcapsules have a potential application value as a food preservative in the food industry. Full article
(This article belongs to the Special Issue Proteins in Food Processing)
►▼ Show Figures

Figure 1

17 pages, 4161 KiB  
Article
Structural Characterization and Evaluation of Interfacial Properties of Pea Protein Isolate–EGCG Molecular Complexes
by Shuang Han, Fengzhan Cui, David Julian McClements, Xingfeng Xu, Cuicui Ma, Yutang Wang, Xuebo Liu and Fuguo Liu
Foods 2022, 11(18), 2895; https://doi.org/10.3390/foods11182895 - 18 Sep 2022
Cited by 12 | Viewed by 3722
Abstract
There is increasing interest in using plant-derived proteins in foods and beverages for environmental, health, and ethical reasons. However, the inherent physicochemical properties and functional performance of many plant proteins limit their widespread application. Here, we prepared pea protein isolate (PPI) dispersions using [...] Read more.
There is increasing interest in using plant-derived proteins in foods and beverages for environmental, health, and ethical reasons. However, the inherent physicochemical properties and functional performance of many plant proteins limit their widespread application. Here, we prepared pea protein isolate (PPI) dispersions using a combined pH-shift/heat treatment method, and then, prepared PPI-epigallocatechin-3-gallate (EGCG) complexes under neutral conditions. Spectroscopy, calorimetry, molecular docking, and light scattering analysis demonstrated that the molecular complexes formed spontaneously. This was primarily ascribed to hydrogen bonds and van der Waals forces. The complexation of EGCG caused changes in the secondary structure of PPI, including the reduction in the α-helix and increase in the β-sheet and disordered regions. These changes slightly decreased the thermal stability of the protein. With the accretion of EGCG, the hydrophilicity of the complexes increased significantly, which improved the functional attributes of the protein. Optimization of the PPI-to-EGCG ratio led to the complexes having better foaming and emulsifying properties than the protein alone. This study could broaden the utilization of pea proteins as functional ingredients in foods. Moreover, protein–polyphenol complexes can be used as multifunctional ingredients, such as antioxidants or nutraceutical emulsifiers. Full article
(This article belongs to the Special Issue Proteins in Food Processing)
►▼ Show Figures

Graphical abstract

Review

Jump to: Research

15 pages, 4597 KiB  
Review
Recent Advances in the Study of Wheat Protein and Other Food Components Affecting the Gluten Network and the Properties of Noodles
by Peng Zang, Yang Gao, Pu Chen, Chenyan Lv and Guanghua Zhao
Foods 2022, 11(23), 3824; https://doi.org/10.3390/foods11233824 - 27 Nov 2022
Cited by 9 | Viewed by 2727
Abstract
Upon hydrating and mixing wheat flour, wheat protein forms a network that strongly affects the structure and physicochemical properties of dough, thus affecting the properties of noodles. Different approaches have been taken to alter the gluten network structure in order to control the [...] Read more.
Upon hydrating and mixing wheat flour, wheat protein forms a network that strongly affects the structure and physicochemical properties of dough, thus affecting the properties of noodles. Different approaches have been taken to alter the gluten network structure in order to control the dough properties. In the current review, we summarize the structure and function of wheat protein, including glutenin and gliadin, and describe food components that may affect noodle quality by interacting with wheat protein. In fact, the ratio of glutenin to gliadin is closely related to the viscosity of dough, and disulfide bonds also contribute to the gluten network formation. Meanwhile, wheat protein coexists with starch and sugar in wheat dough, and thus the nature of starch may highly influence gluten formation as well. Salts, alkali, enzymes and powdered plant food can be added during dough processing to regulate the extensional properties of wheat noodles, obtaining noodles of high quality, with improved sensory and storage properties. This review describes specific methods to reinforce the wheat protein network and provides a reference for improving noodle quality. Full article
(This article belongs to the Special Issue Proteins in Food Processing)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-5
Back to TopTop