International Journal of Biological Macromolecules最新文献

{"title":"Extremozymes for food fermentation: Integrating AI, metagenomics, and protein engineering.","authors":"Subuhi Kashif Ansari, Nusrat Hamid Shah, Noureddine Elboughdiri, Anis Ahmad Chaudhary, Mohamed A M Ali, Atif Khurshid Wani","doi":"10.1016/j.ijbiomac.2026.154351","DOIUrl":"https://doi.org/10.1016/j.ijbiomac.2026.154351","url":null,"abstract":"<p><p>Climate change-induced fluctuations in temperature, pH, salinity, and water activity are increasingly compromising microbial metabolism and fermentation efficiency, exposing the limitations of conventional mesophilic enzymes in maintaining process stability and product consistency. Extremozymes, derived from extremophilic microorganisms, exhibit exceptional structural stability and catalytic activity under harsh physicochemical conditions, making them promising biocatalysts for climate-resilient food fermentation. Although considerable progress has been achieved in extremozyme discovery and engineering, challenges remain in bridging computational prediction with experimental validation, functional characterization, large-scale production, and industrial deployment. This review critically examines the diversity, biochemical properties, and functional roles of extremozymes in food fermentation while evaluating the influence of climate-induced process stresses on microbial performance, enzyme functionality, and fermentation outcomes. It further synthesizes recent advances in Artificial Intelligence (AI)-assisted metagenomics, machine learning, transformer-based protein modelling, generative protein design, multi-omics (MO) integration, and high-throughput screening platforms, including microfluidics, droplet-based systems, and cell-free expression technologies, that are accelerating enzyme discovery, engineering, and validation. Particular emphasis is placed on the integration of computational and experimental workflows to improve the accuracy, scalability, and industrial translation of next-generation extremozymes. Unlike previous reviews that primarily describe individual enzyme classes or AI methodologies, this review provides a comprehensive and critical framework linking climate-driven fermentation challenges with emerging computational and biotechnological solutions. It identifies current knowledge gaps, technological bottlenecks, and future research priorities for developing robust, programmable, and energy-efficient fermentation systems capable of sustaining product quality, process reliability, and sustainable food production under increasingly variable environmental conditions.</p>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":" ","pages":"154351"},"PeriodicalIF":8.7,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148890462","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Valorization of wheat bran and corn husk via steam explosion for antioxidant starch/poly(butylene adipate-co-terephthalate) packaging.","authors":"Lin Yao, Shan Gao, YuanZhe Hou, Arif Rashid, Hanxue Hou","doi":"10.1016/j.ijbiomac.2026.154357","DOIUrl":"https://doi.org/10.1016/j.ijbiomac.2026.154357","url":null,"abstract":"<p><p>Guided by the Field-Film-Field (F-F-F) eco-circular strategy, in which agricultural by-products from the field are converted into functional films and ultimately returned to the field as biodegradable mulch, this study investigated the effects of incorporating steam-explosion-modified wheat bran and corn husk into starch/PBAT films. The results demonstrated that the incorporation of these biomass fillers, even at low loading levels, effectively enhanced the mechanical properties, water resistance, and gas barrier performance of the films. Compared with the control, the film containing 1% (w/w) corn husk exhibited the best overall mechanical performance, with tensile strength and elongation at break increasing by 11.9% and 12.0%, respectively, while the water contact angle increased from 72° to 88°. In contrast, films containing 5% (w/w) biomass fillers displayed excellent gas barrier performance and antioxidant activity. In a fresh-cut potato packaging trial, the active films reduced the peak activity of polyphenol oxidase (PPO) by 20%, effectively retarding enzymatic browning and helping maintain sensory quality. Furthermore, soil germination experiments with tobacco seeds indicated that the film degradation products exhibited no phytotoxicity and showed potential to serve as a \"carbon fertilizer\" that promotes seedling growth. Overall, this study demonstrates the feasibility of an F-F-F closed-loop utilization strategy for agricultural by-products, providing a promising technical pathway for the development of low-cost, biodegradable, and functional food packaging materials.</p>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":" ","pages":"154357"},"PeriodicalIF":8.7,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148890540","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bioactive macromolecules in LAB-fermented cereals: Mechanisms of formation, functional properties, and health benefits.","authors":"Adyasa Barik, Hui-Wen Lin, Chen-Che Hsieh, Yuwen Ting, Ali Demirci, Shella Permatasari Santoso, Chang-Wei Hsieh, Jheng-Jhe Lu, Kuan-Chen Cheng","doi":"10.1016/j.ijbiomac.2026.154349","DOIUrl":"https://doi.org/10.1016/j.ijbiomac.2026.154349","url":null,"abstract":"<p><p>Cereal and pseudo-cereal based fermented food products represent a substantial segment of global diet, nutrition as well as food security. Fermentation, especially by Lactic Acid Bacteria (LAB) increases the nutritional and functional values of foods by increasing palatability, bioavailability and minimizing antinutritional factors. LAB plays a pivotal role in synthesizing bioactive peptides, vitamins, minerals and reducing anti-nutrients parallelly. This review elucidates the mechanism through which LAB revamping nutritional macromolecules, such as peptides and polysaccharides, during fermentation and their role in the development of traditional as well as modern fermented foods. Additionally, these fermented foods have been associated with several health benefits. Recent advancement in biotechnology such as genome sequencing, functional genomics, and AI-assisted bioinformatics, have significantly enhanced our understanding of the diversity of LAB, the metabolism, and adaptation mechanisms. The combination of in silico and experimental methods has enabled the development of novel food enzymes as well as highly precise fermentation processes. Together with new innovations, growing demands for quality, consistency, safety as well as health benefits point out the significance of continued research. More studies employing both conventional and modern methods are necessary to explore these food groups completely and achieve better food quality, increased nutrition, more health benefits and comprehensive socioeconomic advantages.</p>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":" ","pages":"154349"},"PeriodicalIF":8.7,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148890455","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Polysaccharides from Sargassum fusiforme attenuate UV-induced skin photoaging via epidermal repair and dermal matrix reconstruction.","authors":"Yifan Chen, Lijuan Deng, Lijun You, Dongxiao Sun-Waterhouse","doi":"10.1016/j.ijbiomac.2026.154356","DOIUrl":"https://doi.org/10.1016/j.ijbiomac.2026.154356","url":null,"abstract":"<p><p>Skin photoaging is a multifaceted dermatological disorder induced by extrinsic influences (mainly excessive/prolonged exposure to ultraviolet (UV) radiation and intrinsic factors (e.g. oxidative stress), involving progressive disruption of epidermal homeostasis and dermal extracellular matrix (ECM) integrity. This study aimed to systematically evaluate the protective effects of polysaccharides from Sargassum fusiforme (DSFP-45) against UV-induced epidermal and dermal photoaging using UVB-irradiated HaCaT cells and UVA-irradiated HSF cells at concentrations of 125-500 μg/mL, and UVA + UVB-irradiated BALB/c nude mice at oral doses of 100-200 mg/kg/day. Results showed that DSFP-45 effectively alleviated UVB-induced oxidative stress, with intracellular ROS levels reduced by approximately 75% compared with the Model group, while attenuating DNA damage, inflammatory responses, keratinocyte-derived pro-melanogenic signaling pathways and improving skin barrier function in epidermal cells. In dermal fibroblasts, DSFP-45 preserved redox balance, reduced cellular senescence, and suppressed matrix metalloproteinase expression, with MMPs expression reduced by approximately 30%-50% compared with the Model group, thereby preserving ECM homeostasis. In vivo results further confirmed protective effects of DSFP-45 against UV-induced skin damage. DSFP-45 markedly preserved skin structural integrity, reducing UV-induced epidermal thickness by approximately 50% compared with the Model group, while alleviating dermal matrix loss and preserving collagen content in photoaged mice. Accordingly, DSFP-45 effectively attenuated UV-induced skin structural abnormalities and helped preserve skin architecture during photoaging, indicating its potential as a marine-derived functional ingredient for skin health.</p>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":" ","pages":"154356"},"PeriodicalIF":8.7,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148890638","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Heat-moisture treatment-induced starch-protein structural reorganization in whole highland barley flour regulates noodle quality and starch digestibility.","authors":"Ruihao Zheng, Hui Zhang, Hongying Hua, Yan Zhang, Ge Li, Chengming Jin, Jia Tang, Ling Zhu","doi":"10.1016/j.ijbiomac.2026.154361","DOIUrl":"https://doi.org/10.1016/j.ijbiomac.2026.154361","url":null,"abstract":"<p><p>Whole highland barley flour (WHBF) has attracted increasing attention owing to its superior nutritional profile, but its poor processing properties limit its application in noodle production. This study investigated how temperature and moisture during heat-moisture treatment (HMT) regulate the structure of WHBF and consequently affect noodle quality and starch digestibility. HMT increased swelling power, solubility, and pasting stability of WHBF, while inducing minor changes in protein secondary structure. Starch structural order was enhanced at 80 °C but disrupted at 120 °C, and higher moisture intensified these structural changes. The results revealed that HMT promoted starch encapsulation within a more continuous protein network and improved water distribution, leading to reduced cooking loss, enhanced textural properties, and low starch digestibility. Overall, HMT at 100 °C and 25% moisture achieved the best performance, reducing cooking loss to 8.23%, increasing springiness to 0.856, breaking distance to 50.89 mm, and resistant starch to 41.46%. Pearson correlation analysis further showed that glutenin macropolymer was closely related to noodle quality attributes, whereas starch crystallinity was positively correlated with resistant starch formation. These findings provide new insights into HMT-induced structural reorganization of WHBF and support the development of high-quality, slow-digesting WHBF noodles.</p>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":" ","pages":"154361"},"PeriodicalIF":8.7,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148890500","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"An integrated engineering strategy enhances expression and activity of Pseudonocardia thermophila nitrile hydratase in Escherichia coli.","authors":"Xiaolin You, Yuqing Chen, Ziying Tan, Baoyi Huang, Tiansheng Lu, Wenbin Zhang, Yonghong Yu, Haihong Wang, Zhe Hu, Jincheng Ma","doi":"10.1016/j.ijbiomac.2026.154348","DOIUrl":"https://doi.org/10.1016/j.ijbiomac.2026.154348","url":null,"abstract":"<p><p>Nitrile hydratase is a key enzyme for nitrile-to-amide hydration under mild conditions, yet its application is limited by low heterologous expression, poor solubility, and suboptimal catalysis. Here, we present an integrated strategy to enhance expression, assembly, and function of Pseudonocardia thermophila NHase (PtNHase) in Escherichia coli, and dissect its mechanism via kinetic analysis. Codon optimization improved total whole-cell activity by 99% at 36 °C, likely through enhanced translational efficiency and co-translational folding at elevated temperatures. Replacing the native Shine-Dalgarno sequence with a strong RBS increased α-subunit expression 1.8-fold and boosted total whole-cell activity by 215%, outperforming solubilization tag and subunit fusion. Structure-guided saturation mutagenesis identified βTrp72 as a key specificity determinant. The βW72F variant increased apparent activity toward 3-cyanopyridine by 45% while retaining wild-type acrylonitrile activity. However, kinetic analysis revealed that βW72F has lower intrinsic catalytic efficiency (kcat/Km 10.8 vs. 30.9 mM^-1·s^-1), and its apparent gain arises from relieved substrate inhibition at high substrate concentrations (Kᵢ of βW72F increased from 306.1 to 688.4 mM), rather than from enhanced intrinsic rate. This mutation exhibits a trade-off: enhanced activity and tolerance toward 3-cyanopyridine but reduced thermostability and nicotinamide tolerance. Computational analyses suggested that βW72F expands the substrate tunnel entrance (bottleneck radius 0.92 → 1.32 Å), optimizes CoN coordination (5.8 → 4.9 Å), but compromises thermostability due to increased backbone flexibility (RMSD 2.78 → 3.42 Å). This work establishes a high-efficiency expression system for PtNHase and highlights that apparent activity gain does not necessarily equate to improved intrinsic catalytic efficiency, providing a framework for engineering complex metalloenzymes.</p>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":" ","pages":"154348"},"PeriodicalIF":8.7,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148890570","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"An enzyme from Fusarium incarnatum exhibiting diglycosidase and α-L-rhamnosidase activities catalyses the biotransformation of naringin to naringenin.","authors":"Kunwar Vishal, Anuj Kumar, Vinita Yadav, Dinesh Kumar, Pramod K Yadav","doi":"10.1016/j.ijbiomac.2026.154355","DOIUrl":"https://doi.org/10.1016/j.ijbiomac.2026.154355","url":null,"abstract":"<p><p>This study reports the purification, characterization and biotransformation potential of a unique enzyme from a newly isolated fungal strain, Fusarium incarnatum exhibit dual diglycosidase and α-L-rhamnosidase activities. The enzyme was purified to homogeneity using ion-exchange and gel filtration chromatography. It exhibited maximal enzyme activity at 70 °C and pH 10. Steady state kinetic analysis using both natural and synthetic substrates revealed high substrate affinity and catalytic efficiency, as evidenced by the calculated k_cat/K_m values of 11.0 mM^-1 s^-1 and 18.7 mM^-1 s^-1 for naringin and p-nitrophenyl-α-L-rhamnopyranoside (pNPR), respectively. The purified enzyme catalyzed one step hydrolysis of naringin to naringenin, accompanied by the release of neohesperidose. The formation of both products was confirmed by LC-MS analysis, and the formation of neohesperidose was further validated by (1D) ¹H NMR analysis. This single step conversion indicates diglycosidase activity, distinguishing it from classical monoglycosidase activity of α-L-rhamnosidase. Such catalytic efficiency toward the α-L-rhamnosyl-(1 → 2)-β-d-glucose moiety in neohesperidose flavonoids highlights its potential for one-step biotransformation of naringin to naringenin.</p>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":" ","pages":"154355"},"PeriodicalIF":8.7,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148890620","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bioluminescence-based high-throughput screening and identification of direct-acting dengue virus NS5 methyltransferase inhibitors.","authors":"Chenchen Li, Jianfang Zhang, Yuegao Hu, Yanyang Su, Ni Liu, Zhang Zhang, Qinhai Ma, Zifeng Yang, Yingjun Li","doi":"10.1016/j.ijbiomac.2026.154293","DOIUrl":"https://doi.org/10.1016/j.ijbiomac.2026.154293","url":null,"abstract":"<p><p>Dengue virus (DENV) is a mosquito-borne orthoflavivirus that infects millions of people annually across tropical and subtropical regions, posing a severe and growing threat to global public health. Currently there are no antiviral drugs available for DENV infection. The methyltransferase domain of non-structural protein 5 (NS5 MTase) catalyzes two essential methylation reaction in synthesis of the 5' cap-1 structure of viral mRNA, making it a promising yet under-validated target for anti-DENV drug development. Herein, we optimized a bioluminescence-based enzymatic MTase-Glo assay using purified recombinant DENV NS5 MTase and performed high-throughput screening of the focused Methylation Compound Library. Four compounds-SGC0946, AMI-1, salirasib, and gambogenic acid-were identified as potent DENV methylation inhibitors effective against all four serotypes (DENV-1 to -4). Surface plasmon resonance (SPR) analysis confirmed the direct binding between inhibitors and NS5 MTase. Among them, SGC0946 exhibited the strongest inhibitory activity with a half-maximal inhibitory concentration (IC₅₀) of 0.05-0.11 μM against DENV-1 to -4. Molecular docking predicted that SGC0946 binds to the S-adenosylmethionine (SAM)-binding pocket of NS5 MTase. In addition, SGC0946 suppressed DENV replication in C6/36 and BHK-21 cells with EC50 values of 6.67 and 0.60 μM, respectively. Collectively, these findings identify novel DENV MTase inhibitors with diverse scaffolds and provide valuable molecular insights for the rational design of more potent NS5 MTase-targeting inhibitors in the future.</p>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":" ","pages":"154293"},"PeriodicalIF":8.7,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148890497","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural determinants of Mac1 inhibition: Lessons from ligand binding patterns.","authors":"Verena Weber, Sarah Knapp, Patricia Korn, Bernhard Lüscher, Giulia Rossetti","doi":"10.1016/j.ijbiomac.2026.154249","DOIUrl":"https://doi.org/10.1016/j.ijbiomac.2026.154249","url":null,"abstract":"<p><p>This study comprehensively analyzes how various inhibitors bind to the SARS-CoV-2 macrodomain Mac1, a key protein implicated in hampering the host's immune response following viral infection. In this study we used volume-based metadynamics simulations to investigate the binding mechanisms of ADP-ribose and two Mac1 inhibitors: the adenine-analogue GS-441524 and the non-adenine-analogue S09. By combining free-energy simulations with a bioinformatic analysis, we aimed at determining whether the binding patterns observed for the selected ligands can be generalized across Mac1 inhibitors and can be exploited to guide a rational design for future therapeutics. Our simulations show the pivotal role of the adenosine moiety in Mac1 recognition. However, for small molecules, like S09 and GS-441524, the oxyanion hole also emerged as an alternative and essential stabilizing region. This site, which preferentially accommodates electronegative groups, is engaged by approximately 76% of reported Mac1 inhibitors, making it a key target for Mac1 inhibition. In addition, we demonstrate that the unstructured loops 1 and 2 shape ligand entry, with loop 2 functioning as a dynamic gateway. Within this loop, Leu126, part of the virus-specific P-L-L-S motif, serves as a key anchoring residue for potent inhibitors. Collectively, these findings suggest that targeting both the oxyanion hole and Leu126 may enhance both the specificity and affinity of next-generation Mac1 inhibitors.</p>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":" ","pages":"154249"},"PeriodicalIF":8.7,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148890622","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Systematic rheological investigation of chitosan-modified magnetite-reinforced thermosensitive Pluronic F127/chitosan hybrid hydrogels.","authors":"V S Aiswarya Gowri, Karolinekersin Enoch, Anbumozhi Angayarkanni Somasundaram","doi":"10.1016/j.ijbiomac.2026.154346","DOIUrl":"https://doi.org/10.1016/j.ijbiomac.2026.154346","url":null,"abstract":"<p><p>Polymer-modified magnetite nanoparticles hold great promise for diverse biomedical applications, including drug delivery, magnetic hyperthermia, and tissue engineering. However, ensuring their long-term functionality and stability for in vivo applications remains a significant challenge. In this work, chitosan-modified magnetite nanoparticles of different concentrations (0-4% w/v) were incorporated into a Pluronic F127/chitosan thermosensitive hydrogel matrix. All hydrogel formulations exhibited a temperature-induced sol-gel transition in the range of 27-28.94 °C, with viscosity increasing with increasing temperature, confirming their thermoresponsive behaviour. Furthermore, all the hydrogels displayed non-Newtonian shear-thinning behaviour. Incorporation of 4% (w/v) chitosan-modified magnetite nanoparticles into the neat hydrogel enhanced the viscosity and yield stress by 28% and 56%, respectively. The storage modulus exceeded the loss modulus for all hydrogels across the oscillatory strain range within the linear viscoelastic region and over the entire frequency range with no crossover points, validating their structural integrity and suitability for long-term in vivo applications. Thixotropic studies revealed excellent structural recovery in these hydrogels upon removal of the applied shear stress. These rheological findings position chitosan-modified, magnetite-incorporated thermoresponsive hydrogels as a structurally resilient and stable system that exhibits both magnetic and thermoresponsive behaviour, making them suitable for multifunctional biomedical applications such as magnetic hyperthermia, targeted drug delivery, and regenerative medicine.</p>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":" ","pages":"154346"},"PeriodicalIF":8.7,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148890576","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}