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Frontier Analysis in the Emulsifying and Foaming Properties of Food...
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Frontier Analysis in the Emulsifying and Foaming Properties of Food Protein

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 (30 April 2023) | Viewed by 6775

Special Issue Editors

Dr. Zhongjiang Wang

E-Mail Website
Guest Editor
College of Food Science, Northeast Agricultural University, Harbin 150030, China
Interests: vegetable protein; structural characterization; emulsifying activity; interfacial activity; gel property; physical field regulation
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Hui Zhang

E-Mail Website
Guest Editor
College of Biosystems Engineering and Food Science, Zhejiang University, Hangzhou 310058, China
Interests: food oil; food protein; packaging material for food; functional health product development
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The functional characteristics of protein in food affect the processing characteristics, edible quality, nutritional value and application fields of products. Emulsifying and foaming are important functional properties of proteins. The functional properties of proteins are closely related to their uses in food systems; however, in the food production and processing, the application and development of protein functional characteristics are affected by many factors. Therefore, it is necessary to study the external factors that affect the emulsifying and foaming properties of food protein, such as temperature, pH, physical field regulation, biological enzymatic modification and the use of food additives. This can provide a research basis for seeking proteins with good specific functional types or multiple functional characteristics and provide a theoretical basis for the specific application of proteins in food industry.

Prof. Dr. Zhongjiang Wang
Prof. Dr. Hui Zhang
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

  • vegetable protein
  • animal protein
  • emulsifying properties
  • foaming properties
  • modified technique
  • promotion of function
  • application evaluation

Published Papers (4 papers)

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Research

24 pages, 4169 KiB  
Article
Impacts of Industrial Modification on the Structure and Gel Features of Soy Protein Isolate and its Composite Gel with Myofibrillar Protein
by Zhaodong Hu, Yichang Wang, Zihan Ma, Tianfu Cheng, Zengwang Guo, Linyi Zhou and Zhongjiang Wang
Foods 2023, 12(10), 1982; https://doi.org/10.3390/foods12101982 - 13 May 2023
Cited by 2 | Viewed by 1452
Abstract
Native soy protein isolate (N-SPI) has a low denaturation point and low solubility, limiting its industrial application. The influence of different industrial modification methods (heat (H), alkaline (A), glycosylation (G), and oxidation (O)) on the structure of SPI, the properties of the gel, [...] Read more.
Native soy protein isolate (N-SPI) has a low denaturation point and low solubility, limiting its industrial application. The influence of different industrial modification methods (heat (H), alkaline (A), glycosylation (G), and oxidation (O)) on the structure of SPI, the properties of the gel, and the gel properties of soy protein isolate (SPI) in myofibril protein (MP) was evaluated. The study found that four industrial modifications did not influence the subunit composition of SPI. However, the four industrial modifications altered SPI’s secondary structure and disulfide bond conformation content. A-SPI exhibits the highest surface hydrophobicity and I850/830 ratio but the lowest thermal stability. G-SPI exhibits the highest disulfide bond content and the best gel properties. Compared with MP gel, the addition of H-SPI, A-SPI, G-SPI, and O-SPI components significantly improved the properties of the gel. Additionally, MP-ASPI gel exhibits the best properties and microstructure. Overall, the four industrial modification effects may impact SPI’s structure and gel properties in different ways. A-SPI could be a potential functionality-enhanced soy protein ingredient in comminuted meat products. The present study results will provide a theoretical basis for the industrialized production of SPI. Full article
(This article belongs to the Special Issue Frontier Analysis in the Emulsifying and Foaming Properties of Food Protein)
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17 pages, 5241 KiB  
Article
Co-Extraction of Flaxseed Protein and Polysaccharide with a High Emulsifying and Foaming Property: Enrichment through the Sequence Extraction Approach
by Kang-Yu Li, Jie-Ting Ye, Jing Yang, Jia-Qi Shao, Wei-Ping Jin, Chang Zheng, Chu-Yun Wan, Deng-Feng Peng and Qian-Chun Deng
Foods 2023, 12(6), 1256; https://doi.org/10.3390/foods12061256 - 16 Mar 2023
Cited by 2 | Viewed by 1439
Abstract
A new focus with respect to the extraction of plant protein is that ingredient enrichment should target functionality instead of pursuing purity. Herein, the sequence aqueous extraction method was used to co-enrich five protein-polysaccharide natural fractions from flaxseed meal, and their composition, structure, [...] Read more.
A new focus with respect to the extraction of plant protein is that ingredient enrichment should target functionality instead of pursuing purity. Herein, the sequence aqueous extraction method was used to co-enrich five protein-polysaccharide natural fractions from flaxseed meal, and their composition, structure, and functional properties were investigated. The total recovery rate of flaxseed protein obtained by the sequence extraction approach was more than 80%, which was far higher than the existing reports. The defatted flaxseed meal was soaked by deionized water to obtain fraction 1 (supernatant), and the residue was further treated to get fraction 2 (supernatant) and 3 (precipitate) through weak alkali solubilization. Part of the fraction 2 was taken out, followed by adjusting its pH to 4.2. After centrifuging, the albumin-rich supernatant and precipitate with protein content of 73.05% were gained and labeled as fraction 4 and fraction 5. The solubility of fraction 2 and 4 exceeded 90%, and the foaming ability and stability of fraction 5 were 12.76 times and 9.89 times higher than commercial flaxseed protein, respectively. The emulsifying properties of fractions 1, 2, and 5 were all greater than that of commercial sodium caseinate, implying that these fractions could be utilized as high-efficiency emulsifiers. Cryo-SEM results showed that polysaccharides in fractions were beneficial to the formation of network structure and induced the formation of tighter and smoother interfacial layers, which could prevent emulsion flocculation, disproportionation, and coalescence. This study provides a reference to promote the high-value utilization of flaxseed meals. Full article
(This article belongs to the Special Issue Frontier Analysis in the Emulsifying and Foaming Properties of Food Protein)
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17 pages, 14164 KiB  
Article
Effects of Glucose and Homogenization Treatment on the Quality of Liquid Whole Eggs
by Wei Hu, Yong Wu, Hongbing Chen, Jinyan Gao and Ping Tong
Foods 2022, 11(16), 2521; https://doi.org/10.3390/foods11162521 - 20 Aug 2022
Cited by 1 | Viewed by 1659
Abstract
To investigate the effect of glucose on the protein structure, physicochemical and processing properties of liquid whole eggs (LWE) under homogenization, different concentrations of glucose (0.01, 0.02, 0.04, 0.08 g/mL) were added into LWE, followed by homogenizing at different pressures (5, 10, 20, [...] Read more.
To investigate the effect of glucose on the protein structure, physicochemical and processing properties of liquid whole eggs (LWE) under homogenization, different concentrations of glucose (0.01, 0.02, 0.04, 0.08 g/mL) were added into LWE, followed by homogenizing at different pressures (5, 10, 20, 40 MPa), respectively. It was shown that the particle size and turbidity of LWE increased with the increase in glucose concentration while decreasing with the increase in homogenization pressure. The protein unfolding was increased at a low concentration of glucose combined with homogenization, indicating a 40.33 ± 5.57% and 165.72 ± 33.57% increase in the fluorescence intensity and surface hydrophobicity under the condition of 0.02 g/mL glucose at 20 MPa, respectively. Moreover, the remarkable increments in foaming capacity, emulsifying capacity, and gel hardness of 47.57 ± 5.1%, 66.79 ± 9.55%, and 52.11 ± 9.83% were recorded under the condition of 0.02 g/mL glucose at 20 MPa, 0.04 g/mL glucose at 20 MPa, and 0.02 g/mL glucose at 40 MPa, respectively. Reasonably, glucose could improve the processing properties of LWE under homogenization, and 0.02 g/mL–0.04 g/mL and 20–40 MPa were the optimal glucose concentration and homogenization pressure. This study could contribute to the production of high-performance and stable quality of LWE. Full article
(This article belongs to the Special Issue Frontier Analysis in the Emulsifying and Foaming Properties of Food Protein)
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14 pages, 3597 KiB  
Article
Maximizing Recovery of Paenibacillin, a Bacterially Produced Lantibiotic, Using Continuous Foam Separation from Bioreactors
by Emily P. Campbell, David R. Kasler and Ahmed E. Yousef
Foods 2022, 11(15), 2290; https://doi.org/10.3390/foods11152290 - 31 Jul 2022
Viewed by 1603
Abstract
Industrial production of paenibacillin, and similar rare antimicrobial peptides, is hampered by low productivity of the producing microorganisms and lack of efficient methods to recover these peptides from fermentor or bioreactor end products. Preliminary data showed that paenibacillin was preferentially partitioned in foam [...] Read more.
Industrial production of paenibacillin, and similar rare antimicrobial peptides, is hampered by low productivity of the producing microorganisms and lack of efficient methods to recover these peptides from fermentor or bioreactor end products. Preliminary data showed that paenibacillin was preferentially partitioned in foam accumulated during growth of the producer, Paenibacillus polymyxa, in aerated liquid media. This research was initiated to improve the production and recovery of paenibacillin in bioreactors by maximizing partitioning of this antimicrobial agent in the collected foam. This was completed through harvesting foam continuously during paenibacillin production, using modified bioreactor, and optimizing bioreaction conditions through response surface methodology (RSM). During initial screening, the following factors were tested using 400 mL inoculated media in 2 L bioreactors: medium (tryptic soy broth, TSB, with or without added yeast extract), airflow (0 or 0.8 L/min; LPM), stir speed (300 or 500 revolution/min; RPM), incubation temperature (30 or 36 °C), and incubation time (16 or 24 h). Results showed that airflow, time, and stir speed had significant effects (p < 0.05) on paenibacillin recovery in the collected collapsed foam (foamate). These factors were varied together to follow the path of steepest assent to maximize paenibacillin concentration. Once the local maximum was found, RSM was completed with a central composite design to fine-tune the bioreaction parameters. The optimization experiments proved that the significant parameters and their optimal conditions for paenibacillin concentration in the foam were: incubation at 30 °C for 23 h with airflow of 0.95 LPM, and agitation speed of 450 RPM. These conditions increased paenibacillin concentration, predicted by RSM, from 16 µg/mL in bioreaction without foam collection to 743 µg/mL collected in foamate. The optimized conditions also almost doubled the yield of paenibacillin measured in the foam collected from a bioreaction run (12,674 µg/400 mL bioreaction) when compared to that obtained from a run without foam collection (6400 µg/400 mL bioreaction). Results of this study could improve the feasibility of commercial production and downstream processing of paenibacillin and similar novel antimicrobial peptides. Availability of such peptides will eventually help in protecting perishable products against pathogenic and spoilage bacteria. Full article
(This article belongs to the Special Issue Frontier Analysis in the Emulsifying and Foaming Properties of Food Protein)
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