Effects of Processing and Treatment on Protein Structure and Function

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 (22 August 2023) | Viewed by 10425

Special Issue Editors


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Guest Editor
Department of Food Science and Engineering, Northeast Agricultural University, Harbin, China
Interests: food protein modification; food emulsion; muscle foods; muscle protein; protein functionality; new processing techniques
Special Issues, Collections and Topics in MDPI journals

E-Mail Website
Guest Editor
College of Food Science, Northeast Agricultural University, Harbin 150030, China
Interests: meat products processing; gelling properties; quality profiles; novel processing technologies; functional meat products; clean label; consumer perception
Special Issues, Collections and Topics in MDPI journals
State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-Products, Institute of Food Science, Zhejiang Academy of Agricultural Sciences, Hangzhou, China
Interests: protein gel property; protein self-assembly; protein multi-scale structure; protein cross-linking; meat protein; interaction between protein and macromolecule
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The discussions on the protein structure and function in food system are gradually increasing worldwide given the impact of protein conformation and functional properties on food quality. Numerous works have successfully established the link between protein structure and function in food system. Targeted design of processing and treatment strategies to modify protein structure and optimize protein functional properties is an effective way to improve food quality. While many physical and chemical strategies have been developed in recent years to improve the functional properties of food proteins such as solubility, emulsification, foaming, gelling, etc., the potentially mechanisms require further investigation and, their industrial potential needs to be evaluated.

Therefore, this Special Issue of Foods, entitled “Effects of Processing and Treatment on Protein Structure and Function” invites works (original research papers or reviews) on the current stated of knowledge of the subject. Specifically, this Special Issue should include, but is not limited to, the following points:

  • Novel physical or chemical processing strategies to modify food protein structure and function;
  • Novel insights into the mechanism of multi-scale structural changes of food protein during processing/treatment and their relationship with protein functionality;
  • Interactions between protein and other endogenous/exogenous ingredients during food processing/treatment;
  • Methods/techniques for construction of protein-based food systems.

Dr. Haotian Liu
Prof. Dr. Qian Liu
Dr. Jin Zhang
Guest Editors

Manuscript Submission Information

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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

  • food protein
  • protein structure and function
  • physical or chemical processing strategies
  • protein structure modification
  • protein function optimization
  • solubility
  • emulsification
  • gelling
  • protein-based food systems
  • interaction between protein and other molecules

Published Papers (5 papers)

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Research

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13 pages, 3353 KiB  
Article
Effect of Heat Treatment on Protein Self-Digestion in Ruminants’ Milk
by Juliana A. S. Leite, Carlos A. Montoya, Evelyne Maes, Charles Hefer, Raul A. P. A. Cruz, Nicole C. Roy and Warren C. McNabb
Foods 2023, 12(18), 3511; https://doi.org/10.3390/foods12183511 - 21 Sep 2023
Viewed by 1042
Abstract
This study investigated whether heat treatments (raw, 63 °C for 30 min, and 85 °C for 5 min) affect protein hydrolysis by endogenous enzymes in the milk of ruminants (bovine, ovine, and caprine) using a self-digestion model. Self-digestion consisted of the incubation for [...] Read more.
This study investigated whether heat treatments (raw, 63 °C for 30 min, and 85 °C for 5 min) affect protein hydrolysis by endogenous enzymes in the milk of ruminants (bovine, ovine, and caprine) using a self-digestion model. Self-digestion consisted of the incubation for six hours at 37 °C of the ruminants’ milk. Free amino group concentration was measured by the o-phthaldialdehyde method, and peptide sequences were identified by chromatography-mass spectrometry. Results showed that heat treatments prior to self-digestion decreased the free NH2 by 59% in bovine milk heated at 85 °C/5 min, and by 44 and 53% in caprine milk heated at 63 °C/30 min and 85 °C/5 min, respectively. However, after self-digestion, only new free amino groups were observed for the raw and heated at 63 °C/30 min milk. β-Casein was the most cleaved protein in the raw and heated at 63 °C/30 min bovine milk. A similar trend was observed in raw ovine and caprine milk. Self-digestion increased 6.8-fold the potential antithrombin peptides in the bovine milk heated at 63 °C/30 min. Enhancing bioactive peptide abundance through self-digestion has potential applications in the industry for functional products. Overall, heat treatments affected the free amino groups according to the species and heat treatment applied, which was reflected in the varying degrees of cleaved peptide bonds and peptides released during self-digestion. Full article
(This article belongs to the Special Issue Effects of Processing and Treatment on Protein Structure and Function)
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16 pages, 2520 KiB  
Article
Whey Protein Hydrolysate Improved the Structure and Function of Myofibrillar Protein in Ground Pork during Repeated Freeze–Thaw Cycles
by Pengjuan Yu, Jiayan Yan, Lingru Kong, Juan Yu, Xinxin Zhao and Xinyan Peng
Foods 2023, 12(16), 3135; https://doi.org/10.3390/foods12163135 - 21 Aug 2023
Cited by 2 | Viewed by 1023
Abstract
Whey protein hydrolysate (WPH) has made a breakthrough in inhibiting oxidative deterioration and improving the quality of meat products during storage. Based on our previous study of extracting the most antioxidant active fraction I (FI, the molecular weight < 1 kDa) from whey [...] Read more.
Whey protein hydrolysate (WPH) has made a breakthrough in inhibiting oxidative deterioration and improving the quality of meat products during storage. Based on our previous study of extracting the most antioxidant active fraction I (FI, the molecular weight < 1 kDa) from whey protein hydrolysates of different molecular weights, the present study continued to delve into the effects of WPH with fraction I on the structure and function of myofibrillar proteins (MP) in ground pork during the freeze–thaw (F-T) cycles. With the number of F-T cycles raised, the total sulfhydryl content, the relative contents of α-helix, Ca2+-ATPase activity, K+-ATPase activity, solubility, emulsion activity index (EAI), and emulsion stability index (ESI) of MP gradually decreased. Conversely, the carbonyl content and the relative content of random curl showed an increasing trend. In particular, the damage to the structure and the function of MP became more pronounced after three F-T cycles. But, during F-T cycles, FI stabilized the structure of MP. Compared to the control group, the 10% FI group showed a remarkable improvement (p < 0.05) in the total sulfhydryl content, Ca2+-ATPase activity, K+-ATPase activity, solubility, EAI and ESI after multiple F-T cycles, suggesting that 10% FI could effectively inhibit protein oxidation and had the influence of preserving MP function properties. In conclusion, WPH with fraction I can be used as a potential natural antioxidant peptide for maintaining the quality of frozen processed meat products. Full article
(This article belongs to the Special Issue Effects of Processing and Treatment on Protein Structure and Function)
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21 pages, 3417 KiB  
Article
Effect of Freezing on Soybean Protein Solution
by Wenhui Li, Qiongling Chen, Xiaowen Wang and Zhenjia Chen
Foods 2023, 12(14), 2650; https://doi.org/10.3390/foods12142650 - 9 Jul 2023
Cited by 6 | Viewed by 1892
Abstract
To investigate the impact of frozen storage conditions on the physicochemical properties of soybean protein and explore the underlying mechanisms, this study focused on soybean isolate (SPI), ß-soybean companion globulin (7S), and soybean globulin (11S). The protein solutions were prepared at a concentration [...] Read more.
To investigate the impact of frozen storage conditions on the physicochemical properties of soybean protein and explore the underlying mechanisms, this study focused on soybean isolate (SPI), ß-soybean companion globulin (7S), and soybean globulin (11S). The protein solutions were prepared at a concentration of 2% and subjected to freezing for 1 and 5 days. Subsequently, the protein content, physicochemical properties, secondary structure, sulfhydryl content, and chemical interaction forces were assessed and analyzed using UV spectrophotometry, Zeta potential measurements, SDS-PAGE, Fourier infrared spectroscopy, and endogenous fluorescence photoemission spectroscopy. The obtained results revealed that the solubility and total sulfhydryl content of SPI, 7S, and 11S exhibited a decreasing trend with prolonged freezing time. Among them, 11S demonstrated the largest decrease in solubility and total sulfhydryl content, followed by SPI, and 7S the least. During freezing, the aromatic amino acids of SPI, 7S, and 11S molecules were exposed, leading to increased hydrophobicity, protein aggregation, and particle size enlargement, and the structure of the protein changed from disordered structure to ordered structure. After freezing, the polarity of the microenvironment of SPI, 7S, and 11S increased, and their maximum fluorescence emission wavelengths were red-shifted. Notably, the largest red shift of SPI was from 332 nm to 335 nm. As freezing time increased, the contribution of hydrogen bonding increased, while the contribution of hydrophobic interactions decreased. This indicates that freezing affects the hydrophobic interactions, hydrogen bonding, and other chemical forces of the protein. The growth of ice crystals leads to the unfolding of protein molecular chains, exposure of internal hydrophobic groups, enhancement of hydrophobicity, and alters the secondary structure of the protein. Full article
(This article belongs to the Special Issue Effects of Processing and Treatment on Protein Structure and Function)
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20 pages, 8608 KiB  
Article
Study on the Structure, Function, and Interface Characteristics of Soybean Protein Isolate by Industrial Phosphorylation
by Yanan Guo, Caihua Liu, Yitong Ma, Lulu Shen, Qi Gong, Zhaodong Hu, Zhongjiang Wang, Xin Liu, Zengwang Guo and Linyi Zhou
Foods 2023, 12(5), 1108; https://doi.org/10.3390/foods12051108 - 5 Mar 2023
Cited by 6 | Viewed by 2183
Abstract
The impacts of industrial phosphorylation on the structural changes, microstructure, functional, and rheological features of soybean protein isolate (SPI) were spotlighted. The findings implied that the spatial structure and functional features of the SPI changed significantly after treatment with the two phosphates. Sodium [...] Read more.
The impacts of industrial phosphorylation on the structural changes, microstructure, functional, and rheological features of soybean protein isolate (SPI) were spotlighted. The findings implied that the spatial structure and functional features of the SPI changed significantly after treatment with the two phosphates. Sodium hexametaphosphate (SHMP) promoted aggregation of SPI with a larger particle size; sodium tripolyphosphate (STP) modified SPI with smaller particle size. SDS–polyacrylamide gel electrophoresis (SDS-PAGE) results showed insignificant alterations in the structure of SPI subunits. Fourier transform infrared (FTIR) and endogenous fluorescence noted a decline in α-helix quantity, an amplification in β-fold quantity, and an increase in protein stretching and disorder, indicating that phosphorylation treatment fluctuated the spatial structure of the SPI. Functional characterization studies showed that the solubility and emulsion properties of the SPI increased to varying degrees after phosphorylation, with a maximum solubility of 94.64% for SHMP-SPI and 97.09% for STP-SPI. Emulsifying activity index (EAI) and emulsifying steadiness index (ESI) results for STP-SPI were better than those for SHMP-SPI. Rheological results showed that the modulus of G’ and G″ increased and the emulsion exhibited significant elastic behavior. This affords a theoretical core for expanding the industrial production applications of soybean isolates in the food and various industries. Full article
(This article belongs to the Special Issue Effects of Processing and Treatment on Protein Structure and Function)
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Review

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25 pages, 2730 KiB  
Review
Protein-Stabilized Emulsion Gels with Improved Emulsifying and Gelling Properties for the Delivery of Bioactive Ingredients: A Review
by Yuan Xu, Liping Sun, Yongliang Zhuang, Ying Gu, Guiguang Cheng, Xuejing Fan, Yangyue Ding and Haotian Liu
Foods 2023, 12(14), 2703; https://doi.org/10.3390/foods12142703 - 14 Jul 2023
Cited by 4 | Viewed by 3670
Abstract
In today’s food industry, the potential of bioactive compounds in preventing many chronic diseases has garnered significant attention. Many delivery systems have been developed to encapsulate these unstable bioactive compounds. Emulsion gels, as colloidal soft-solid materials, with their unique three-dimensional network structure and [...] Read more.
In today’s food industry, the potential of bioactive compounds in preventing many chronic diseases has garnered significant attention. Many delivery systems have been developed to encapsulate these unstable bioactive compounds. Emulsion gels, as colloidal soft-solid materials, with their unique three-dimensional network structure and strong mechanical properties, are believed to provide excellent protection for bioactive substances. In the context of constructing carriers for bioactive materials, proteins are frequently employed as emulsifiers or gelling agents in emulsions or protein gels. However, in emulsion gels, when protein is used as an emulsifier to stabilize the oil/water interface, the gelling properties of proteins can also have a great influence on the functionality of the emulsion gels. Therefore, this paper aims to focus on the role of proteins’ emulsifying and gelling properties in emulsion gels, providing a comprehensive review of the formation and modification of protein-based emulsion gels to build high-quality emulsion gel systems, thereby improving the stability and bioavailability of embedded bioactive substances. Full article
(This article belongs to the Special Issue Effects of Processing and Treatment on Protein Structure and Function)
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