Ozone treatment increase the whiteness of soy protein isolate through the degradation of isoflavone.

The color of soy protein isolate (SPI) influences the appearance of products such as tofu and soymilk, consequently impacting consumer preferences. Typically, whiter-colored SPIs were more favorite. However, products currently manufactured in the industry predominantly exhibit a yellowish hue.

Both Hemocyanin and β-1,3-Glucan-Binding Protein from the Shrimp Shell of Are Responsible for Its Color Change from Brown to Red during Thermal Processing.

Because of the composition and structural complexity of crustacean shells, their color change mechanism during thermal processing remains unclear. This study identified and characterized two intrinsic protein components, hemocyanin (Lv-Hc) and β-1,3-glucan-binding protein (Lv-BGBP) from shrimp shells by a combination of ion-exchange chromatography, gel filtration, and mass spectrometry. It was found that a mixture of Lv-Hc, a gray protein, and Lv-BGBP (which is a natural astaxanthin-binding protein with a red color) is responsible for the brown color of fresh shrimp shells.

Metals at the Helm: Revolutionizing Protein Assembly and Applications.

Protein assembly is an essential process in biological systems, where proteins self-assemble into complex structures with diverse functions. Inspired by the exquisite control over protein assembly in nature, scientists have been exploring ways to design and assemble protein structures with precise control over their topologies and functions. One promising approach for achieving this goal is through metal coordination, which utilizes metal-binding motifs to mediate protein-protein interactions and assemble protein complexes with controlled stoichiometry and geometry.

Construction of An Artificial Photosynthesis System with A Single CdS QDs-Ferritin Hybrid Molecule.

Establishing artificial photosynthesis systems in a simple but effective manner to mitigate the greenhouse effect and address the energy crisis remains challenging. The combination of photocatalysis technology with bioengineering is an emerging field with great potential to construct such artificial photosynthesis systems, but so far, it has barely been explored in this area. Herein, an artificial photocatalysis platform is constructed with high CO conversion and HO splitting capability by integration of CdS QDs into the intra-subunit interface of H-type ferritin (Marsupenaeus japonicus), a natural ferroxidase through protein interface redesign.

Harnessing Protein Hydrolysates and Peptides for Hyperuricemia Management: Insights into Sources, Mechanisms, Techniques, and Future Directions.

Hyperuricemia (HUA) is a metabolic disorder characterized by an imbalance in uric acid production and excretion, frequently leading to gout and various chronic conditions. Novel bioactive compounds offer effective alternatives for managing HUA, reducing side effects of traditional medications. Recent studies have highlighted the therapeutic potential of protein hydrolysates and peptides in managing HUA.

Understanding the Role of Filamentous Actin in Food Quality: From Structure to Application.

Actin, a multifunctional protein highly expressed in eukaryotes, is widely distributed throughout cells and serves as a crucial component of the cytoskeleton. Its presence is integral to maintaining cell morphology and participating in various biological processes. As an irreplaceable component of myofibrillar proteins, actin, including G-actin and F-actin, is highly related to food quality.

A comprehensive review on hemocyanin from marine products: Structure, functions, its implications for the food industry and beyond.

Hemocyanin, an oxygen-transport protein, is widely distributed in the hemolymph of marine arthropods and mollusks, playing an important role in their physiological processes. Recently, hemocyanin has been recognized as a multifunctional glycoprotein involved in the immunological responses of aquatic invertebrates. Consequently, the link between hemocyanin functions and their potential applications has garnered increased attention.

Advancements of the Molecular Directed Design and Structure-Activity Relationship of Ferritin Nanocage.

Ferritin nanocages possess remarkable structural properties and biological functions, making them highly attractive for applications in functional materials and biomedicine. This comprehensive review presents an overview of the molecular characteristics, extraction and identification of ferritin, ferritin receptors, as well as the advancements in the directional design of high-order assemblies of ferritin and the applications based on its unique structural properties. Specifically, this Review focuses on the regulation of ferritin assembly from one to three dimensions, leveraging the symmetry of ferritin and modifications on key interfaces.

Construction of Manganese-Based Oyster () Ferritin Nanozyme with Catalase-like Enzyme Activity.

MnO is a nanozyme that inhibits the decomposition of hydrogen peroxide (HO) into a hydroxyl radical (OH), thus preventing its conversion into reactive oxygen species (ROS). Oyster ferritin (GF1) is a macromolecular protein that provides uniform size and high stability and serves as an excellent template for the biomineralization of nanozyme. This study presents a unique method in which MnO is grown in situ in the GF1 cavity, yielding a structurally stable ferritin-based nanozyme (GF1@Mn).

Characterization and Structural Analyses of Enolase from Shrimp ().

Transcriptome analysis had recognized enolase from shrimp (), which is termed LvEnolase, as one of the allergens, but its amino acid sequence and protein structure have been lacking. In this study, natural LvEnolase was isolated from and characterized for the first time. The full-length cDNA sequence of LvEnolase was effectively cloned, which encoded 434 amino acid residues.

Preparation and Unique Three-Dimensional Self-Assembly Property of Starfish Ferritin.

The structure and assembly properties of ferritin derived from aquatic products remain to be explored. Constructing diverse three-dimensional (3D) protein architectures with the same building blocks has important implications for nutrient delivery, medicine and materials science. Herein, ferritin from (AfFer) was prepared, and its crystal structure was resolved at 1.

Shape-Anisotropic Assembly of Protein Nanocages with Identical Building Blocks by Designed Intermolecular π-π Interactions.

Protein lattices that shift the structure and shape anisotropy in response to environmental cues are closely coupled to potential functionality. However, to design and construct shape-anisotropic protein arrays from the same building blocks in response to different external stimuli remains challenging. Here, by a combination of the multiple, symmetric interaction sites on the outer surface of protein nanocages and the tunable features of phenylalanine-phenylalanine interactions, a protein engineering approach is reported to construct a variety of superstructures with shape anisotropy, including 3D cubic, 2D hexagonal layered, and 1D rod-like crystalline protein nanocage arrays by using one single protein building block.

Advanced Insights into Walnut Protein: Structure, Physiochemical Properties and Applications.

Facing extreme pressure from an increasing population and climate degeneration, it is important to explore a green, safe and environmentally sustainable food source, especially for protein-enriched diets. Plant proteins have gained much attention in recent years, ascribing to their high nutritional value and environmental friendliness. In this review, we summarized recent advances in walnut protein with respect to its geographical distribution, structural and physiochemical properties and functional attributes.

Oyster (Crassostrea gigas) ferritin relieves lead-induced liver oxidative damage via regulating the mitophagy.

Lead can induce oxidative stress and increase lipid peroxidation in biofilms, leading to liver damage and physiological dysfunction. This study aimed to investigate how oyster ferritin (GF1) attenuates lead-induced oxidative damage to the liver in vitro and in vivo. Animal experiments have confirmed that lead exposure can lead to oxidative damage and lipid peroxidation of the liver, and ferritin can regulate the activity of antioxidant enzymes and alleviate pathological changes in the liver.

Highly Stretchable, Transparent, and Adhesive Double-Network Hydrogel Dressings Tailored with Fish Gelatin and Glycyrrhizic Acid for Wound Healing.

It remains challenging to fabricate highly stretchable and adhesive hydrogel dressings for wound healing using simple, safe, and green methods. Herein, inspired by the main components of snail mucus, a fully physical double-network (DN) hydrogel dressing composed of fish gelatin (FGel) and glycyrrhizic acid (GL) was fabricated, in which FGel provided a protein scaffold to mimic snail mucus proteins, while GL mimicked the adhesion and bioactivity of snail mucus because of its abundant carboxyl and hydroxyl groups and intrinsic immunomodulatory activity. As expected, the obtained FGel/GL hydrogel dressings exhibited outstanding mechanical and adhesive performances (flexibility, stretchability, adhesive ability, and removability), high transparency, and good antifreezing properties.

Oyster ferritin can efficiently alleviate ROS-mediated inflammation attributed to its unique micro-environment around three-fold channels.

The conversion of toxic Fe into non-toxic Fe stored in the inner cavity of ferritin nanocage could effectively reduce the occurrence of the Fenton reaction and inhibit the formation of harmful reactive oxygen species (ROS). In this study, we reveal that oyster ferritin (GF1) can rely on its high catalytic activity (7.7 times that of rHuHF) and high binding ability of Fe (9.

Spatiotemporal control over 3D protein nanocage superlattices for the hierarchical encapsulation and release of different cargo molecules.

Taking inspiration from Nature, we have constructed a two-compartment system based on 3D ferritin nanocage superlattices, the self-assembly behavior of which can be spatiotemporally controlled using two designed switches. One pH switch regulates the assembly of the ferritin subunit into its shell-like structure, whereas the other metal switch is responsible for assembly of the 3D superlattices from ferritin nanocages as building blocks. Consequently, this system holds great promise for the hierarchical encapsulation and release of two different cargo molecules.

Dietary Heme-Containing Proteins: Structures, Applications, and Challenges.

Heme-containing proteins, commonly abundant in red meat and blood, are considered promising dietary sources for iron supplementation and fortification with higher bioavailability and less side effects. As the precise structures and accurate bioactivity mechanism of various heme-containing proteins (hemoglobin, myoglobin, cytochrome, etc.) are determined, many methods have been explored for iron fortification.

Microencapsulation of Carvacrol by Complex Coacervation of Walnut Meal Protein Isolate and Gum Arabic: Preparation, Characterization and Bio-Functional Activity.

As a natural phenolic compound, carvacrol has attracted much attention due to its excellent antibacterial and antioxidant activities. However, its application is limited due to its instability, such as easy volatilization, easy oxidation, etc. Protein-polysaccharide interactions provide strategies for improving their stability issues.

Oyster (Crassostrea gigas) ferritin should be a promising Fe nanocarrier.

Ferritin, one of the storage forms of iron, which widely exists in all living organisms and shows its potential as functional nanomaterial. In this study, Fe were added to oyster ferritin (GF1) in vitro until reached experimental saturation state. The structure characterization and monodisperse morphology of ferritin were showed that the protein structure of ferritin did not change significantly after adding Fe and GF1 with 1000 Fe (GF1-1000 Fe) was selected for subsequent experiments.

Directed Self-Assembly of Dimeric Building Blocks into Networklike Protein Origami to Construct Hydrogels.

Engineering proteins to construct self-assemblies is of crucial significance not only for understanding the sophisticated living systems but also for fabricating advanced materials with unexplored functions. However, due to the inherent chemical heterogeneity and structural complexity of the protein surface, designing complex protein assemblies in an anisotropic fashion remains challenging. Here, we describe a self-assembly approach to fabricating protein origami with a networklike structure by designing dual noncovalent interactions on the different positions of a single protein building block.

A natural strategy for astaxanthin stabilization and color regulation: Interaction with proteins.

The pigment astaxanthin, one of the carotenoids, is regarded as a functional factor with various biological activities, widely applied in feed, nutraceutical, and cosmetic industries. However, its low stability and poor water solubility limit its application. Examples in nature suggest that binding to proteins is a simple and effective method to improve the stability and bioavailability of astaxanthin.

Zinc binding strength of proteins dominants zinc uptake in Caco-2 cells.

Zinc plays a vital role in structural, catalysis, and signal regulation in the human body. Zinc deficiency leads to the dysfunction of many organs and immunity systems. Diet proteins have distinct effects on zinc uptake.