Research Keyword: protein modification

The Effects of Iterative Freeze–Thaw Cycles on the Structure, Functionality, and Digestibility of Grifola frondosa Protein

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This research shows that freezing and thawing maitake mushroom protein in controlled cycles can significantly improve its ability to stabilize oil and water mixtures in food products. The best results occur after 2-3 cycles, which enhance both how well the protein breaks down during digestion and how effectively it works as an emulsifier in foods like sauces and dressings. This simple physical treatment method offers a sustainable way to improve mushroom protein for food manufacturing without affecting its nutritional quality.

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Identification of the High Mannose N-Glycan Isomers Undescribed by Conventional Multicellular Eukaryotic Biosynthetic Pathways

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Researchers developed a new method to identify the sugar structures attached to proteins in various foods and organisms. They discovered that many of these sugar structures are different from what scientists previously thought based on standard biological pathways. Using advanced mass spectrometry technology, they created a database to quickly identify these novel sugar structures, which could help better understand how organisms modify their proteins.

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Antimicrobial effects and mechanisms of hydrogen sulphide against nail pathogens

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Researchers discovered that hydrogen sulphide (H2S), a small gas molecule, can effectively kill the fungi and bacteria that cause painful nail infections. Unlike current treatments that struggle to penetrate into the nail, hydrogen sulphide easily diffuses through the nail plate. The study found that H2S works by damaging the fungi’s respiratory system and creating harmful reactive oxygen species, while also modifying proteins in a way that disrupts their normal function. This innovative approach could offer patients a new topical treatment option for nail infections that have been difficult to treat with existing medications.

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Effects of ultrasound-assisted extraction and transglutaminase treatment on the physicochemical properties of protein from Stropharia rugosoannulata

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Researchers developed improved methods to extract and modify protein from Stropharia rugosoannulata mushrooms to make them better for use in plant-based meat products. Using ultrasound waves and an enzyme called transglutaminase, they were able to increase the protein yield and improve how well the protein can hold water and oil. These modifications enhanced the mushroom protein’s ability to work as a meat substitute in food products.

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Cross-linking impacts the physical properties of mycelium leather alternatives by targeting hydroxyl groups of polysaccharides and amino groups of proteins

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Scientists have developed a leather-like material grown from mushroom mycelium (the root structure of fungi) that can match the strength of animal leather through a process called cross-linking or tanning. They tested different cross-linking chemicals—both synthetic ones like glutaraldehyde and natural plant extracts—and found that these chemicals improve the material’s strength and durability. The best results came from treating the mycelium with a low concentration of glutaraldehyde, which made it nearly as strong as real leather while using a sustainable, environmentally-friendly process.

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Effects of Freeze–Thaw Cycles on the Structures and Functional Properties of Clitocybe squamulosa Protein Isolates

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Researchers studied how repeatedly freezing and thawing a protein extract from the edible Clitocybe squamulosa mushroom affects its usefulness in food products. They found that three freeze-thaw cycles improved the protein’s ability to create stable foams and emulsions, while two cycles best preserved digestibility and antioxidant benefits. This simple, chemical-free treatment method could help food manufacturers create better products using mushroom proteins.

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