Atmospheric cold plasma pretreatment for effective enhancement of covalent crosslinking between coconut globulin and tannic acid: Improving interfacial activity and emulsifying properties.

Atmospheric cold plasma (ACP) represents a promising approach for enhancing covalent interactions between proteins and polyphenols, circumventing the drawbacks associated with traditional methods. This study aims to investigate the enhancement of covalent interactions between coconut globulin (CG) and tannic acid (TA) facilitated by ACP at varying pH levels. At acidic pH, ACP treatment was found to promote free radical-induced covalent cross-linking between CG and TA, whereas at pH 7.0 and 9.0, ACP treatment enhanced quinone-induced covalent cross-linking. In contrast, the covalent crosslinking induced by quinone significantly disrupted the protein structure, leading to greater exposure of hydrophobic groups. At pH 9.0, the CG-TA complex treated with ACP exhibited the highest interfacial activity, with an interfacial adsorption mass of 5292 ng/cm2. This was accompanied by improvements in droplet size, viscosity, and stability of the CG-TA-stabilized emulsion. These findings offer novel insights into the covalent modification of proteins and polyphenols, thereby broadening the potential applications of food protein.

Fabrication and characterization of novel curcumin-loaded thermoreversible high amylose maize starch emulsion gel.

This study developed a novel thermoreversible emulsion gel system based on high amylose maize starch (HAMS) and investigated the impact of the oil-to-water ratio on its physicochemical properties and encapsulation performance (using curcumin as model guest molecule). Electron microscopy showed a tightly porous network structure of the HAMS-based emulsion gels. Thermal results revealed a sol-gel transition occurring in the range of 59.41 to 67.64 °C for the prepared emulsion gels. Rheological analysis suggested that all samples displayed shear-thinning behavior and HAMS-based emulsion gels exhibited typical gel-like behavior with the gel strength bolstered by higher aqueous phases. Particle size analysis showed that droplet size of emulsion gel decreased from 245 to 184 nm with increased starch aqueous phase content. Texture profile analysis indicated enhanced strength, hardness, and chewiness of the emulsion gel with increased aqueous phases. Curcumin encapsulation efficiency in the HAMS-based emulsion gel also improved with higher aqueous phase content, reaching up to 93.82 %, which attributed to the smaller droplets caused increased interfacial area. The novel HAMS-based emulsion gel system showed considerable encapsulation capacity and desirable mechanical properties. It provided valuable insights into the application of starch-based emulsion gels in food and medical area.

Mechanisms of Degradation of Insoluble Dietary Fiber from Coconut Chips by Ultra-High Pressure.

Coconut chips are a popular leisure food, but the residual crumbly feeling after chewing affects the eating experience. To address this problem, we investigated the mechanism of degradation of insoluble dietary fiber (IDF) from coconut chips by ultra-high pressure (UHP). The optimal conditions for UHP treatment were 100 MPa and 40 min. After UHP treatment, the hardness decreased by 60%, and the content of soluble dietary fiber (SDF) increased by 55%. So far, the meaning of SDF has not been defined. The microstructure of IDF was damaged and the surface was rough. There was no obvious change in the chemical structure. The position of the characteristic diffraction peaks was basically unchanged, but the crystallinity dropped by almost three times. The thermal stability decreased, and the composition of the monosaccharides changed. Together, UHP treatment can improve the problem of the residual crumbly feeling after chewing coconut chips and improve the quality of the product.

Shear, extensional rheology, and tribology of polysaccharide-thickened soy protein-based liquid systems for dysphagia management.

Modifying food texture is a valuable approach to enhancing the quality of life for patients with dysphagia. Incorporating thickened soy protein-based liquid systems (SPLS) into their diet not only improves protein intake but also promotes safer swallowing. However, the properties of thickened SPLS are crucial for safe swallowing, may vary depending on the conformation of the thickened polysaccharides used. In this study, SPLS with different levels of thickening were prepared using xanthan gum, pectin and guar gum. The influence of polysaccharide conformation on the rheological (shear and extensional) and tribological properties of thickened SPLS was investigated. The results revealed that xanthan gum-thickened SPLS exhibiting the highest shear viscosity (110.073 Pa.s) and extensional viscosity (7.405 Pa.s), which increased with polysaccharide concentration. Meanwhile, xanthan gum possessed the strongest lubricating properties. These results shed light on the development of plant protein-based solutions for dysphagia management.

The Hofmeister series: Anion effect on microbial transglutaminase cross-linked soybean protein isolate hydrogels.

In this paper, the possibility of the kosmotropic anion (CO32-, Citrate3-, SO42-, H2PO4-, CH3COO- and Cl-) to improve the gel properties of microbial transglutaminase (MTG)-crosslinked soybean isolate protein (SPI)-based hydrogels was explored using a soaking strategy. The results of this experiment demonstrated that the hardness of the hydrogel undergoes different degrees of enhancement after different salt treatments in the following order: H2PO4- > CH3COO- > SO42- > Citrate3- > Cl- > CO32-. Rheological results showed that salt treatment led to enhancement of the energy storage modulus of the hydrogels. Further experiments indicated that the water-binding capacity of different salts depended on the salting out effect. Based on the Hofmeister effect, hardness-enhanced SPI-based hydrogels were successfully prepared. The Hofmeister effect offers a simple, an effective and a novel method for the preparation of functional SPI hydrogels.

The composition, extraction, functional property, quality, and health benefits of coconut protein: A review.

Coconut is widely appreciated for its distinctive flavor and is commonly utilized in the production of a variety of goods. Coconut protein, a by-product derived from coconut oil and coconut milk cake, is frequently underutilized or discarded. This study provides a comprehensive overview of the distribution and composition of coconut protein. Analyses reveal that coconut protein, specifically 11S globulin and 7S globulin, is predominantly found in coconut flesh. Furthermore, various extraction techniques for coconut protein, such as chemical, enzymatic, and physical methods, are discussed. The alkali dissolution and acid precipitation methods are widely utilized for extracting coconut protein, with the potential for enhancement through the incorporation of physical methods such as ultrasound. The evaluation of functional properties, quality, and health benefits of coconut protein is essential, given the limitations imposed by its solubility. Modification may be necessary to optimize its functional properties. Coconut presents a promising source of food protein, characterized by balanced amino acid composition, high digestibility, and low allergenic potential. In conclusion, this study provides a comprehensive overview of the extraction methods, functional properties, quality, and nutritional benefits of coconut protein, offering insights for potential future research directions in the field. Additionally, the information presented may serve as a valuable reference for incorporating coconut protein into plant-based food products.

Protein blend extrusion: Crafting meat analogues with varied textural structures and characteristics.

With an increasing emphasis on health and environmental consciousness, there is a growing inclination toward plant protein-based meat substitutes as viable alternatives to animal meat. In the pursuit of creating diverse and functional plant protein-based substitutes, innovative plant proteins have been introduced in conjunction with soy protein isolate (SPI), encompassing pea protein isolate (PPI), rice bran protein (RBP), fava bean protein isolate (FPI), and spirulina protein isolate (SPPI). Notably, SPI-WG extrudates and SPI-PPI extrudates exhibited superior fiber structures (fiber degrees were 1.72 and 1.88, respectively), with coarse fibers in SPI-WG extrudates and fine, dense fibers in SPI-PPI extrudates. The addition of RBP, FPI and SPPI had minimal effect on fiber structure. Fresh SPI-FPI displayed the slowest rate of water loss, losing about 7.11% of their total weight in 5 h. Different plant proteins can be selected for the preparation of plant protein-based meat substitutes according to practical needs.

Polyphenol improve the foaming properties of soybean isolate protein: Structural, physicochemical property changes and application in angel cake.

With the increasing demand for food foaming, how to enhance the foaming properties of protein has gradually become the research focus. This work studied the effect of synephrine (SY) on foaming properties, structure properties, and physicochemical properties of soybean protein isolate (SPI). When the mass ratio of SY to SPI was 1:2, compared with SPI alone, the foam capacity and foam stability of the SY-SPI complex were significantly enhanced. Optical microscopy and confocal laser scanning microscope showed that the improvement in foaming performance was mainly due to the reduction of bubble size and uniform protein distribution. Circular dichroism spectrum and fluorescence spectra indicated that the hydrogen bond of SPI was destroyed and blue shifted with the addition of SY. What's more, the absolute value of Zeta potential, solubility, and hydrophobicity all increased, while the particle size decreased. As a result of molecular docking, surface hydrogen bonds, Van der Waals forces and hydrophobic interactions are the main driving forces. The addition of SY and SPI improved the specific volume and texture of angel cake. This study shows that SY has the potential to be developed into a new type of blowing agent.

Advancing molecular understanding in high moisture extrusion for plant-based meat analogs: Challenges and perspectives.

In recent years, meat analogs based on plant proteins have received increasing attention. However, the process of high moisture extrusion (HME), the method for their preparation, has not been thoroughly explored, particularly in terms of elucidating the complex interactions that occur during extrusion, which remain challenging. These interactions arise from the various ingredients added during HME, including proteins, starches, edible gums, dietary fibers, lipids, and enzymes. These ingredients undergo intricate conformational changes and interactions under extreme conditions of high temperature, pressure, and shear, ultimately forming the fibrous structure of meat analogs. This review offers a overview of these ingredients and the molecular interaction changes they undergo during the extrusion process. Additionally, it delves into the major molecular interactions such as disulfide bonding, hydrogen bonding, and hydrophobic interactions, providing detailed insights into each.

Insight into the Stabilization Mechanism of Succinylation Modification on Black Bean Protein Gels: Molecular Conformation, Microstructure, and Gel Properties.

The objective of this work was to investigate the effect of succinylation treatment on the physicochemical properties of black bean proteins (BBPI), and the relationship mechanism between BBPI structure and gel properties was further analyzed. The results demonstrated that the covalent formation of higher-molecular-weight complexes with BBPI could be achieved by succinic anhydride (SA). With the addition of SA at 10% (v/v), the acylation of proteins amounted to 92.53 ± 1.10%, at which point there was a minimized particle size of the system (300.90 ± 9.57 nm). Meanwhile, the protein structure was stretched with an irregular curl content of 34.30% and the greatest processable flexibility (0.381 ± 0.004). The dense three-dimensional mesh structure of the hydrogel as revealed by scanning electron microscopy was the fundamental prerequisite for the ability to resist external extrusion. The thermally induced hydrogels of acylated proteins with 10% (v/v) addition of SA showed excellent gel elastic behavior (1.44 ± 0.002 nm) and support capacity. Correlation analysis showed that the hydrogel strength and stability of hydrogels were closely related to the changes in protein conformation. This study provides theoretical guidance for the discovery of flexible proteins and their application in hydrogels.

Effect of pH on the soybean whey protein-gum arabic emulsion delivery systems for curcumin: Emulsifying, stability, and digestive properties.

A novel curcumin (CUR) delivery system was developed using soybean whey protein (SWP)-based emulsions, enhanced by pH-adjustment and gum arabic (GA) modification. Modulating electrostatic interactions between SWP and GA at oil/water interface, pH provides favorable charging conditions for stable distribution between droplets. GA facilitated the SWP form a stable interfacial layer that significantly enhanced the emulsifying properties and CUR encapsulation efficiency of the system at pH 6.0, which were 90.15 ± 0.67%, 870.53 ± 3.22 m2/g and 2157.62 ± 115.31%, respectively. Duncan's test revealed significant improvements in thermal, UV, oxidative, and storage stabilities of CUR (P < 0.05). At pH 6.0, GA effectively protected CUR by inhibiting SWP degradation during gastric digestion and promoting the release of CUR by decreasing steric hindrance with oil droplets during intestinal digestion, achieving the highest CUR bioaccessibility (69.12% ± 0.28%) based on Duncan's test. The SWP-GA-CUR emulsion delivery system would be a novel carrier for nutrients.

Sacrificial hydrogen bonds enhance the performance of covalently crosslinked composite films derived from soy protein isolate and dialdehyde starch.

Soy protein films have the advantage of being eco-friendly and renewable, but their practical applications are hindered by the mechanical properties. The exceptional tensile strength and fracture toughness of natural silk stem from sacrificial hydrogen bonds it contains that effectively dissipates energy. In this study, we draw inspiration from silk's structural principles to create biodegradable films based on soy protein isolate (SPI). Notably, composite films containing sodium lignosulfonate (LS) demonstrate exceptional strain at break (up to 153%) due to the augmentation of reversible hydrogen bonding, contrasted to films with the addition of solely dialdehyde starch (DAS). The enhancement of tensile strength is realized through a combination of Schiff base cross-linking and sacrificial hydrogen bonding. Furthermore, the incorporation of LS markedly improves the films' ultraviolet (UV) blocking capabilities and hydrophobicity. This innovative design strategy holds great promise for advancing the production of eco-friendly SPI-based films that combine strength and toughness.

Effect of heat treatment on the structural and emulsifying properties of copra meal protein: Improving interfacial properties to enhance performance of its Pickering emulsion.

This study investigated the impact of different temperatures and durations on the structural and emulsifying properties of copra meal protein. Additionally, the stability of copra meal protein Pickering emulsions was assessed through rheological and interfacial characteristics. Findings revealed a positive correlation between emulsification properties and heating temperature and duration. Thermal aggregates, facilitated by hydrogen bonds, hydrophobic interactions, and disulfide bonds, significantly enhanced surface hydrophobicity. Heat-treated copra meal protein-based Pickering emulsions demonstrate enhanced adsorption at the oil-water interface and resistance to diffusion. The three-phase contact angle increases from 57.7° to 79.8° following heating at 95 °C for 30 min. The addition of NaCl and heating treatment did not affect emulsion particle size or interface adsorption ability. But it improved the rheological properties to varying degrees. These results offer valuable insights for optimizing the physicochemical and functional attributes of copra meal protein in the food industry.

Complexes of soybean protein fibrils and chlorogenic acid: Interaction mechanism and antibacterial activity.

This study explored the mechanism of interaction between chlorogenic acid (CA) and protein fibrils (PF) as well as the effects of varying the CA/PF concentration ratio on antibacterial activity. Analysis of various parameters, such as ζ-potential, thioflavin T fluorescence intensity, surface hydrophobicity, and free sulfhydryl groups, revealed that the interaction between PF and CA altered the structure of PF. Fluorescence analysis revealed that hydrogen bonding and hydrophobic interactions were the primary interaction forces causing conformational rearrangement, resulting in a shorter, more flexible, and thicker fibril structure, as observed through transmission electron microscopy. Fourier-transform infrared spectroscopy, small-angle X-ray scattering, and X-ray diffraction analyses revealed that the characteristic fibril structure was destroyed when the CA/PF ratio exceeded 0.05. Notably, the CA-PF complexes inhibited the growth of Escherichia coli and Staphylococcus aureus and also exhibited antioxidant activity. Overall, this study expands the application prospects of CA and PF in the food industry.

Soybean isolate protein complexes with different concentrations of inulin by ultrasound treatment: Structural and functional properties.

The effects of ultrasound and different inulin (INU) concentrations (0, 10, 20, 30, and 40 mg/mL) on the structural and functional properties of soybean isolate protein (SPI)-INU complexes were hereby investigated. Fourier transform infrared spectroscopy showed that SPI was bound to INU via hydrogen bonding. All samples showed a decreasing and then increasing trend of α-helix content with increasing INU concentration. SPI-INU complexes by ultrasound with an INU concentration of 20 mg/mL (U-2) had the lowest content of α-helix, the highest content of random coils and the greatest flexibility, indicating the proteins were most tightly bound to INU in U-2. Both UV spectroscopy and intrinsic fluorescence spectroscopy indicated that it was hydrophobic interactions between INU and SPI. The addition of INU prevented the exposure of tryptophan and tyrosine residues to form a more compact tertiary structure compared to SPI alone, and ultrasound caused further unfolding of the structure of SPI. This indicated that the combined effect of ultrasound and INU concentration significantly altered the tertiary structure of SPI. SDS-PAGE and Native-PAGE displayed the formation of complexes through non-covalent interactions between SPI and INU. The ζ-potential and particle size of U-2 were minimized to as low as -34.94 mV and 110 nm, respectively. Additionally, the flexibility, free sulfhydryl groups, solubility, emulsifying and foaming properties of the samples were improved, with the best results for U-2, respectively 0.25, 3.51 µmoL/g, 55.51 %, 269.91 %, 25.90 %, 137.66 % and 136.33 %. Overall, this work provides a theoretical basis for improving the functional properties of plant proteins.

Encapsulation and characterization of ω-3 medium- and long-chain triacylglycerols microencapsulated with different proteins as wall materials.

In this study, ω-3 medium- and long-chain triacylglycerols (MLCTs) microcapsules with excellent performance were obtained using soy protein as the wall component to address the oxidation-related problems of MLCTs. Additionally, the effect of soy, whey, or pea proteins on microcapsules in terms of the changes in their structure and physicochemical properties was investigated. The results showed that the small particle size, low PDI (polydispersity index) and zeta potential, fast adsorption rate, and low interfacial tension of these protein-based samples fabricated through the O/W template method were conducive to maintaining the integrity of microcapsules during spray-drying. The microcapsules, characterized by a spherical shape, exhibited superior encapsulation efficiency of 94.56%, surpassing the findings of previous investigations. Overall, these microcapsules exhibited long-term storage stability and low controllable release rates, which could be utilized as carriers for liposoluble actives.

Fabrication of soy protein nanoparticles based on metal-phenolic networks for stabilization of nano-emulsions delivery system.

The use of soy protein isolate (SPI) nanoparticles as a stabilizer in nano-emulsion systems has garnered significant interest. While metal-phenolic networks (MPNs) have been explored for their multifunctional surface modification capabilities, their integration with food protein-based delivery systems remains less explored. In this study, we attempt to develop a novel strategy to encapsulate cinnamaldehyde using MPNs (EGCG-Fe3+) with self-assembling soy protein nanoparticles (SE-Fe NPs) as a stabilizer for nano-emulsions. UV, Raman, and X-ray photoelectron spectroscopy analyses demonstrated that SE-Fe NPs were generated through metal-phenolic coordination and covalent interactions. SE-Fe NPs had a narrower particle size distribution and enhanced radical scavenging (up to 3.35-fold), as well as thermal stability. Furthermore, the smaller droplet size, higher modulus, higher cinnamaldehyde encapsulation efficiency (from 63.5% to 84.2%), and improved bio-accessibility of SE-Fe NPs stabilized nano-emulsions delivery system demonstrated in this study shows promising future applications in the food industry.

Analytical approaches for assessing protein structure in protein-rich food: A comprehensive review.

This review focuses on changes in nutrition and functional properties of protein-rich foods, primarily attributed to alterations in protein structures. We provide a comprehensive overview and comparison of commonly used laboratory methods for protein structure identification, aiming to offer readers a convenient understanding of these techniques. The review covers a range of detection technologies employed in food protein analysis and conducts an extensive comparison to identify the most suitable method for various proteins. While these techniques offer distinct advantages for protein structure determination, the inherent complexity of food matrices presents ongoing challenges. Further research is necessary to develop and enhance more robust detection methods to improve accuracy in protein conformation and structure analysis.

Liposomes decorated with ß-conglycinin and glycinin: Construction, structure and in vitro digestive stability.

Liposomes were modified with different proportions of ß-conglycinin (7S) and glycinin (11S) to form Lip-7S and Lip-11S. The morphology, interaction and in vitro simulated digestion of liposomes were studied. The particle size of Lip-7S was smaller than that of Lip-11S. When the values of Lip-7S and Lip-11S were 1:1 and 1:0.75, respectively, the ζ-potential had the maximum absolute value and the dispersion of the system was good. The results of multispectral analysis showed that hydrogen-bond and hydrophobic interaction dominated protein-modified liposomes, the protein structure adsorbed on the surface of liposomes changed, the content of α-helix decreased, and the structure of protein-modified liposomes became denser. The surface hydrophobicity and micropolarity of liposomes decreased with the increase of protein ratio, and tended to be stable after Lip-7S (1:1) and Lip-11S (1:0.75). Differential scanning calorimetry showed that Lip-7S had higher phase transition temperature (≥170.5 °C) and better rigid structure. During simulated digestion, Lip-7S (22.5 %) released less Morin than Lip (40.6 %) and Lip-11S (26.2 %), and effectively delayed the release of FFAs. The environmental stability of liposomes was effectively improved by protein modification, and 7S had better modification effect than 11S. This provides a theoretical basis for 7S and 11S modified liposomes, and also provides a data reference for searching for new materials for stabilization of liposomes.

Enhancing the properties of soy protein isolate and dialdehyde starch films for food packaging applications through tannic acid crosslinking.

The utilization of naturally derived biodegradable polymers, including proteins, polysaccharides, and polyphenols, holds significant promise in addressing environmental concerns and reducing reliance on nonrenewable resources. This study aimed to develop films with enhanced UV resistance and antibacterial capabilities by covalently cross-linking soy protein isolate (SPI) with dialdehyde starch (DAS) through the incorporation of tannic acid (TA). The covalent crosslinking of TA with DAS and SPI was shown to establish a stable chemical cross-linking network. The tensile strength of the resulting SPI/DAS/15TA film exhibited a remarkable increase of 208.27 % compared to SPI alone and 52.99 % compared to SPI/DAS film. Notably, the UV absorption range of SPI/DAS/10TA films extended from 200 nm to 389 nm. This augmentation can be attributed to the oxidation of TA's phenolic hydroxyl groups to quinone under alkaline conditions, which then facilitated cross-linking with the SPI chain via Michael addition and Schiff base reactions. Furthermore, the film demonstrated robust antibacterial properties due to the incorporation of TA. Collectively, the observed properties highlight the significant potential of the SPI/DAS/10TA film for applications in food packaging, where its enhanced mechanical strength, UV resistance, and antibacterial characteristics can contribute to improved product preservation and safety.