Analytical Methods
·
2025
·
IF 2.6
Tianping Chen,Yanru Tao,Xi Cao,Shiyi He,Hua Zhao,Jiangling Hu,Hongmei Wang,Xinhui Jiang
This study developed a high-performance liquid chromatography coupled with fluorescence detection (HPLC-FLD) method for the simultaneous determination of 19 amino acids in the cortex, hippocampus, and bone marrow samples of BALB/C-nu/nu and NOD/SCID mice. We measured the changes in the levels of 19 amino substances in the cortex, hippocampus, and bone marrow samples of mice in the blank model group, acute leukemia model group, chronic leukemia model group, and treatment group. The chromatographic column used was a COSMOSIL 5 C18-MS-II analytical column (150 mm × 4.6 mm, 5 μm), with the column temperature set at 35 °C. The mobile phase was a methanol-ammonium acetate buffer solution (30 mmol L−1 ammonium acetate solution, adjusted to pH 6.40 with acetic acid), at a flow rate of 0.9 mL min−1. The single analysis time was 46 minutes. By optimizing the analysis conditions, the newly established HPLC-FLD method exhibits high sensitivity, good accuracy, and good reproducibility. This method can be successfully applied to determine 19 amino substances in the cortex, hippocampus, and bone marrow of BALB/C-nu/nu and NOD/SCID mice. The differences in amino acid content between different groups can be used to further study the development process of leukemia, disease diagnostic markers, and personalized treatment plans.
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Food Bioscience
·
2026
·
IF 6.2
Juntao Yu,Tonghao Du,Xingyu Zhu,Jiajia Zhang,Chengzhe Liu,Xiaobin Ruan,Xiaoxia Sun,Li Yang,Tao Xiong,Mingyong Xie,Tao Huang
Lacticaseibacillus paracasei NCU215 was recognized for its robust probiotic activities and excellent fermentation capabilities. In the present study, whole-genome, comparative genomics analysis, and experimental validation were integrated to systematically investigate the potential functional traits of NCU215. Genomic analysis revealed that NCU215 harbors a repertoire of functional genes and is devoid of genes associated with human pathogenicity. Additionally, the metabolic pathways involved in amino acid and carbohydrate metabolism in NCU215 were computationally predicted. Based on average nucleotide identity (ANI), average amino acid identity (AAI), and core-genome phylogenetic reconstruction, the taxonomic assignment of NCU215 was revised from Lacticaseibacillus casei to Lacticaseibacillus paracasei . Comparative genomic analysis indicated that NCU215 contains higher abundance of genes associated with cell adhesion, carbohydrate metabolism, and a unique amino acid metabolic gene cluster ( cysK–ctl1–cysE ). Experimental validation confirmed that NCU215 displays a high adhesion rate of 7.86 ± 0.65% to Caco-2 cells, the ability to convert methionine to cysteine, enhanced utilization of galactose, mannose, fructooligosaccharides, and inulin, as well as bile salt hydrolase activity and a high cholesterol-lowering efficacy of 47.30 ± 2.61%. Furthermore, soymilk fermented with NCU215 exhibited a substantial reduction in volatile compounds such as hexanal and 1-octen-3-ol, while the contents of acetoin and 2,3-butanedione were notably elevated.
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COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS
·
2026
·
IF 5.4
Zhuo Pu,Qiuhao Wang,Liming Tao,Hongqi Fu,Jianyong He,Zhiyong Gao
Zircon is the primary mineral for zirconium and hafnium extraction. However, removing associated gangue minerals such as feldspar from fine zircon ore is challenging due to the limitations of utilizing a single collector. This paper proposed a mixed collector n-octylphosphonic acid (n-OPA)/octyl hydroxamic acid (OHA) to promote the separation of zircon and feldspar. Accordingly, solution chemistry calculations, zeta potential, surface tension measurements and density functional theory (DFT) calculations were performed to study the detailed adsorption mechanism of mixed collector on surface of zircon. Flotation results for single minerals demonstrated that the mixed collector effectively facilitated the separation of zircon from feldspar, achieving a maximum recovery difference exceeding 88.00%. Run-of-mine ore flotation tests indicated that the use of n-OPA/OHA as a collector resulted in a zircon concentrate with a ZrSiO 4 grade of 12.57% and a recovery of 82.21%. In contrast, when sodium oleate (NaOL) was used as the collector, the ZrSiO 4 grade and recovery were 8.33% and 66.01%, respectively. Solution chemistry calculations and zeta potential measurements indicated that at pH 2.0, the mixed collector exists in the forms of n-OPA molecules, n-OPA −1 , and OHA molecules. Following interaction with the mixed collector, the surface potential of zircon significantly decreased by 14.8 mV. Surface tension measurements demonstrated a positive synergistic effect between n-OPA and OHA. DFT calculations revealed that the intermolecular interaction energies between n-OPA-OHA and n-OPA −1 -OHA were 41.5 and 32.8 kJ/mol, respectively, primarily attributed to hydrogen-bonding between them.
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POLYMER
·
2026
·
IF 4.5
Xianyu Guo,Wentao Tan,Ling Wang,Fengrui Yang,Yuhang Ma,Yi Shen,Caihong Luo,Qian Luo,Xiao Xie,Hui Li
Chiral separation of D- and L-Serine is of great value in the fields of biopharmaceuticals. For this purpose, a D-Serine imprinted polymer was prepared by precipitation polymerization with the aid of deep eutectic solvent (DES) and crowding agent (polymethyl methacrylate, PMMA). The preparation conditions were optimized by a L 9 (3 4 ) orthogonal design. Structure characterization was performed by the FTIR, SEM, AFM and XPS techniques and adsorption selectivity and separation efficiency for this imprinted material investigated. The results showed that under the conditions of pH 5.0 and 303 K, the polymer exhibited maximum adsorption capacity, reaching 121.4 mg g -1 , with a selectivity factor as high as 11.87. When this D-serine-imprinted material was used as a chromatographic stationary phase to separate a mixture of D- and L-serine, the resolution achieved was 1.765, demonstrating high chiral separation efficiency. The high adsorption selectivity for the novel imprinted material might result from the synergistic effect of deep eutectic solvent with macromolecular crowding reagent during the preparation of the imprinted materials. One hand, deep eutectic solvent can stabilize the zwitterionic form of D-Serine ( + H 3 N-CH(CH 2 OH)-COO - ) and hence enhance the ionic interactions between the template and functional monomers and the stability of template-functional monomer complexes; on the other hand, crowding agents significantly improved the binding efficiency between the functional monomer and the template molecules during the pre-assembly stage through the "excluded volume effect". This synergy promotes to form higher density and more precise specific recognition sites during the synthesis of the imprinted polymer and to improve the adsorption selectivity of the material obtained.
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FOOD RESEARCH INTERNATIONAL
·
2026
·
IF 8.8
Qianqian Wang,Yue Zhang,Zirui Xu,Yingwu Su,Xinyu Fu,Xiao Guan,Sen Li
Mannose-glycosylated soy peptide nanoparticles were developed for vitexin delivery. • Vitexin was amorphously encapsulated with a high efficiency over 94%. • M-SPAV regulated the polarization of macrophage via targeted delivery. • M-SPAV enhanced the cellular uptake of Vitexin and blocked the TLR4/MyD88/NF-κB signaling axis. • The system provides a novel oral delivery strategy for hydrophobic bioactives. Soy peptide aggregates (SPA) are the hydrolysate products of soy protein isolate, which possess good biocompatibility and self-assembly properties, making them excellent materials for nanocarriers. In this study, a green, food-grade nanocarrier based on mannose-modified soy peptide aggregates (M-SPAV) was developed for the efficient encapsulation and targeted delivery of vitexin, a bioactive polyphenol, which has poor water solubility and low bioavailability. The mannose modification of the soy peptide aggregates was performed via a mild and feasible glycosylation method to achieve macrophage targeting. The results demonstrated that nanoparticles prepared at a mannose-to-soy protein aggregate mass ratio of 1:1 exhibited a minimum particle size of 142 nm and achieved an encapsulation efficiency as high as 93.46%. Notably, M-SPAV displayed excellent stability across a broad pH range (3.0–8.0), under high ionic strength conditions and prolonged storage, while effectively protecting vitexin and maintaining antioxidant capacity throughout simulated gastrointestinal digestion. Furthermore, mannose modification not only improved the physicochemical properties of the soy protein aggregates but also endowed the nanoparticles with specific macrophage-targeting capability through receptor recognition. This nanoparticle system substantially enhanced the cellular uptake efficiency of vitexin. Consequently, M-SPAV significantly reduced intracellular reactive oxygen species (ROS) levels in LPS-stimulated macrophages compared to free vitexin, and anti-inflammatory activity by inhibiting the TLR4 / MyD88 / NF-κB signaling axis and regulating macrophage polarization. In summary, M-SPAV provides a promising food-grade nanoplatform for precision immunomodulatory intervention in macrophage-associated inflammatory diseases. Download: Download high-res image (194KB) Download: Download full-size image
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FOOD HYDROCOLLOIDS
·
2026
·
IF 13.8
Yushi Wei,Hongtao Chen,Deming Gong,Xing Hu,Guowen Zhang
The study aimed to construct a microwave-modified peanut protein isolate (MPPI)–gallic acid (GA)–carrageenan (CG) (MPGC) ternary covalent conjugate, and systematically investigate the effects of glycation covalent modification on the conformation, functional properties and interfacial behavior of MPPI, with the goal of developing new emulsifiers exhibiting superior oil-water interfacial performance. Additionally, the environmental stability of emulsions formulated using the covalent conjugate was evaluated. The results showed that as the proportion of CG increased, the degree of covalent modification significantly enhanced. When the mass ratio of the MPPI-GA conjugates to CG was 1:4 (MPGC4), the grafting degree reached 28.72%. The covalent grafting of CG induced the unfolding of MPPI-GA conjugates structure (decreased β-sheet content and increased random coil content), leading to enhanced surface hydrophobicity and surface charge of the MPPI-GA conjugates. Analysis of oil-water interface characteristics revealed that the MPGC4 conjugates exhibited optimal wettability, significantly reducing the oil-water interfacial tension from 17.34 mN/m to 13.99 mN/m, and demonstrated greater rates of interfacial diffusion, penetration and rearrangement, forming a dense adsorption layer at the interface. The emulsifying activity and emulsion stability of the MPGC4 conjugates were increased to 143.98 m 2 /g and 405.60 min, respectively. When 1.5% (w/v) MPGC4 conjugate was applied to oil-in-water emulsions, the emulsion exhibited a significantly reduced particle size with a more uniform distribution, and excellent environmental stability. This study provides a theoretical basis for the development of novel high-performance plant protein-based emulsifiers.
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CHEMICAL ENGINEERING JOURNAL
·
2026
·
IF 12.5
Huiwen Zhang,Xia Zhang,Yue Ma,Yingnan Zhao,Rui-Qi Yao,Xinying Sun,Tonghui Wang,Beibei Xiao,Gao-Feng Han,Xing-You Lang,Qing Jiang
Cyanide-free electrosynthesis converts amino acids to nitriles with >90% FE. • Low-coordinated Ni sites promote NiOOH formation for decarboxylation–dehydrogenation. • Carbon radicals induce nitrogen lone-pair delocalization, facilitating N H cleavage. • Broad amino acid scope includes challenging aromatic substrates. Leveraging biomass for organic nitrogen synthesis can reduce dependency on fossil ammonia, streamline synthetic pathways, and decrease carbon footprint and contamination. However, the conversion is chemically disfavored owing to the competition with deamination, overoxidation, and crosslink. Herein, we report a novel electrochemical synthesis route for biomass-derived amino acid oxidation, using L-alanine as the representative example to produce acetonitrile with high selectivity in the electrolyte. Upon dynamic reconstruction, defect-rich NiO anchored on O-doped carbon interacts with carboxylate groups, thereby facilitating decarboxylation. The resulting carbon radical induces partial delocalization of the nitrogen lone pair electrons, which weakens the N H bond, ultimately promoting nitrile production. The optimized electrocatalyst delivers a Faradaic efficiency of up to 92.2% together with a high acetonitrile production rate of 580.1 mmol g cat −1 h −1 and excellent stability. Moreover, our strategy has proven to be applicable to multiple α-amino acids. This work reveals the fundamental mechanism of amino acid electrooxidation to nitriles and paves the way for green and sustainable nitrogen utilization. An electrochemical strategy to convert biomass-derived amino acids into value-added nitriles using low-coordinated Ni catalysts. The process initiates decarboxylation to generate carbon-centered radical, which reorganize the local C N bonding environment and lower the barrier for C N bond formation, providing a sustainable and cyanide-free route for nitrogen valorization from renewable feedstocks. Download: Download high-res image (72KB) Download: Download full-size image
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2026
·
IF 8.7
Kangdi Cao,Zhiyuan Yin,Ningfei Duan,Zhiguo Zhang
Wet-heating Maillard conjugation improved FPC solubility and stability. • CG and KGM induced distinct structural changes in Mucor FPC. • FPC-CG showed greater functional improvement than FPC-KGM. • The 20:3 FPC/polysaccharide ratio gave the best overall performance. Fungal protein concentrate (FPC) is a promising sustainable protein ingredient, but its poor solubility and limited interfacial stability restrict its food applications. In this study, Mucor-derived FPC was conjugated with cassia gum (CG) or konjac glucomannan (KGM) by wet-heating Maillard reaction at different mass ratios. Compared with native FPC and physical-mixture controls, both conjugates showed evident structural modification and improved functionality, with the best overall performance at an FPC/polysaccharide ratio of 20:3. At this ratio, the degree of glycation reached 38.86% for FPC-CG and 29.62% for FPC-KGM, while surface hydrophobicity decreased from 254.68 to 146.11 and 179.43, respectively. Intrinsic fluorescence showed red shifts from 315 nm to 318 nm (FPC-CG) and 319 nm (FPC-KGM), and ordered secondary structure decreased by 12.20% and 10.54%, respectively. These structural changes were associated with enhanced solubility, emulsifying properties, foam stability, water- and oil-holding capacities, and DPPH radical-scavenging activity. Overall, CG produced stronger improvements than KGM, indicating that polysaccharide structure is critical for designing functional fungal protein-polysaccharide conjugates.
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FOOD HYDROCOLLOIDS
·
2026
·
IF 13.8
Mengya Deng,Meng Niu,Yan Xu
The low solubility of rice glutelin (RG) leads to the poor solubility of rice protein as a whole, which significantly limits its application in liquid foods and protein-based functional ingredients. Therefore, developing efficient methods to enhance the solubility of RG is crucial for expanding the food applications of rice protein. In this study, homologous assembling combined with sonication was utilized to improve the solubility of RG, with assemblies constructed using RGs from japonica and indica rice at different ratios. The solubility, emulsifying, and foaming properties of the assemblies were evaluated. Additionally, the multi-level structures, molecular weight distributions, surface properties, and aggregation state of these assemblies were characterized in order to reveal the potential mechanism underlying the improved solubility of RG after homologous assembling and sonication. The solubility of RG increased up to 8 times after homologous assembling and sonication, while the emulsifying and foaming capacities increased up to 1 and 3 times, respectively, compared to natural RG. The two RGs tend to assemble through hydrophobic interaction (mainly) and electrostatic force, forming assemblies with more charged groups exposed on protein surface. The increased exposure of charged groups further induces strong repulsive forces among molecules, preventing protein aggregation and thereby enhancing water-solubility. With improved water-solubility, the assemblies were easier to be absorbed at water/oil or water/air interfaces, leading to enhanced emulsifying and foaming ability. This study may provide a reference for expanding the utilization of rice protein and other plant proteins with poor water-solubility in the food industry.
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LWT-FOOD SCIENCE AND TECHNOLOGY
·
2026
·
IF 7.1
Muguo Tang,Yan Zhou,Fa Li,Ruiping Li,Yifan Wang,Siyi Li,Jun Sheng,Liang Tao,Yang Tian
In this study, walnut protein isolate (WNPI) was glycosylated with maltodextrin (M) to prepare a glycosylated protein conjugate (WNPI-M) and its conformational and functional properties were comprehensively analyzed. Subsequently, WNPI-M was employed as a wall material to fabricate walnut oil microcapsules, and the impact of WNPI-M on microcapsule stability was systematically investigated. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and multiple spectroscopic techniques confirmed that glycosylation with M induced significant modifications in WNPI's molecular structure and morphology. The glycosylation profoundly enhanced WNPI's functional properties: solubility at neutral pH increased to 76.94%, emulsifying activity reached 18.16 m 2 /g, and emulsion stability was extended to 244.74 min. Concurrently, the antioxidant capacity of the conjugate was markedly improved. When applied to microencapsulation, WNPI-M demonstrated superior performance in solubility, moisture content, and storage stability of walnut oil microcapsules. These findings substantiate the potential of WNPI-M as a novel, clean-label, and “same-source” wall material for microencapsulation, providing a viable strategy for the high-value utilization of walnut processing by-products.
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Foods
·
2026
·Vol. 15
·期 15
·2580
·
IF 6
Qi Zhang,Mengyan Jian,Yali Wang,Zimeng Wei,Yuehui Wang,Xiaoyu Bao,Wenping Ding
Rice glutelin hydrolysates (RGHs) with different degrees of hydrolysis (DH) were prepared using papain, and the structural characterization, physicochemical stability, and antioxidant activity of RGH were analyzed. Results showed that RGH primarily consisted of low molecular weight (MW) peptides (<3 kDa), with hydrophobic/aromatic amino acid content increasing with DH. Higher DH level led to reduced average particle size and zeta potential of RGH. Structurally, as DH increased, a decrease in α-helix content alongside increased β-sheet/random coil ratios was observed in RGH, indicating a transition towards a more disordered structure in RGH. Furthermore, the antioxidant activity of RGH was significantly enhanced with the increase in DH, with RGH-18 showing the highest bioactivity. RGH maintained stability and antioxidant capacity under gastrointestinal digestion as well as various environmental stresses, including varying pH and temperatures, and the presence of metal ions. Cellular experiments demonstrated that RGH-18 alleviated H2O2-induced oxidative damage in HepG2 cells, likely by inhibiting Keap1 and activating Nrf2 via the Keap1/Nrf2 pathway. This study supports the potential of RGH as a functional ingredient and provides insights for targeted rice peptide production.
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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
·
2026
·Vol. 74
·期 28
·22149-22158
·
IF 6.7
Sun Ze-Rui,Xia Yu-Xin,Li Yi-Ran,Liu Li,Voglmeir Josef
The deacetylation of N -acetylglucosamine
(GlcNAc)
to glucosamine (GlcN) is a key step in enzymatic chitin valorization.
We identified a novel GlcNAc deacetylase (AbNGD) from Acinetobacter baumannii with high substrate specificity
and catalytic activity but poor thermal stability (half-life of 5.5
h at 37 ° C). Using the FireProt platform, we generated a combinatorial
mutant, AbNGD-M3 (T93P–C153T-A244M). Its optimal temperature
increased to 37 ° C, and its half-life reached 28.1 h (5.1-fold
improvement), while retaining 97% of wild-type catalytic efficiency
( k cat / K m =
3.4 mM –1 ·s –1 ). Site-directed
mutagenesis confirmed Asp54 and His160 as key catalytic residues.
Molecular dynamics simulations revealed that T93P reduces backbone
flexibility, C153T enhances β-sheet rigidity via hydrogen bonding,
and A244M improves hydrophobic packing by filling a core cavity. These
distal mutations collectively balance stability and activity. Substrate
channel analysis identified a likely transport pathway centered on
T1. This study expands the deacetylase repertoire and provides a framework
for engineering stable industrial enzymes.
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