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Intermolecular interactions influenced the gelation and texture improvement of sturgeon surimi gels by walnut protein isolates.

Food Chem

March 2025

College of Food Science and Technology, Yunnan Agricultural University, 425 Fengyuan Road, Kunming 650201, Yunnan, China. Electronic address:

Intermolecular interaction is a key factor in the fortification of surimi gels by plant protein addition. Here, the effects of different intermolecular interactions, such as ionic, covalent and non-covalent interactions, on gel structure, gelation strength and water-holding properties were investigated, using sturgeon surimi fortified by three walnut isolates, including walnut meal (WM), protein isolate (WPI) and peptide (WP), as representatives. Quantitative creep-recovery analysis and soluble protein assay demonstrated that secondary bonds, mainly hydrophobic interaction and hydrogen bond, possibly played a dominant role in walnut protein-fortified surimi gels.

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Combining single atoms via phase transition engineering (from 2H to 1T) remains a challenge in MoS-based catalysts. Herein, we report that Pt single atoms (Pt) were doped into a 3D flower-like 1T-MoS catalyst (Pt@MoS) using a Pt-S bonding strategy. Doping with Pt induced a phase transition in MoS from the 2H phase to the 1T phase.

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Chemical peptide engineering, enabled by residue insertion, backbone cyclization, and incorporation of an additional disulfide bond, led to a unique cyclic peptide that efficiently inhibits the invasion of red blood cells by malaria parasites. The engineered peptide exhibits a 20-fold enhanced affinity toward its receptor (AMA1) compared to the native peptide ligand (RON2), as determined by surface plasmon resonance. In-vitro parasite growth inhibition assay revealed augmented potency of the engineered peptide.

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Plant Defense Peptides: Exploring the Structure-Function Correlation for Potential Applications in Drug Design and Therapeutics.

ACS Omega

March 2025

Department of Biosciences and Technology, School of Science and Environmental Studies, Dr. Vishwanath Karad MIT-World Peace University, Kothrud, Pune, Maharashtra 411038, India.

Defense peptides are part of plants' innate immune system and show widespread occurrence across the plant kingdom. Most of them belong to the category of antimicrobial peptides (AMPs) and act as strong chemical weapons against the biotic stresses that plants encounter. Plant AMP families exhibit remarkably conserved topology, being cysteine-rich with a conserved number of disulfide bridges stabilizing their three-dimensional structure, cationic in nature, and having hydrophobic surfaces.

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Background: Phenols have been demonstrated to enhance protein gelation but their stability is often compromised in heat-induced gels. This has prompted the development of cold-induced gels. The objective of this study was to enhance the gel properties of hazelnut isolate protein (HPI) through the incorporation of transglutaminase (TGase), glucono-δ-lactone (GDL), and chlorogenic acid (CA).

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