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Food Proteins: Structural, Physicochemical, Functional and Nutritional Properties
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Food Proteins: Structural, Physicochemical, Functional and Nutritional Properties

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 May 2024) | Viewed by 10998

Special Issue Editors

Dr. Zhaojun Zheng

E-Mail Website
Guest Editor
School of Food Science and Technology, Jiangnan University, Wuxi, China
Interests: food proteins and peptides; bioactive compounds; antioxidants; protein modification; functional and structural properties
Dr. Luping Gu

E-Mail Website
Guest Editor
School of Food Science and Technology, Jiangnan University, Wuxi, China
Interests: food proteins; food colloid; protein modification; physicochemical properties; delivery system

Special Issue Information

Dear Colleagues,

Food proteins are essential macronutrients for human health, and thus, make significant contributions to the unique functions of different foods. The nutritional and functional properties of food protein ingredients depend on their source, extraction, modification during food manufacture and interactions with other food components. Physical, chemical and biological treatments for the modification of proteins are considered as being among the major emerging and promising technologies for improving the functional and nutritional properties of food products. However, protein modification is a complex task, which produces extensive effects on the digestibility, nutritional compositions and conformational structures of proteins. Recent advances that refer to the specific changes occurring within proteins are currently under study. Therefore, we are highly interested in and encourage manuscripts related to the efficient and innovative modification methods on protein structures and physicochemical properties, the exploitation of proteins with functional and nutritional properties, the structural–functional relationship, as well as the exploration of protein resources.

Dr. Zhaojun Zheng
Dr. Luping Gu
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

  • food proteins 
  • structure 
  • physicochemical properties 
  • functionality 
  • nutritional properties 
  • food processing 
  • protein modification 
  • digestive profile

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Published Papers (6 papers)

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Research

18 pages, 4179 KiB  
Article
Hydroxyl Radical-Induced Oxidation on the Properties of Cathepsin H and Its Influence in Myofibrillar Proteins Degradation of Coregonus peled In Vitro
by Xuemei Fan, Mengjie Ma, Pingping Liu, Xiaorong Deng and Jian Zhang
Foods 2024, 13(16), 2531; https://doi.org/10.3390/foods13162531 - 14 Aug 2024
Viewed by 785
Abstract
The most frequently occurring protein modification in fish postmortem is oxidization, which further affects meat quality through multiple biochemical pathways. To investigate how hydroxyl radicals affect the structure of cathepsin H and its ability to break down myofibrillar proteins in Coregonus peled, [...] Read more.
The most frequently occurring protein modification in fish postmortem is oxidization, which further affects meat quality through multiple biochemical pathways. To investigate how hydroxyl radicals affect the structure of cathepsin H and its ability to break down myofibrillar proteins in Coregonus peled, cathepsin H was oxidized with 0, 0.1, 0.5, 1, 5, and 10 mM H2O2 and subsequently incubated with isolated myofibrillar proteins. The results showed that as the H2O2 concentration increased, the carbonyl and sulfhydryl contents of cathepsin H significantly increased and decreased, respectively. There were noticeable changes in the α-helix structures and a gradual reduction in UV absorbance and fluorescence intensity, indicating that oxidation can induce the cross-linking and aggregation of cathepsin H. These structural changes further reduced the activity of cathepsin H, reaching its lowest at 10 mM H2O2, which was 53.63% of the activity at 0 mM H2O2. Moreover, desmin and troponin-T all degraded at faster rates when cathepsin H and myofibrillar proteins were oxidized concurrently as opposed to when cathepsin H was oxidized alone. These findings provide vital insights into the interaction mechanism between oxidation, cathepsin H, as well as myofibrillar protein degradation, laying a groundwork for understanding the molecular mechanisms underlying changes in fish meat quality after slaughter and during processing. Full article
(This article belongs to the Special Issue Food Proteins: Structural, Physicochemical, Functional and Nutritional Properties)
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23 pages, 8668 KiB  
Article
The Effect of Nanoscale Modification of Nisin by Different Milk-Derived Proteins on Its Physicochemical Properties and Antibacterial Activity
by Jing Wang, Rui Liu, Xiaoyang Huang, Yuexin Bao, Xiaohong Wang, Huaxi Yi and Youyou Lu
Foods 2024, 13(11), 1606; https://doi.org/10.3390/foods13111606 - 22 May 2024
Viewed by 1486
Abstract
Nisin is used as a natural food preservative because of its broad-spectrum antimicrobial activity against Gram-positive bacteria. However, free nisin is susceptible to various factors that reduce its antimicrobial activity. Milk protein, a protein derived from milk, has self-assembly properties and is a [...] Read more.
Nisin is used as a natural food preservative because of its broad-spectrum antimicrobial activity against Gram-positive bacteria. However, free nisin is susceptible to various factors that reduce its antimicrobial activity. Milk protein, a protein derived from milk, has self-assembly properties and is a good carrier of bioactive substances. In this study, lactoferrin–nisin nanoparticles (L-N), bovine serum albumin–nisin nanoparticles (B-N), and casein–nisin nanoparticles (C-N) were successfully prepared by a self-assembly technique, and then their properties were investigated. The studies revealed that lactoferrin (LF) and nisin formed L-N mainly through hydrophobic interactions and hydrogen bonding, and L-N had the best performance. The small particle size (29.83 ± 2.42 nm), dense reticular structure, and good thermal stability, storage stability, and emulsification of L-N laid a certain foundation for its application in food. Further bacteriostatic studies showed that L-N enhanced the bacteriostatic activity of nisin, with prominent inhibitory properties against Listeria monocytogenes, Staphylococcus aureus, and Bacillus cereus, which mainly disrupted the cell membrane of the bacteria. The above results broaden our understanding of milk protein–nisin nanoparticles, while the excellent antibacterial activity of L-N makes it promising for application as a novel food preservative, which will help to improve the bioavailability of nisin in food systems. Full article
(This article belongs to the Special Issue Food Proteins: Structural, Physicochemical, Functional and Nutritional Properties)
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18 pages, 2553 KiB  
Article
Enhancing the Gelation Behavior of Transglutaminase-Induced Soy Protein Isolate(SPI) through Ultrasound-Assisted Extraction
by Gaolin Li, Ran Tao, Yufeng Sun, Lili Wang, Yurui Li, Bei Fan and Fengzhong Wang
Foods 2024, 13(5), 738; https://doi.org/10.3390/foods13050738 - 28 Feb 2024
Cited by 1 | Viewed by 1870
Abstract
Gelation, as an important functional property of soy protein isolate (SPI), can be improved by some green technologies in food manufacturing, including ultrasound, ultrahigh pressure and microwave treatments. This work investigated the effect of an alkaline solubilisation step in SPI extraction combined with [...] Read more.
Gelation, as an important functional property of soy protein isolate (SPI), can be improved by some green technologies in food manufacturing, including ultrasound, ultrahigh pressure and microwave treatments. This work investigated the effect of an alkaline solubilisation step in SPI extraction combined with sonication on protein properties. The TGase-induced gel of the modified SPI was prepared to explore the effect of ultrasound on gel properties, including structures, strength, water-holding capacity and rheological properties. Additionally, the differences between traditional ultrasound modification of SPI and current modification methods were analyzed. The results showed that the ultrasonication-assisted extraction method could result in a significant increase in extraction rate from 24.68% to 42.25%. Moreover, ultrasound-assisted modification of SPI gels induced with transglutaminase (TGase) exhibited significant improvement in mechanical properties, such as texture, water-holding capacity and rheological properties, In particular, SPI extracted at 400 W ultrasound intensity for 180 s showed the best overall performance in terms of gel properties. Our method efficiently uniformizes gel structure, enhancing mechanical properties compared to conventional ultrasound methods, which reduced energy consumption and costs. These findings provide insights into the production of high-gelation SPI in food manufacturing. Full article
(This article belongs to the Special Issue Food Proteins: Structural, Physicochemical, Functional and Nutritional Properties)
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16 pages, 3290 KiB  
Article
Emulsion-Templated Liquid Oil Structuring with Egg White Protein Microgel- Xanthan Gum
by Yujie Su, Wanqiu Zhang, Ruidan Liu, Cuihua Chang, Junhua Li, Wen Xiong, Yanjun Yang and Luping Gu
Foods 2023, 12(9), 1884; https://doi.org/10.3390/foods12091884 - 3 May 2023
Cited by 5 | Viewed by 2665
Abstract
In this study, oleogels were prepared by the emulsion-template method using egg-white protein microgel as a gelator and xanthan gum (XG) as thickener. The physicochemical properties of the emulsion and oleogels were investigated. The adsorption of protein on the surface of the oil [...] Read more.
In this study, oleogels were prepared by the emulsion-template method using egg-white protein microgel as a gelator and xanthan gum (XG) as thickener. The physicochemical properties of the emulsion and oleogels were investigated. The adsorption of protein on the surface of the oil droplet reached saturation when the protein microgel concentration reached 2%. The excess protein combined with XG and accumulated on the outer layer of the oleogel, which prevented the emulsion from flocculation, enhanced the oil-holding capacity of the oleogel, and had a positive effect on preventing the oxidation of oil. When the concentration of XG was less than 0.4%, the EWP microgel, combined with the XG, stabilized the emulsion. As the concentration of XG was greater than 0.4%, excessive XG in the emulsion improved the viscosity and mechanical properties of the emulsion to prevent the aggregation of oil droplets. However, the change in XG concentration had no significant effect on the oxidation of the oil. Full article
(This article belongs to the Special Issue Food Proteins: Structural, Physicochemical, Functional and Nutritional Properties)
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19 pages, 3029 KiB  
Article
Transglutaminase-Catalyzed Glycosylation Improved Physicochemical and Functional Properties of Lentinus edodes Protein Fraction
by Shan-shan Wu, Wei Han, Yan-fen Cheng, Shao-jun Yun, Ming-chang Chang, Fei-er Cheng, Jin-ling Cao and Cui-ping Feng
Foods 2023, 12(9), 1849; https://doi.org/10.3390/foods12091849 - 29 Apr 2023
Cited by 4 | Viewed by 1587
Abstract
Lentinula edodes has high nutritional value and abundant protein. In order to develop and utilize edible mushroom protein, this study was designed to investigate the effects of TGase-catalyzed glycosylation and cross-linking on the physicochemical and functional properties of Lentinus edodes protein fraction. The [...] Read more.
Lentinula edodes has high nutritional value and abundant protein. In order to develop and utilize edible mushroom protein, this study was designed to investigate the effects of TGase-catalyzed glycosylation and cross-linking on the physicochemical and functional properties of Lentinus edodes protein fraction. The results showed that within a certain time, glycosylation and TGase-catalyzed glycosylation decreased the total sulfydryl, free sulfydryl, disulfide bond, surface hydrophobicity, β-fold and α-helix, but increased the fluorescence intensity, random coil, β-turn, particle size and thermal stability. The apparent viscosity and the shear stress of the protein with an increase in shear rate were increased, indicating that TGase-catalyzed glycosylation promoted the generation of cross-linked polymers. In addition, the TGase-catalyzed glycosylated proteins showed a compact texture structure similar to the glycosylated proteins at the beginning, indicating that they formed a stable three-dimensional network structure. The flaky structure of proteins became more and more obvious with time. Moreover, the solubility, emulsification, stability and oil-holding capacity of enzymatic glycosylated Lentinus edodes protein fraction were significantly improved because of the proper TGase effects of glycosylation grafting and cross-linking. These results showed that glycosylation and TGase-catalyzed glycosylation could improve the processing characteristics of the Lentinula edodes protein fraction to varying degrees. Full article
(This article belongs to the Special Issue Food Proteins: Structural, Physicochemical, Functional and Nutritional Properties)
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18 pages, 3082 KiB  
Article
Structural and Functional Characteristics of Hemp Protein Isolate–Pullulan Polysaccharide Glycosylation Conjugate in an Aqueous Model System
by Ziwen Ding, Fan Jiang, Kun Liu, Fangshuo Gong, Yuanfa Liu, Zhaojun Zheng and Yong-Jiang Xu
Foods 2023, 12(7), 1416; https://doi.org/10.3390/foods12071416 - 27 Mar 2023
Cited by 5 | Viewed by 1944
Abstract
Hemp protein, with its important nutritional and industrial value, has trickled into the aisles of protein demand; however, its poor functional properties have largely limited its implementation in food. Herein, we aimed to modify hemp protein isolate (HPI) via glycosylation coupling with pullulan [...] Read more.
Hemp protein, with its important nutritional and industrial value, has trickled into the aisles of protein demand; however, its poor functional properties have largely limited its implementation in food. Herein, we aimed to modify hemp protein isolate (HPI) via glycosylation coupling with pullulan polysaccharide, and we subsequently characterized its structural and functional properties. The conjugation variables were HPI to pullulan ratio (i.e., 3:1, 2:1, 1:1, 1:2, and 1:3 w/w), incubation temperature (i.e., 50, 60, 70, 80, and 90 °C), and incubation time (i.e., 3, 6, 12, 24, and 48 h). Native HPI was used as a control for comparison purposes. We found that DG tended to decrease when the pullulan to HPI ratio was greater than 1:1 and when the temperature exceeded 80 °C. SDS-PAGE analysis shows that when the DG is increased, wider and heavier molecular weight bands emerge near the top of the running gel, while such observations were absent in the control. Further, glycosylation could loosen the HPI’s secondary and tertiary structures, as well as increase surface hydrophobicity. The solubility of HPI after glycosylation significantly increased (p < 0.05) at pH 7.0 compared to HPI without glycosylation. Emulsifying activity improved significantly (p < 0.05), with glycosylation with HPI–pullulan at a ratio of 1:3 showing maximum emulsifying activity of 118.78 ± 4.48 m2/g (HPI alone: 32.38 ± 3.65 m2/g). Moreover, the HPI–pullulan glycosylation time of 24 h showed maximum foaming activity (23.04 ± 0.95%) compared to HPI alone (14.20 ± 1.23%). The foaming stability of HPI (79.61 ± 3.33%) increased to 97.78 ± 3.85% when HPI–pullulan was conjugated using a glycosylation temperature of 80 °C. Compared with the un-glycated HPI, HPI–pullulan also increased WHC (4.41 ± 0.73 versus 9.59 ± 0.36 g/g) and OHC (8.48 ± 0.51 versus 13.73 ± 0.59 g/g). Intriguingly, correlation analysis showed that protein functional characteristics were significantly and positively correlated with DG. Overall, our findings support the notion that pullulan conjugation provides further functional attributes to the HPI, thereby broadening its potential implementation in complicated food systems. Full article
(This article belongs to the Special Issue Food Proteins: Structural, Physicochemical, Functional and Nutritional Properties)
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