Journal of Coatings Technology and Research
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2025
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IF 2.8
Ran Ke,Kang Fenghua,Zhou Wentao,Zhang Ziyuan,Li Yintao,He Zhiyu
The widely used indicator, 2-(5-bromo-2-pyridylazo)− 5-diethylaminophenol (Br-PADAP), can enable color tracing of radioactive contaminants when incorporated into strippable decontamination materials. However, its practical application is hindered by poor dispersion in aqueous substrates. To address this issue, this study prepared an amphiphilic diblock copolymer, PEA-b-PAA, using a one-pot synthesis method. Ethyl acrylate (EA) and acrylic acid (AA) were used as monomers, with S,S,S-trisulfanyl dibenzyl carbonate (DBTTC) serving as the initiator for reversible addition-fragmentation chain transfer (RAFT) polymerization. Test results demonstrated that block copolymers with EA:AA monomer ratios of 2:1, 1.5:1, and 1:1 effectively dispersed and stabilized the Br-PADAP indicator. Among these, the copolymer with a 1.5:1 monomer ratio, added at a concentration of 4%, improved the mechanical properties of the peelable decontamination material without compromising the color tracing function of Br-PADAP. This enhancement facilitates practical applications by enabling incorporation into aqueous peelable substrates, while maintaining the indicator’s color development mechanism. The resulting materials exhibit both effective decontamination and reliable color tracing capabilities.
研究领域:
高分子化学
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材料科学
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环境科学
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核技术
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产品关联
DOI
高影响因子
Food Bioscience
·
2022
·
IF 5.318
Mengqi Pei,Zifu Zhao,Song Chen,E.I. Reshetnik,S.L. Gribanova,Chun Li,Guofang Zhang,Libo Liu,Lin Zhao
Pea ( Pisum sativum L.) is an important source of plant proteins . However, the use of pea flour as a food ingredient is greatly limited due to its strong beany flavor. In this work, we investigated the effects of Lactobacillus rhamnosus L08 ( L. rhamnosus L08) fermentation on the physicochemical characteristics, amino acids composition and volatile flavor compounds of pea flour. We found that L. rhamnosus L08 had the probiotic potential of utilizing pea flour as fermentation substrate. L. rhamnosus L08 fermentation significantly increased the content of most amino acids , and total amino acid content increased from 222.18 mg/g at 0 h to 262.35 mg/g at 6 h. A total of 44 volatile compounds were identified in pea flour. L. rhamnosus L08 fermentation increased the variety of acids and esters, while reduced the unpleasant flavor such as nonanal , decanal , octanal , 1-hexanol and 2-ethyl-1-hexanol. The emulsifying stability and foam stability of pea flour were slightly enhanced during fermentation. Our results illustrate that lactic acid bacteria fermentation is a promising approach to eliminate undesirable aroma of pea flour. Moreover, this study provides theoretical support for the application of peas as high-quality protein source.
研究领域:
食品科学
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微生物学
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化学
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DOI
高影响因子
Foods
·
2025
·Vol. 14
·期 19
·3363
·
IF 5.1
Xiaoyue Zhang,Guozhi Ji,Yan Zhao,Bingyu Chen,Wenhui Li,Zimeng Guo,Shan He,András Koris,Xuchun Zhu,Zhishen Mu,Hongzhi Liu
Pea protein yogurt (PPY), as an alternative to traditional dairy yoghurt, has the advantages of being a green raw material, lactose cholesterol-free, and adaptable to the needs of lactose-intolerant people. PPY was prepared by fermenting a mixture of pea protein and water (1:10,w/v) supplemented with 5% fructose for 10 h after heat sterilisation. During fermentation, lactic acid bacteria metabolise pea protein to produce aldehydes and other aromatic compounds, imparting a unique sweet–sour balance and mellow flavour. However, issues such as weak gel formation and prominent soybean-like off-flavours severely restrict the development and consumer acceptance of PPY. In this study, five fermentation systems were systematically investigated to elucidate the fermentation mechanisms of pea yoghurt and explore effective methods for eliminating undesirable soy flavours. The results indicated that hydrophobic interactions and disulfide bonds are the predominant forces driving gel formation in PPY. Additionally, the protein content increased by 0.81 g/100 g following fermentation. A total of 43 volatile flavour compounds—including aldehydes, alcohols, acids, ketones, and furans—were identified, among which the concentrations of hexanal and 2-pentylfuran, known markers for soybean off-flavour, significantly decreased. Furthermore, high-temperature and high-pressure treatments (121 °C, 3 min) demonstrated superior effectiveness in reducing soybean-like flavours. Although the high-temperature and high-pressure treatment, double-enzyme hydrolysis, and flavour-masking methods operate through distinct mechanisms, their flavour profiles converged, displaying substantial deodorisation effects and synergistic interactions. These findings provide a theoretical basis and processing parameters for flavour modulation in PPY; however, further formulation optimisation is required to enhance its nutritional and textural properties. PPY shows promise as a potential alternative to conventional dairy products in the future.
研究领域:
食品科学
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蛋白质化学
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发酵工程
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食品风味化学
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植物基食品
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产品关联
DOI
PubMed
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2026
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IF 8.7
Jieyao Chen,Jiaxing Xie,Pei Chen,Lingyun Chen,Weijuan Huang
While plant protein-based emulsion gels have attracted widespread attention, their physical stability remains a challenge. To address this, we improved the physical stability of pea protein isolate (PPI) emulsion gels through the incorporation of tea saponin (TS). Emulsion gels were fabricated by crosslinking PPI-TS complex emulsions with calcium ions. The PPI-TS/Ca 2+ emulsion gel exhibited a higher storage modulus and superior physical stability than the PPI/Ca 2+ emulsion gel (i.e., 5.0% PPI and 6 mM Ca 2+ ). Increasing the concentration of both PPI and calcium ions led to a more compact gel structure, enhanced gel elasticity and physical stability. Moreover, the structural changes in PPI induced by TS were examined. The increase in free sulfhydryl content, surface hydrophobicity, and intrinsic fluorescence intensity indicated that tea saponin promoted the unfolding of PPI. This unfolding exposed hydrophobic groups, and the addition of calcium ions facilitated the cross-linking of PPI, thereby enhancing the hydrophobic interactions within the protein molecules. These structural modifications facilitated stronger hydrophobic interactions and more efficient cross-linking between protein molecules upon calcium ions addition, ultimately leading to a denser and more robust gel network with improved physical stability. These findings present a promising strategy for the development of stable emulsion gel-based products.
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产品关联
DOI
PubMed
高影响因子
FOOD HYDROCOLLOIDS
·
2019
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IF 5.839
Yue Wei,Zhixiang Cai,Min Wu,Yalong Guo,Ran Tao,Ruiqi Li,Pengguang Wang,Aiqin Ma,Hongbin Zhang
The utilization of pea protein as an alternative to animal proteins for the production protein fortified foods and beverage products has recently gained tremendous interest due to the quality and health benefits associated with pea proteins. However, its use in food systems is often limited by technical issues such as the stability of pea protein dispersions (PPD). The objective of this study was to improve the physical stability of PPD by using corn fiber gum (CFG), high-methoxy pectin (HMP), carboxymethyl cellulose (CMC), and konjac glucomannan (KGM). The stabilization mechanism of PPD by these four different polysaccharides was investigated at native pH (roughly 5.5–7.5) and acidified pH (ca. 3.5) using particle size, zeta potential , rheological and physical stability evaluations. All four polysaccharides effectively improved the stability of PPD at various levels, but the physical stability of PPD was highly dependent on the type and concentration of the polysaccharides as well as the pH. Electrostatic repulsion, steric hindrance and the high viscosity of continuous phase were the main contributions to the improvement in PPD stability. Overall, these results have significant implications for the development of protein-based beverages with improved physical stability. The findings derived from this research can provide valuable information that may increase the utilization of pea protein in the food industry.
研究领域:
食品科学
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生物化学
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DOI
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
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2020
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IF 4.006
Qiaozhen Liu,Yangyong Dai,Hanxue Hou,Wentao Wang,Xiuzhen Ding,Hui Zhang,Xiangyang Li,Haizhou Dong
The aim of this paper is to expand application scope of pea protein isolate by improving its emulsification . Pea protein isolate was ground for different time, and changes in its structure and emulsification properties were studied, and then revealed the influence mechanism of grinding on emulsification. It was found that the β-sheet of protein decreased from 39.92% to 31.47% after grinding for 20 min, and the pea protein was converted from a solid ball to a hollow ball. So the emulsion flocculation index decreased from 1.01% to 0.29% and the amount of protein adsorbed increased by 4.5%, which showed that the emulsion stability of the pea protein was significantly improved. Within a short grinding time (2.5–5 min), the viscosity of the emulsion was increased. Studies had shown that proper grinding treatment made pea protein isolate possess greater potential for an excellent emulsifier.
研究领域:
食品科学
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蛋白质化学
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产品关联
DOI
高影响因子
CHEMICAL ENGINEERING SCIENCE
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2021
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IF 4.311
Xuesong Jiang,Jian Shi,Chen Chen,Wangfeng Song,Boyuan Ban,Jingwei Li,Anshu Wang,Jian Chen
In this study, the flotation behavior and adsorption mechanism of quartz flotation using poly (propylene glycol) bis (2-aminopropyl ether) (PEA) with different carbon chain lengths as collectors were studied. The mineral properties and adsorption mechanism were analyzed using XRD, ICP-OES, FTIR, and XPS tests. The results show that the water solubility of the collector is negatively related to the chain length. The insertion of the ether bonds (C─O─C) and the two amine groups (─NH 2 ) improve the water solubility of PEA. Their collection capacity is proportional to the chain length and the insertion of the ether bonds hardly affects their collection capacity. PEA is attached to the quartz surface mainly by electrostatic adsorption, and to a less extent by hydrogen bond adsorption. Based on the above results, PEA-D400 can be used as a collector to separate low-grade quartz into products of different purity levels.
研究领域:
矿物加工工程
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表面化学
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产品关联
DOI
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
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2022
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IF 8.025
Weibo Zhang,Shucheng Zhang,Chong Chen,Ning Liu,Dong Yang,Pengjie Wang,Fazheng Ren
Pea albumin (PA) can reach the intestine in the active form because it is highly resistant to gastric acid and proteolytic enzymes after their oral intake, which can supply various bioactivities. However, there is no detailed knowledge of the intestinal cell uptake about PA. The aim of this work was to study the internalization mechanism and intracellular trafficking route of PA. The uptake of PA-cyanine 5.5 NHS ester (Cy5.5) was a time-dependent and concentration-dependent process in Caco-2 cells. Endocytosis inhibitors or small interfering RNA (siRNA) techniques revealed that the internalization of PA-Cy5.5 was energy-dependent and mediated by caveolin-mediated endocytosis. Furthermore, we observed colocalization of PA-Cy5.5 and its subcellular localization in Caco-2 cells by using confocal laser scanning microscopy, which revealed that the intracellular trafficking process of PA-Cy5.5 was related to endoplasmic reticulum, Golgi, and lysosome. Interestingly, PA can alleviate lipopolysaccharide -induced ER stress, which may be the main reason why pea albumin is anti-inflammatory. Overall, our findings suggest caveolin may be critical for PA uptake in enterocytes and could contribute to explore the bioactivities mechanism of pea albumin in body.
研究领域:
营养学
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细胞生物学
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分子生物学
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产品关联
DOI
PubMed
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2023
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IF 8.2
Qian Shen,Wei Zheng,Fei Han,Jun Dai,Rong Song,Jing Li,Yan Li,Bin Li,Yijie Chen
Proteins and low-molecular-weight (LMW) surfactants are widely used for the physical stabilization of many emulsion-based food products. This study investigated the oil-water interfacial behavior between pea protein isolate (PPI) and phospholipid (PL). The emulsions prepared with different concentrations of PPI and PL were stabilized by their synergetic or competitive adsorption at the oil-water interface. In addition, the quantitative proteomics results could illustrate the displacements of proteins by PL. The result showed that the vicilin (7S) could be preferentially displaced by PL. Meanwhile, the results of quartz crystal microbalance with dissipation (QCM-D) indicated the high affinity of legumin (11S) with PL, suggesting that the legumin possessed higher interfacial affinity to prevent interfacial displacement. This research could help us to understand the interaction and competitive adsorption between plant proteins and LMW surfactants profoundly, which could promote the development of plant protein-based emulsion beverage with improved stability.
研究领域:
食品科学
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界面化学
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植物蛋白研究
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产品关联
DOI
PubMed
高影响因子
CHEMICAL RESEARCH IN CHINESE UNIVERSITIES
·
2022
·Vol. 38
·期 4
·1111-1117
·
IF 2.726
Zhang Xiangyu,Bai Shan,Zang Leilei,Chen Xiaoqi,Yuan Xiaoyan
With adjustable amphiphilicity and anionic/cationic charge, biodegradability and biocompatibility, amino acid-based poly(ester amide)s(PEAs) have drawn attention in the research of tissue engineered vascular grafts. In this work, L -phenylalanine-based PEAs with or without L -lysine were synthesized through polycondensation, and ultrafine fibrous grafts consisted of PEAs and poly( ε -caprolactone)(PCL) in given mass ratios were further prepared via blend electrospinning. Surface characterizations by Fourier transform infrared spectroscopy and X-ray photoelectron spectroscopy confirmed the chemical structure, and the wettability indicated that the prepared PCL/PEAs electrospun membranes exhibited less hydrophobic than PCL. Tensile results showed that the PCL/PEAs membranes possessed suitable mechanical properties, which could meet the requirements of artificial blood vessels. Cell culture and hemolytic tests exhibited that the PCL/PEAs electrospun membranes are biocompatible. In general, the electrospun grafts of PCL/PEAs could be applied for vascular repair.
研究领域:
组织工程
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生物材料
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生物医学工程
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材料科学
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产品关联
DOI
高影响因子
Foods
·
2022
·Vol. 11
·期 18
·2895
·
IF 5.561
Shuang Han,Fengzhan Cui,David Julian McClements,Xingfeng Xu,Cuicui Ma,Yutang Wang,Xuebo Liu,Fuguo Liu
HighlightsPea protein isolate (PPI) and EGCG spontaneously formed complexes.Protein–polyphenol complexation was mainly driven by hydrogen bonding.The binding of EGCG influenced the structure and functionality of PPI.PPI-EGCG complexes had better emulsifier properties than PPI.AbstractThere is increasing interest in using plant-derived proteins in foods and beverages for environmental, health, and ethical reasons. However, the inherent physicochemical properties and functional performance of many plant proteins limit their widespread application. Here, we prepared pea protein isolate (PPI) dispersions using a combined pH-shift/heat treatment method, and then, prepared PPI-epigallocatechin-3-gallate (EGCG) complexes under neutral conditions. Spectroscopy, calorimetry, molecular docking, and light scattering analysis demonstrated that the molecular complexes formed spontaneously. This was primarily ascribed to hydrogen bonds and van der Waals forces. The complexation of EGCG caused changes in the secondary structure of PPI, including the reduction in the α-helix and increase in the β-sheet and disordered regions. These changes slightly decreased the thermal stability of the protein. With the accretion of EGCG, the hydrophilicity of the complexes increased significantly, which improved the functional attributes of the protein. Optimization of the PPI-to-EGCG ratio led to the complexes having better foaming and emulsifying properties than the protein alone. This study could broaden the utilization of pea proteins as functional ingredients in foods. Moreover, protein–polyphenol complexes can be used as multifunctional ingredients, such as antioxidants or nutraceutical emulsifiers.
研究领域:
食品科学
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生物化学
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DOI
高影响因子
Materials Chemistry Frontiers
·
2020
·Vol. 5
·期 2
·937-943
·
IF 6.788
Xupeng Gao,Xinyu Shen,Dingke Xue,Xin Li,Po Lu,Min Lu,Chunyan Li,William W. Yu,Xue Bai
Two-dimensional (2D) perovskites have become a research hotspot due to their large exciton binding energy and excellent stability. However, it is difficult to achieve longer wavelength emission than blue and green light in the 2D perovskites owing to their wide band gap resulting from their strong quantum confinement. Herein, we demonstrate a simple, efficient and low energy consumption crystallization method at room temperature to synthesize Mn2+ ion doped 2D (PEA)2PbBr4 nanocrystals (NCs) with dual-color emission centered at 410 nm from the exciton transition of the host and 600 nm from the d–d transition of Mn2+ ions. The periodic XRD peaks prove the formation of 2D perovskites. It is reassuring that the high PLQY of 54% has been achieved in the Mn2+ ion doped 2D (PEA)2PbBr4 NCs. The temperature-dependent and time-resolved spectra illustrate the efficient energy transfer from excitons to Mn2+ dopant ions. The realization of white LEDs with different color temperatures presents an opportunity and prospect for Mn2+ ion doped 2D perovskites in LED application.
研究领域:
材料科学
·
光学
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DOI
高影响因子
危险品化学品经营许可证（带存储）