Search

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. As a worldwide cultivated and largely consumptive crop, allergies and some physicochemical limitations have also led to a few concerns about walnut protein. Through comprehensive analysis and discussion, some strategies may be useful for future research, extraction and processing of walnut protein. [ABSTRACT FROM AUTHOR]

The conversion of toxic Fe2+ into non-toxic Fe3+ 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 Fe2+ (9.1 times that of rHuHF) to reduce the precursors of Fenton reaction, thus inhibiting the occurrence of Fenton reaction and slowing down reactive oxygen species-mediated inflammation. The above significant advantage of GF1 can be attributed to the Asp at the position 120th, which could increase the negatively charged area of three-fold channels from 37.8% (rHuHF) to 67.8% and then enhance its oxidation rate and ability of GF1. The findings are of great value in advancing novel nanoparticle drug design based on crystalline structure. [Display omitted] • Asp120 of oyster ferritin had a contribution to the catalytic oxidation rate of Fe2+. • Oyster ferritin shows the catalytic activity of 7.7 times higher than that of rHuHF. • Oyster ferritin shows the binding ability of 9.1 times higher than that of rHuHF. • Oyster ferritin could significantly reduce the precursors of Fenton reaction. [ABSTRACT FROM AUTHOR]

Understanding the effect of thermal treatment on the physical and chemical properties of protein and its mechanisms has important theoretical implications in food science. Pea seed ferritin (PSF) is an iron storage protein naturally occurring in pea seeds, which represents a promising iron supplement. However, how thermal processing affects the structure and function of PSF remains unknown. In this work, during the production of pea seed milk, we investigated the effect of thermal treatments at boiling temperature for two different times (5 and 10 min), respectively, on the structure and function of PSF. The results demonstrated that thermal treatment resulted in a pronounced change in the primary, secondary, and tertiary structure, iron content, and iron oxidation activity of PSF. However, the shell-like structure of PSF can be kept during the processing of pea seed milk. Interestingly, upon thermal treatment, both thermal-treated samples exhibit larger higher iron absorption rate by Caco-2 than untreated PSF at the same protein concentration. Such an investigation provides a better understanding of the relationship between the structure and function of food protein, as affected by thermal treatment. [ABSTRACT FROM AUTHOR]

Heavy metal ions pollution can cause damage to human body through food, so the development of a new kind of macromolecular that can remove heavy metal ions damage has a good application prospect. The possibilities of removing heavy metal ions from food system with ferritin were studied in this paper. In this study, oyster ferritin (GF1) can resistant to denaturation induced by Pb2+, Cd2+, Cr3+ and still maintains its basic structure. GF1 can bind more Pb2+, Cd2+, Cr3+ than recombinant human H-chain ferritin (rHuHF), especially Pb2+, and the findings suggest that each GF1 can capture about 51.42 Pb2+ in solution. The hard and soft acids and base also verifies that Pb2+ have stronger binding ability to the key amino acids at the outer end of the three-fold symmetry channel. Cells preprotected by ferritin could resistant to heavy metal ions. And GF1 can reduce the high blood lead in mice and may play a role in alleviating lead poisoning in vivo. All findings demonstrated that GF1 can be used as a novel macromolecule to bind heavy metal ions, and the study can broaden the research scope of ferritin in contaminated food systems. [Display omitted] • Oyster ferritin can maintain certain structural and physiological activities upon treatment with Pb2+, Cd2+ and Cr3+. • Oyster ferritin can bind more Pb2+ than recombination human heavy chain ferritin. • Oyster ferritin can significantly reduced blood lead levels in mice. [ABSTRACT FROM AUTHOR]

Over the past few decades, 1D self-assembly of proteins into various filaments has received considerable attention. Protein filaments ubiquitously exist in nature, which not only govern the cellar metabolism in vivo but also tune the physiochemical properties of foodstuffs in vitro. Myofibrillar proteins and collagens are natural filaments abundantly occurring in muscles, with a precise associating and dissociating mechanism. Sharing similar morphologies, a great number of globular proteins, sourced from versatile foodstuffs, can likewise be converted into filaments upon different treatments, albeit their structure remains enigmatic. This review summarized both natural and synthetic protein filaments by characterizing their distinct structures, assembly behaviors, methodologies, and promising applications. Finally, current challenges and future strategies in this research field are discussed. The goal of this review is to highlight the essence of different protein filaments constructed by natural and denatured building blocks, which may support valuable insights into food science and broader applications. [Display omitted] • Protein filaments are ubiquitously existed in foodstuffs. • Myofibrillar proteins and collagens have specific assembly mechanism. • Natural and synthesized protein filaments have been compared. • A few factors affect the process of protein fibrilization. [ABSTRACT FROM AUTHOR]

• Point mutation in D120G could improve the thermal stability of oyster ferritin. • The spherical shell of mutated ferritin can be kept well at 90 °C and below. • The stability of oyster ferritin was promoted via the improved 3-fold interfaces. Ferritin can be widely used as functional nanomaterial. But the physiological activity of ferritin can be damaged under excessive temperatures, which affect the self-assembly property. In this study, point mutation was produced in Asp120 to Gly120 of ferritin amino acid sequence and the heat resistance was improved significantly. The thermal denaturation temperature of mutated ferritin is 89.17 °C and has increased by 13 °C more than the wild-type oyster ferritin. The effect of thermal treatment on the denaturation, aggregation state, particle size and the structure of ferritin was not changed before 90 °C. The computational modeling and analysis indicated that mutated ferritin promotes the overall structural stability assembly via decreasing the interaction energies of 62 percent energies in 3-fold interface. Improving the thermal stability of oyster ferritin by point mutation enhances its applications as a food ingredient. [ABSTRACT FROM AUTHOR]

• Thermal treatment could induce denaturation and aggregation of oyster ferritin. • The ferritin spherical shell destroyed gradually and could not be observed at 100 °C. • Thermal treatment could change the structure of oyster ferritin. The unique nanocage structure of ferritin can be used as functional nanomaterials and has wide application prospects. However, thermal treatment may affect the structure of ferritin, further affecting self-assembly property. In this study, the oyster ferritin gene GF1 was obtained, prokaryotically expressed in E. coli BL21 (DE3). Then the purified ferritin was heated from 60 to 100 °C for 10 min with untreated ferritin as a control sample. The aggregation state of ferritin was investigated and the difference in protein structure was evaluated in terms of particle size and protein structures. The results of electrophoresis indicated that thermal treatment induced denaturation and aggregation of ferritin macromolecules. Moreover, the particle size distribution shifted to larger size trend and aggregates were visible with the heated samples and the secondary structure and tertiary structure were destroyed gradually. The findings are beneficial for understanding the relationship of the structure and function of ferritin. [ABSTRACT FROM AUTHOR]