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Advanced Technology to Improve Food Protein Functionality
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Advanced Technology to Improve Food Protein Functionality

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

Deadline for manuscript submissions: closed (25 October 2023) | Viewed by 12722

Special Issue Editors

Dr. Manat Chaijan

E-Mail Website
Guest Editor
Food Technology and Innovation Research Center of Excellence, School of Agricultural Technology and Food Industry, Walailak University, Nakhon Si Thammarat 80160, Thailand
Interests: seafood proteins; surimi chemistry; protein functionality; gelation
Dr. Worawan Panpipat

E-Mail Website
Guest Editor
Food Technology and Innovation Research Center of Excellence, School of Agricultural Technology and Food Industry, Walailak University, Nakhon Si Thammarat 80160, Thailand
Interests: protein functionality; alternative proteins; protein–lipid interaction; emulsion; bioactive peptides

Special Issue Information

Dear Colleagues,

This Special Issue focuses on protein structure, protein denaturation, the inter-relationship between the structure and functional properties of protein, protein modification, and processing-induced physical, chemical, and nutritional changes in proteins. The characteristics and applications of several food proteins, including those found in meat, seafood, egg whites, soy products, plants, milk, insects, and others, are covered. Methods for the extraction, purification, and characterization of some intriguing proteins are also encouraged, as is the advancement of cutting-edge technology to enhance the functionality of food proteins.

This Special Issue also discusses the significance of protein modification in the functional properties of foods, estimation analytical methods for the structure and functional features of proteins, and the impact of various process parameters on the molecular structures in food proteins. Using state-of-the-art technology, functional protein components are produced, and their quality, safety, and assessment of biological activities as well as biochemical mechanisms are all covered. The use of functional food protein components in food products and knowledge of functional food protein claims to control human consumption are also encouraged.

Dr. Manat Chaijan
Dr. Worawan Panpipat
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
  • techno-functionality
  • thermal processing
  • non-thermal processing
  • green extraction
  • protein purification
  • storage stability
  • solubility
  • interfacial property
  • emulsion
  • gelation
  • foam
  • film
  • flavor binding
  • dough formation
  • meat proteins
  • egg proteins
  • insect proteins
  • plant proteins
  • seafood proteins
  • alternative proteins
  • protein–lipid interaction
  • protein–polysaccharide interaction
  • protein modification
  • maillard reactions
  • enzymatic hydrolysis
  • protein hydrolysate
  • collagen
  • gelatin
  • surimi
  • protein-based coating
  • analytical methods for food proteins
  • emerging technology for food proteins
  • proteomics
  • functional food proteins’ ingredients
  • bioactive peptides

Published Papers (6 papers)

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Research

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15 pages, 5004 KiB  
Article
Enhancing Solubility and Reducing Thermal Aggregation in Pea Proteins through Protein Glutaminase-Mediated Deamidation
by Lijuan Luo, Yuanyuan Deng, Guang Liu, Pengfei Zhou, Zhihao Zhao, Ping Li and Mingwei Zhang
Foods 2023, 12(22), 4130; https://doi.org/10.3390/foods12224130 - 15 Nov 2023
Cited by 1 | Viewed by 1326
Abstract
The limited solubility and stability of pea proteins hinder their utilization in liquid formulations. In this study, protein glutaminase (PG) was employed to modify pea protein isolates (PPIs) and obtain deamidated PPI with varying degrees of deamidation (DD, 10–25%). The solubility and thermal [...] Read more.
The limited solubility and stability of pea proteins hinder their utilization in liquid formulations. In this study, protein glutaminase (PG) was employed to modify pea protein isolates (PPIs) and obtain deamidated PPI with varying degrees of deamidation (DD, 10–25%). The solubility and thermal stability of these deamidated PPI samples were assessed, and a comprehensive analysis, including SDS-PAGE, zeta potential, FTIR, surface hydrophobicity, and intrinsic fluorescence, was conducted to elucidate the mechanism behind the improvement in their functional properties. The results reveal that PG modification greatly enhances the solubility and heat stability of PPI, with the most notable improvements observed at higher DD (>20%). PG modification increases the net charge of PPI, leading to the unfolding and extension of the protein structures, thus exposing more hydrophobic groups. These structural changes are particularly pronounced when DD exceeds 20%. This increased electrostatic repulsion between carboxyl groups would promote protein unfolding, enhancing interactions with water and hindering the aggregation of unfolded protein in the presence of salts at elevated temperatures (supported by high-performance size exclusion chromatography and transmission electron microscopy). Accordingly, PG-mediated deamidation shows promise in enhancing the functional properties of PPI. Full article
(This article belongs to the Special Issue Advanced Technology to Improve Food Protein Functionality)
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14 pages, 516 KiB  
Article
Cricket Protein Isolate Extraction: Effect of Ammonium Sulfate on Physicochemical and Functional Properties of Proteins
by Edward, Thanakorn Wongprasert, Thasorn Bunyakanchana, Panattida Siripitakpong, Kotchakorn Supabowornsathit, Tirayut Vilaivan and Inthawoot Suppavorasatit
Foods 2023, 12(21), 4032; https://doi.org/10.3390/foods12214032 - 5 Nov 2023
Cited by 1 | Viewed by 2404
Abstract
Crickets are known to be a promising alternative protein source. However, a negative consumer bias and an off-flavor have become obstacles to the use of these insects in the food industry. In this study, we extracted the protein from commercial cricket powder by [...] Read more.
Crickets are known to be a promising alternative protein source. However, a negative consumer bias and an off-flavor have become obstacles to the use of these insects in the food industry. In this study, we extracted the protein from commercial cricket powder by employing alkaline extraction–acid precipitation and including ammonium sulfate. The physicochemical and functional properties of the proteins were determined. It was found that, upon including 60% ammonium sulfate, the cricket protein isolate (CPI) had the highest protein content (~94%, w/w). The circular dichroism results indicated that a higher amount of ammonium sulfate drastically changed the secondary structure of the CPI by decreasing its α-helix content and enhancing its surface hydrophobicity. The lowest solubility of CPI was observed at pH 5. The CPI also showed better foaming properties and oil-holding capacity (OHC) compared with the cricket powder. In conclusion, adding ammonium sulfate affected the physicochemical and functional properties of the CPI, allowing it to be used as an alternative protein in protein-enriched foods and beverages. Full article
(This article belongs to the Special Issue Advanced Technology to Improve Food Protein Functionality)
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14 pages, 2030 KiB  
Article
Expression and Transformation Characteristics of a Novel Glutamic Acid Decarboxylase LcGAD10s and Its Application on Sufu Processing
by Zhou Chen, Run Wang, Yanyin Song, Aijin Ma, Siting Li and Yingmin Jia
Foods 2023, 12(17), 3186; https://doi.org/10.3390/foods12173186 - 24 Aug 2023
Viewed by 1108
Abstract
Gamma-aminobutyric acid (GABA) is an important non-proteinogenic amino acid and a potent bioactive compound with many anti-hypertensive and anti-depressant activities. The bioconversion of GABA by glutamic acid decarboxylase (GAD) has been eagerly studied. Herein, novel pyridoxal-5-phosphate monohydrates (PLP)-dependent GAD, which is not quite [...] Read more.
Gamma-aminobutyric acid (GABA) is an important non-proteinogenic amino acid and a potent bioactive compound with many anti-hypertensive and anti-depressant activities. The bioconversion of GABA by glutamic acid decarboxylase (GAD) has been eagerly studied. Herein, novel pyridoxal-5-phosphate monohydrates (PLP)-dependent GAD, which is not quite similar to reporting, was cloned from Latilactobacillus curvatus and efficiently expressed in E. coli. The conveniently purified GAD (designated LcGAD10s) appeared as a single protein on SDS-PAGE with a molecular mass of 52.0 kDa. LcGAD10s exhibited a specific activity of 303.7 U/mg after purification by Ni–IDA affinity chromatography, with optimal activity at 55 °C and pH 5. LcGAD10s displayed excellent temperature (50 °C) and pH (4–8) stability which relative activity above 80% and 70%, respectively. The enzymatic activity was, respectively, increased and depressed by 130%, and 24% in the presence of Mn+ and Cu2+. Enzyme activity over 90% can be achieved by adding at least 25 mM of PLP. LcGAD10s was able to efficiently transform 15 g/L GABA with a single-factor optimized reaction of pH (5), temperature (50 °C), time (2 h), LcGAD10s dosage (0.4 U) and monosodium glutamate level (5 g/L). Additionally, LcGAD10s can be applied to a tofu fermentation system to achieve GABA conversion and achieved 14.9 mg/g of GABA conversion when added at 2 U/mL, which is higher than most of the commercial sufu and previous application reports, increasing its functional substances. Full article
(This article belongs to the Special Issue Advanced Technology to Improve Food Protein Functionality)
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18 pages, 5052 KiB  
Article
Impact of Washing with Antioxidant-Infused Soda–Saline Solution on Gel Functionality of Mackerel (Auxis thazard) Surimi
by Porntip Thongkam, Manat Chaijan, Ling-Zhi Cheong and Worawan Panpipat
Foods 2023, 12(17), 3178; https://doi.org/10.3390/foods12173178 - 24 Aug 2023
Cited by 6 | Viewed by 1657
Abstract
Mackerel (Auxis thazard), a tropical dark-fleshed fish, has the potential to be used in the production of surimi. It is necessary to identify the optimal washing method to make better use of this species since efficient washing is the most important [...] Read more.
Mackerel (Auxis thazard), a tropical dark-fleshed fish, has the potential to be used in the production of surimi. It is necessary to identify the optimal washing method to make better use of this species since efficient washing is the most important step in surimi processing to ensure maximal gelling and high-quality surimi. The purpose of this study was to evaluate the combined effect of cold carbonated water (CW) with NaCl and antioxidants in washing media, so-called antioxidant-infused soda–saline solution, on lipid and myoglobin removal efficacy, biochemical characteristics, gelling properties, sensory features, and the oxidative stability of mackerel surimi in comparison with unwashed mince (T1) and conventional water washed surimi (T2). Mackerel mince was washed with CW in the presence of 0.6% NaCl at a medium to mince ratio of 3:1 (v/w) without antioxidant (T3) or with the addition of 1.5 mM EDTA plus 0.2% (w/v) sodium erythorbate and 0.2% sodium tripolyphosphate (T4), 100 mg/L gallic acid (T5), and 5 mM citric acid containing 8 mM calcium chloride (T6). During the first washing cycle, the antioxidants were mixed into the washing medium. The second and third washing cycles were then completed with cold water. The yields of all treatments were roughly 75–83%, based on the gross weight of the raw mince. The pH of the surimi was in a range of 5.47–6.46. All of the surimi had higher reactive sulfhydryl (SH) content and surface hydrophobicity but lower Ca2+-ATPase activity than unwashed mince (p < 0.05). After washing, lipids decreased significantly (p < 0.05), accounted for a 65–76% reduction. The T2 surimi had the highest peroxide value (PV). T1 had the lowest conjugated diene value. T1 and T4 surimi had the lowest TBARS value (p < 0.05). A lower non-heme iron level was found in all antioxidant-treated samples than in T1. Washing can increase the redox stability of myoglobin regardless of the washing media, as seen by the relatively low metmyoglobin levels. According to the dynamic viscoelastic behavior, all surimi and unwashed mince underwent the same degree of sol–gel transition following heat gelation. T1 showed the lowest breaking force, deformation, gel strength, and whiteness (p < 0.05). Surimi made from T4 or T5 had the highest gel strength when both breaking and deformation were considered, but the latter’s expressible drip was noticeably higher. Surimi gel appears to be stabilized against lipid oxidation, as demonstrated by low PV and TBARS levels, when produced with T4. Because of the low level of TBARS, all 10 panelists rated rancid odor as low (~1 out of 4), with no significant variations across treatments. Only treatments with T4 and T6 tended to have a lower fishy odor score as compared to unwashed mince. Scanning electron microscope demonstrated that surimi gels washed with all washing media exhibited microstructures that were very comparable, with the exception of the T6 treatment, which had big pores and aggregates. Based on the quality features, T4 appeared to be the optimal medium to enhance the gel functionality of mackerel surimi. Full article
(This article belongs to the Special Issue Advanced Technology to Improve Food Protein Functionality)
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13 pages, 1517 KiB  
Article
Whey Protein–Tannic Acid Conjugate Stabilized Emulsion-Type Pork Sausages: A Focus on Lipid Oxidation and Physicochemical Features
by Tanong Aewsiri, Palanivel Ganesan and Hataikan Thongzai
Foods 2023, 12(14), 2766; https://doi.org/10.3390/foods12142766 - 20 Jul 2023
Viewed by 1411
Abstract
The purpose of this study was to investigate the oxidative stability and physicochemical properties of pork emulsion sausages with whey protein–tannic acid conjugate and native whey protein. Over the course of 21 days, the thiobarbituric acid reactive substances (TBARS) of sausages containing a [...] Read more.
The purpose of this study was to investigate the oxidative stability and physicochemical properties of pork emulsion sausages with whey protein–tannic acid conjugate and native whey protein. Over the course of 21 days, the thiobarbituric acid reactive substances (TBARS) of sausages containing a whey protein–tannic acid conjugate were lower than those of sausages with regular whey protein (p < 0.05). Kinetically, sausage containing the whey protein–tannic acid conjugate (k = 0.0242 day−1) appeared to last longer than sausage containing regular whey protein (k = 0.0667 day−1). The addition of the whey protein–tannic acid conjugate had no effect on product texture because there was no difference in hardness, springiness, cohesiveness, or water-holding capacity between the control and treated samples at Day 0 (p > 0.05). Scanning electron microscopy revealed that, at Day 21, the control sausage exhibited emulsion coalescence, as evidenced by an increase in the number of oil droplets and large voids, but not the whey protein–tannic acid conjugate-added sausage. There was no variation in the L*, a*, and b* values of the sausages when the whey protein–tannic acid conjugate was added (p > 0.05). However, there was a little increase in ΔE value in the treated sample. Thus, the whey-protein–tannic acid conjugate appeared to stabilize the lipid and physicochemical properties of the sausages by lowering the rate of TBARS production, retaining texture, water-holding capacity, and color, as well as by minimizing lipid coalescence during refrigerated storage. Full article
(This article belongs to the Special Issue Advanced Technology to Improve Food Protein Functionality)
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Review

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34 pages, 1609 KiB  
Review
Yellow Field Pea Protein (Pisum sativum L.): Extraction Technologies, Functionalities, and Applications
by Nancy D. Asen, Rotimi E. Aluko, Alex Martynenko, Alphonsus Utioh and Pankaj Bhowmik
Foods 2023, 12(21), 3978; https://doi.org/10.3390/foods12213978 - 30 Oct 2023
Cited by 4 | Viewed by 3917
Abstract
Yellow field peas (Pisum sativum L.) hold significant value for producers, researchers, and ingredient manufacturers due to their wealthy composition of protein, starch, and micronutrients. The protein quality in peas is influenced by both intrinsic factors like amino acid composition and spatial conformations [...] Read more.
Yellow field peas (Pisum sativum L.) hold significant value for producers, researchers, and ingredient manufacturers due to their wealthy composition of protein, starch, and micronutrients. The protein quality in peas is influenced by both intrinsic factors like amino acid composition and spatial conformations and extrinsic factors including growth and processing conditions. The existing literature substantiates that the structural modulation and optimization of functional, organoleptic, and nutritional attributes of pea proteins can be obtained through a combination of chemical, physical, and enzymatic approaches, resulting in superior protein ingredients. This review underscores recent methodologies in pea protein extraction aimed at enhancing yield and functionality for diverse food systems and also delineates existing research gaps related to mitigating off-flavor issues in pea proteins. A comprehensive examination of conventional dry and wet methods is provided, in conjunction with environmentally friendly approaches like ultrafiltration and enzyme-assisted techniques. Additionally, the innovative application of hydrodynamic cavitation technology in protein extraction is explored, focusing on its prospective role in flavor amelioration. This overview offers a nuanced understanding of the advancements in pea protein extraction methods, catering to the interests of varied stakeholders in the field. Full article
(This article belongs to the Special Issue Advanced Technology to Improve Food Protein Functionality)
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