ACS Biomaterials Science & Engineering
·
2021
·
IF 4.749
Zhenjie Zhang,Xiaoyan Niu,Xiaoyue Feng,Xiaohui Wang,Licheng Yu,Wei Wang,Zhi Yuan
The method of tumor microenvironment (TME)-responsive aggregation has become a promising approach to enhance treatment effect by improving the accumulation of nanoparticles in tumors. The enzymatic cross-linking strategy has widely attracted attention owing to its good aggregation stability and biocompatibility. However, the enzymes in nontumor tissue can also catalyze the cross-linking reaction and reduce accumulation of nanoparticles in tumor. In this work, a “dual key”-responsive strategy is utilized to construct a transglutaminase (TGase)/pH-responsive radiosensitizer (Au@TAcoGal) with specific aggregation behavior in hepatic tumor cells. Au@TAcoGal can retain its stability in blood circulation (pH 7.4) even in the presence of TGase in plasma. On reaching tumor sites, it can be endocytosed by hepatoma cells by the active targeting of phenylboronic acid (PBA) and aggregated under acidity and overexpression of TGase in cells. Due to its specific accumulation in hepatoma cells, radiotherapy can be operated under a lower dose of X-ray. The results show that the cellular accumulation of Au@TAcoGal increases by 30–70%, and the cell survival rate is less than 25% under X-ray irradiation. The antineoplastic results show that Au@TAcoGal exhibits a higher therapeutic effect, and the tumor inhibition rate can reach 84.21%.
研究领域:
纳米技术
·
癌症研究
·
生物医学工程
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产品关联
DOI
PubMed
高影响因子
Food and Bioprocess Technology
·
2023
·Vol. 17
·期 1
·245-256
·
IF 5.6
Dong Mengxue,Sun Yusha,Xiong Dandan,Song Qi,jia Jie,Liu Xuebo,Sheng Long,Duan Xiang
Wheat gluten protein (WGP) is a fine-quality plant-based protein resource. However, as its unparalleled reticulation structure, the processing properties of WGP are extremely poor, limiting its application. To overcome these drawbacks, the purpose of this work was to embellish wheat gluten protein by three relatively novel and mainstream chemical modifications. The results showed the pH-shifting treatment altered the apparent morphology of protein, showing a uniform flocculent structure, leading to significant improvements in foaming capacity and emulsification property. After deamidation by acetic acid, the solubility of WGP was greatly improved (60.1%), which was nearly four times that of the control group (15.8%), and its foam stability was also significantly improved. The WGP had the highest thermal stability (deformation temperature up to 148 ℃) after TGase deamidation. These results indicate that the three modification methods enhance the functional characters of WGP in different aspects and expand its application potential.
研究领域:
食品科学
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蛋白质化学
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化学修饰
·
生物技术
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DOI
高影响因子
TEXTILE RESEARCH JOURNAL
·
2021
·
IF 1.82
Taotao Qiang,Yadong Pu,Qi Zhang
Down fiber – a natural and environmentally recyclable insulation material – is applied mainly in the area of natural-filled products. However, owing to its natural deficiencies of low fluffiness and thermal stability, large-scale application is limited. In our work, an enzyme preparation (transglutaminase (TGase)) was used as a fluffy agent to improve the fluffy degree of down. With fluffy as the main index, the single factor condition of only using TGase enzyme was optimized, and fluffiness was increased by 22%. On the basis of this optimum condition, the compound dosage of papain and TGase was further optimized. The fluffy degree of down was improved by hydrolysis of papain and crosslinking of TGase. Amino group content, thermogravimetry (TG), differential scanning calorimetry (DSC), moisture absorption, tensile strength, and elongation at break of down treated with different enzyme reagents were tested. The results showed that the thermal stability of down fiber treated with the multi enzyme increased significantly, the denaturation temperature was increased from 53.7°C to 77.4°C, and the moisture absorption was also improved. The elastic property also exhibited a great enhancement; elongation at break increased from 12.4% to 37.7%, nearly three times higher than the original property, and the tensile strength increased from 180 MPa to 370 MPa, almost 2.1 times as much as before, increased by 105.6%.
研究领域:
生物化学
·
材料科学
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DOI
高影响因子
Materials Chemistry Frontiers
·
2019
·Vol. 3
·期 7
·1365-1374
·
IF 0
Xuefeng Gao,Yang Liu,Yingying Li,Xiaoyan Niu,Jing Cao,Xiaomin Li,Yapei Zhang,Dongzhi Tan,Wei Wang,Zhi Yuan
Superparamagnetic iron oxides (SPIO) are attractive MRI contrast agents but suffer from limited sensitivity and low tumor specificity. In this study, two sets of SPIO nanoparticles (SPIONPs) were synthesized that were designed to selectively crosslink upon sensing transglutaminase (TGase), which is highly expressed at tumor site, thereby leading to the formation of SPIO nanocluster with T2 signal enhancement properties. For this purpose, SPIONPs with glutamine and lysine surfaces were synthesized. In vitro studies showed that the SPIONPs could crosslink to form aggregates with diameter of 1.3 μm in the presence of TGase and showed a 1.8 fold enhancement in r2 relaxivity compared with the dispersed state. The cellular uptake results illustrated that the SPIONPs could crosslink in high TGase expressing HeLa cells and showed an aggregation-induced retention effect compared with the controlled MCF-7 cell-line (about 1.9 fold). Simultaneously, the administration of the SPIONPs in the HeLa tumor-bearing mice verified the TGase-responsive aggregation and tumor enrichment of the nano contrast agent. MRI imaging also demonstrated the T2 signal enhancing ability of the TGase-responsive SPIONPs; the ΔT2 signal of the SPIONPs in the HeLa tumor-bearing group was about 2.3 fold higher than the MCF-7 group and the TGase-inhibitor treated group.
研究领域:
纳米技术
·
生物医学工程
·
医学成像
·
癌症研究
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DOI
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2026
·
IF 8.5
Chang Liu,Wanting Zhang,Meng Li,Jinjing Chen,Yiming Chen
This study primarily focuses on the utilization of Cyperus esculentus , which is mainly used for oil extraction. The Cyperus esculentus protein (CEP) hydrolysates glycosylated product was prepared under the mediation by transglutaminase (TGase) with glucosamine. Response surface methodology was used to optimize the preparation process for the glycosylated products, with the optimal conditions being a TGase addition of 21 U/g, a ratio of protein hydrolysate to glucosamine of 3:1, and a reaction time of 1.5 h.The degree of grafting for the glycosylated products was 40.72%. The glycosylation product prepared under this condition exhibited excellent emulsifying activity index (EAI 64.75 m 2 /g), which was slightly lower than the theoretical value of 66.15 m 2 /g. It can be attributed that the actual reaction time was longer than the theoretical time, and the slight rise in viscosity of the reaction mixture has caused some aggregation, leading to a minor reduction in the emulsifying property of the glycosylated product. Infrared spectroscopy, fluorescence spectroscopy, UV - visible absorption spectroscopy and NMR results indicated that the internal groups of Cyperus esculentus protein changed after enzymatic hydrolysis and glycosylation, confirming the occurrence of both processes. The thermal stability of the glycosylated products has been enhanced, and their antioxidant properties have also been improved. This study provided a new option of protein emulsifier based on plants and supplemented methods and theories for protein modification. The obtained glycosylated protein emulsifier has potential research value in applications of food processing, cosmetic manufacturing and drug encapsulation, etc.
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产品关联
DOI
PubMed
高影响因子
CARBOHYDRATE POLYMERS
·
2025
·
IF 12.5
Si-Jie Wu,Ran Feng,Ran Meng,Qiu-Ya Ji,Han Tao,Bao Zhang
To address the challenges of natural enzyme instability and mass transfer limitations in traditional immobilization techniques, this study proposes a sacrificial template strategy to develop cage-like nanogels (GNI-TG) that integrate efficient substrate transport with enzyme conformation protection, significantly enhancing enzyme stability and catalytic efficiency. The study employed methacrylated/quaternized dual-modified dextrin (MQD) to construct the continuous matrix of the nanogel, while designing Ca 2+ -ethylenediaminetetraacetic acid (EDTA) dynamic-responsive oxidized sodium alginate (OSA) as the sacrificial template. Structural analysis confirmed that the OSA and MQD formed a stable TG-protected structure through synergistic cross-linking mechanisms involving covalent Schiff base bonding and non-covalent interactions. GNI-TG retained 70 % of initial enzyme activity while demonstrating exceptional thermal stability (>50 % activity after 70 °C treatment) and broad pH adaptability (>70 % activity within pH 4–9). Leveraging polysaccharide-protein synergistic effects, GNI-TG significantly enhanced the comprehensive performance of whey protein/gelatin hydrogels. Compared to physically crosslinked and free TG crosslinked systems, CNI-TG crosslinked hydrogels exhibited superior gel strength (536.4 g), compressive strength (28.12 kPa), water-holding capacity (>99 %), thermal stability (T m = 138.4 °C), elastic behavior (G' > 1500 Pa), and network recovery (96.3 % recovery rate). This study establishes an enzyme immobilization paradigm through covalent anchoring, electrostatic assembly, and sacrificial templating strategies, demonstrating broad applicability in food processing, biocatalysis, and biomedical fields.
研究领域:
食品加工
·
生物催化
·
酶工程
·
纳米技术
·
高分子科学
·
生物医学工程
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产品关联
DOI
PubMed
高影响因子
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
·
2025
·
IF 3.5
Mingze Zhi,Yingshan Xie,Hongyan Li,Zeyuan Deng,Han Peng,Yanfang Yu,Bing Zhang
BACKGROUND Mulberry leaf protein (MLP) is a high-quality protein with significant nutritional value and functional properties. Enzymatic modification of proteins can enhance their functional properties by using proteases to covalently crosslink or hydrolyze proteins. This study investigates the potential of transglutaminase (TGase)-induced crosslinked MLP as an emulsifier in the formation of high-internal-phase Pickering emulsions. RESULTS Crosslinked MLP samples were prepared with TGase concentrations ranging from 0 to 25 U g −1 . High-internal-phase Pickering emulsions (80% v/v) were formed at pH 8, with a crosslinking temperature of 50 °C, a TGase concentration of 20 U g −1 and an optimal crosslinking time of 60 min. As the enzyme concentration increased, the content of exposed sulfhydryl groups progressively increased, while the total free sulfhydryl content remained relatively stable. After varying crosslinking durations, both total free and exposed sulfhydryl group contents initially increased before declining. Additionally, the content of free amino groups in MLP gradually decreased with higher enzyme dosages and longer crosslinking times. The surface hydrophobicity of crosslinked MLP increased initially, followed by a decrease, reflecting changes in the spatial structure of MLP. SDS-PAGE analysis confirmed the formation of polymer masses after TGase-catalyzed crosslinking. Under optimal crosslinking conditions, the high-internal-phase Pickering emulsion prepared with TGase-induced crosslinked MLP exhibited a relatively uniform droplet distribution. CONCLUSION TGase-induced crosslinking enhances both the emulsifying activity and stability of MLP emulsions. © 2025 Society of Chemical Industry.
研究领域:
食品科学
·
生物化学
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产品关联
DOI
PubMed
高影响因子
FOOD HYDROCOLLOIDS
·
2026
·
IF 13.8
Shufang Kang,Teng Zhang,Mengying Wu,Yong Han
To enable high-value utilization of yeast-derived protein, this study developed an ultrasonication-transglutaminase (TGase) synergistic modification strategy for yeast protein film (YPF), and systematically elucidated its structure-activity regulation mechanism, addressing the research gap in synergistic modification of yeast protein-based edible films. The core innovation is the discovery of the dose-dependent threshold effect of ultrasonication, which governs the dynamic balance between protein unfolding and TGase-mediated covalent cross-linking: low power (100 W) fails to effectively unfold protein and inhibits TGase activity, while excessive power (500 W) causes protein over-unfolding and slightly disrupts preformed cross-linking bonds. The optimal 300 W ultrasound unlocks protein conformations via cavitation and shear forces, exposes Gln/Lys cross-linking sites, and promotes ε-(γ-glutamyl)-lysine covalent bond formation, thus constructing a dense network dominated by hydrophobic interactions and stabilized by hydrogen bonds. Multiscale characterizations (ATR-FTIR, AFM, TGA, etc.) confirmed that optimized YPF has maximized strong-binding water content, significantly reduced water solubility and swelling degree, comprehensively improved thermal stability and light barrier property, along with retained excellent UV shielding performance. This strategy realizes high-value conversion of yeast-derived protein, and provides a novel technical route and molecular mechanistic basis for developing high-performance eco-friendly food packaging materials, with both scientific innovation and industrial application potential.
✓ 已验证
DOI
高影响因子
危险品化学品经营许可证（带存储）