{"title":"Pulsed electric field modulates lactoferrin conformation to enhance quercetin binding and complex stability","authors":"Sijie Shan , Xinxin Xia , Youzhi Xu , Yanling Zeng , Jiali Ren , Guliang Yang","doi":"10.1016/j.ijbiomac.2026.152262","DOIUrl":"10.1016/j.ijbiomac.2026.152262","url":null,"abstract":"<div><div>Quercetin (QUE) is a natural flavonoid whose practical application is severely limited by poor aqueous solubility, environmental instability, and low oral bioavailability. Lactoferrin (LF), a generally recognized as safe (GRAS) glycoprotein, is a promising carrier for hydrophobic bioactives; however, its native compact globular structure causes significant steric hindrance, resulting in inefficient ligand binding. Herein, continuous-flow pulsed electric field (PEF) treatment was employed to modulate LF conformation, enhancing the binding efficiency and stability of LF-QUE complexes. The findings revealed that moderate PEF treatment (10 kV·cm<sup>−1</sup>) induced controlled unfolding of LF, exposing internal hydrophobic cavities and increasing QUE loading capacity by 40.2% compared with untreated LF. Excessive field intensities (≥15 kV·cm<sup>−1</sup>) triggered intermolecular disulfide cross-linking of LF, which masked specific binding sites and reduced loading performance. Multispectral analysis demonstrated that the LF10-QUE20 complex had the strongest binding affinity via a static quenching mechanism, with more binding sites than the native complex. The LF10-QUE20 complex exhibited superior colloidal dispersibility, thermal stability (denaturation temperature of 86.3 °C), and a 21.5% increase in the in vitro bioaccessibility of QUE, accompanied by a complete crystalline-to-amorphous transition of encapsulated QUE. Molecular simulations revealed that PEF treatment enhanced the binding stability of QUE to LF (binding energy: −9.0 kcal·mol<sup>−1</sup>) mainly via hydrogen bonding, van der Waals forces, π-cation, and π-alkyl interactions. Overall, this study presents a facile, non-thermal PEF strategy to optimize protein-based delivery systems for hydrophobic bioactives in functional food applications, avoiding irreversible protein denaturation and chemical residues associated with conventional thermal or chemical modification methods.</div></div>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":"364 ","pages":"Article 152262"},"PeriodicalIF":8.5,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147806906","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":"Bio-based photocatalytic self-cleaning superhydrophobic cotton fabric based on rosin acid/TiO₂: Efficient and recyclable application in oil-water separation","authors":"Yike Han , Zongxue Yu , Pengao Yu , Shuangshuang Xia , Jiao Chen , Chao Peng","doi":"10.1016/j.ijbiomac.2026.152234","DOIUrl":"10.1016/j.ijbiomac.2026.152234","url":null,"abstract":"<div><div>The utilization of superhydrophobic membrane materials in oil-water separation applications offers considerable promise; nevertheless, the durability and recyclability of conventional membranes remain unsatisfactory. In this study, rosin acid was used to modify nano-TiO₂ to achieve hydrophobicity, and a low-surface-energy substance, polydimethylsiloxane (PDMS), was introduced. Nanoparticles were loaded onto a cotton fabric substrate using a two-step dip-coating method, resulting in the successful construction of a uniform micro-nano rough structure. This resulted in the formation of a superhydrophobic-superoleophilic fabric membrane, RTP-cotton (WCA = 154.6°).Synergizing with TiO₂ photocatalysis, RTP-cotton achieves excellent self-cleaning performance within 20 min under light exposure after being fully dyed with 60 ppm of Oil Red O and Methylene Blue dyes; the water contact angle (WCA) of the contaminated RTP-cotton recovered to superhydrophobic levels from 145.1° and 141.2°, respectively, and the self-cleaning performance remained stable over five cycles. Furthermore, RTP-cotton demonstrates elevated chemical stability and exceptional mechanical properties. The membrane exhibited excellent separation performance for various of oil-water mixtures, achieving separation efficiencies that consistently surpassed 98% and attaining a maximum separation flux of 4793.3 L·m<sup>−2</sup>·h<sup>−1</sup>. Furthermore, it exhibited outstanding reusability, maintaining a separation efficiency of 96.5% after 50 separation cycles with a flux decay of less than 15%.</div></div>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":"364 ","pages":"Article 152234"},"PeriodicalIF":8.5,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147806921","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}
Xinxin Chen , Yiting Lin , Yue Yi , Mengyao Ma , Ruoqi Song , Ying Wang , Sheng Niu , Fang Yan , Xiaolong Gao , Yunjun Zhao , Wen-xia Tian , Jianle Ren
{"title":"Development and application of a novel multi-peptide indirect ELISA based on VP1/VP2/VP3 proteins for the antibody detection against Senecavirus A","authors":"Xinxin Chen , Yiting Lin , Yue Yi , Mengyao Ma , Ruoqi Song , Ying Wang , Sheng Niu , Fang Yan , Xiaolong Gao , Yunjun Zhao , Wen-xia Tian , Jianle Ren","doi":"10.1016/j.ijbiomac.2026.152287","DOIUrl":"10.1016/j.ijbiomac.2026.152287","url":null,"abstract":"<div><div>The newly emerged senecavirus A (SVA) has been identified as an important etiological agent of vesicular disease in pigs, posing a major threat to the global swine industry. The absence of licensed vaccines in China against SVA underscores the urgent need for reliable diagnostic tools to control SVA infections. In this study, twelve immunodominant peptides were screened from the VP1, VP2, and VP3 proteins of SVA. Subsequently, a multi-peptide fusion protein VP123 expressed in <em>Escherichia coli</em> was used to develop an indirect ELISA (iELISA) for SVA antibodies detection. This assay showed no cross-reactivity with serum antibodies against other common swine viruses, and exhibited remarkable reproducibility and stability. ROC analysis revealed AUC values of 0.955 (vs. IFA) and 0.973 (vs. VNT), with strong correlation to VNT (Spearman's <em>R</em> = 0.6998). When the iELISA was employed to detect SVA seroprevalence in large-scale pig farms in Shanxi Province, China, the results revealed that SVA was widely circulating in pig farms, with a positive rate of 81.95%. In conclusion, the novel iELISA features strong stability, specificity, and sensitivity. It holds great promise as a diagnostic tool for SVA infections and for monitoring antibody responses in pigs vaccinated with SVA vaccines.</div></div>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":"364 ","pages":"Article 152287"},"PeriodicalIF":8.5,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147807026","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}
Chuanfen Pu , Risheng Li , Chunxiao Wu , Qingjie Sun , Jiawen Fan , Man Li , Wenting Tang
{"title":"Composite hydrogels encapsulating soy oleosome-associated protein-modified liposomes: Effects of protein on gel texture and release attribute","authors":"Chuanfen Pu , Risheng Li , Chunxiao Wu , Qingjie Sun , Jiawen Fan , Man Li , Wenting Tang","doi":"10.1016/j.ijbiomac.2026.152269","DOIUrl":"10.1016/j.ijbiomac.2026.152269","url":null,"abstract":"<div><div>To address the challenge of poor environmental stability of liposomes, a composite gellan gum hydrogel encapsulating soy oleosome-associated protein (SOP)-modified liposomes was fabricated. Particle size, zeta-potential, spectroscopic analysis and morphological analysis confirmed that SOP was successfully anchored, with the particle size increased from 113.4 nm for bare liposomes to 128.5–137.3 nm for SOP-modified liposomes. An appropriate SOP inclusion amount (0.4 mg/mL) endowed the gel (SOP<sub>0.4</sub>-Lip-G) with desirable hardness, elasticity, and cohesiveness. Increasing SOP concentration (from 0.4 mg/mL to 0.8 mg/mL) resulted in a corresponding reduction in gel formation time from 3.68 min to 2.85 min. The gel structure formation was attributed to non-covalent interactions, including hydrogen bonding, hydrophobic effects, and electrostatic interactions. Luteolin encapsulation within the composite gel induced a transformation from a crystalline to an amorphous state. <em>In vitro</em> simulated digestion analysis demonstrated that the composite hydrogel exhibited enhanced sustained-release performance and improved luteolin bioavailability due to the hierarchical liposome-in-hydrogel system. SOP<sub>0.4</sub>-Lip-G also exhibited favorable pH, ionic strength, and storage stability. This work presents a tunable fabrication strategy for developing liposome-loaded composite hydrogel dietary supplements and nutraceuticals products with improved stability and bioavailability.</div></div>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":"364 ","pages":"Article 152269"},"PeriodicalIF":8.5,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147807128","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":"Complex coacervation of pea/soy protein, pectin and OSA-modified starch as carriers for EPA/DHA in soy milk-effervescent tablets: Simulated digestion and sensory attributes","authors":"Mojtaba Delfanian, Mohammad Hossein Azizi","doi":"10.1016/j.ijbiomac.2026.152257","DOIUrl":"10.1016/j.ijbiomac.2026.152257","url":null,"abstract":"<div><div>This study aimed to encapsulate eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) through complex coacervation using soy protein isolate, OSA-modified starch, pectin (SOP) and pea protein isolate, OSA-modified starch, pectin (POP). FTIR analysis indicated that fish oil was encapsulated within protein-polysaccharide microcapsules via hydrogen bonding, electrostatic, and hydrophobic interactions. The SOP microcapsules exhibited significantly lower percentage increases in hydroperoxide (1.15 vs.1.82 meq/kg), hexanal (2.06 vs. 2.78 ng/g) and propanal (18.35 vs. 24.58 ng/g) compounds, as well as lower EPA/DHA loss (6.6 vs.7.45%) compared to POP after 90 days of storage. SOP also showed favorable physical properties, including optimal moisture content (2.16%), water activity (0.18), and color, as well as high solubility (88.63%) and superior in vitro intestinal release (85.92%). In the second phase, SOP and POP microcapsules were incorporated into soy milk-effervescent tablets. SOP tablets showed enhanced oxidative stability, minimal EPA/DHA loss, and desirable physical characteristics over storage. In vitro digestion revealed efficient intestinal release of EPA/DHA from SOP tablets (90.33%), while POP tablets showed premature release in the gastric phase (69.41%). Preliminary sensory evaluation, supported by principal component analysis, indicated that SOP-based tablets exhibited more favorable sensory attributes compared to POP tablets (<em>p</em> < 0.05). These findings suggest that SOP microcapsules may serve as a promising delivery system for omega-3 s in plant-based effervescent tablets, with potential to improve stability, bioaccessibility, and consumer acceptance. With further studies on in vivo performance, scale-up, and stability, this system could be developed into an effective omega-3 effervescent tablet formulation.</div></div>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":"364 ","pages":"Article 152257"},"PeriodicalIF":8.5,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147758832","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}
Hengrong Jiang , Fajun Lai , Yong Zhou , Jingjing Zhang , Yangyang Hu , Meng Chen , Hui Sun , Chang Guan , Sen Nie , Fei Wang , Xian Li , Wenqiang Li , Lixin Ma
{"title":"A programmable pAgo DNase from Hydrogenophilus thermoluteolus guided by small DNA and RNA","authors":"Hengrong Jiang , Fajun Lai , Yong Zhou , Jingjing Zhang , Yangyang Hu , Meng Chen , Hui Sun , Chang Guan , Sen Nie , Fei Wang , Xian Li , Wenqiang Li , Lixin Ma","doi":"10.1016/j.ijbiomac.2026.152250","DOIUrl":"10.1016/j.ijbiomac.2026.152250","url":null,"abstract":"<div><div>Argonaute (Ago) proteins are programmable nucleases found in both eukaryotes and prokaryotes that use small nucleic acid guides to cleave complementary DNA or RNA targets. However, the limited catalytic efficiency and substrate versatility of currently characterized prokaryotic Argonautes (pAgos) have restricted their broader applications. Here, we characterized HthAgo, a pAgo from the thermophilic bacterium <em>Hydrogenophilus thermoluteolus</em>, and show that it possesses broad and precise nucleic acid cleavage activities. HthAgo efficiently cleaves DNA targets when loaded with 5′-phosphorylated DNA guides (5′P-gDNA), 5′-hydroxylated DNA guides (5′OH-gDNA), or 5′-phosphorylated RNA guides (5′P-gRNA), and also cleaves RNA targets when guided by 5′P-gDNA or 5′OH-gDNA. Remarkably, HthAgo maintains precise cleavage with both 5′P- and 5′OH-gDNA, with 5′P-guides directing canonical cleavage between guide positions 10 and 11, whereas 5′OH-guides shift cleavage exclusively to positions 11 and 12. Biochemical analyses showed that HthAgo remains active over a broad range of reaction conditions, displays optimal activity at 60–70 °C in the presence of Mn<sup>2+</sup>, and exhibits no apparent preference for the 5′-terminal nucleotide of the guide. Binding and thermal stability analyses further suggest that HthAgo preferentially utilizes DNA guides and DNA targets owing to their stronger binding affinity and higher complex stability. In addition, HthAgo enables efficient and accurate cleavage of double-stranded DNA at elevated temperature using paired DNA guides. Together, these findings expand the functional landscape of thermophilic pAgos and establish HthAgo as a promising programmable nuclease platform for versatile nucleic acid manipulation.</div></div>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":"364 ","pages":"Article 152250"},"PeriodicalIF":8.5,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147758839","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}
Wu Wang , Niels J. Nieuwenhuizen , Shijie Zhang , Yu Chen , Yuqiang Zhao , Cancan Zhu , Guoming Wang
{"title":"Enzymatic functions of CmPAL1 and CmPAL2 in Chinese chestnut (Castanea mollissima BL.): Key catalysts in powdery mildew resistance via MeJA signaling","authors":"Wu Wang , Niels J. Nieuwenhuizen , Shijie Zhang , Yu Chen , Yuqiang Zhao , Cancan Zhu , Guoming Wang","doi":"10.1016/j.ijbiomac.2026.152360","DOIUrl":"10.1016/j.ijbiomac.2026.152360","url":null,"abstract":"<div><div>Phenylalanine ammonia-lyase (PAL) is a key enzyme catalyzing the conversion of <em>L</em>-phenylalanine into trans-cinnamic acid and plays a crucial role in plant secondary metabolism and stress responses. However, the enzymatic functions of PAL proteins in Chinese chestnut remain largely unexplored. In this study, we characterized four CmPAL proteins encoded in the chestnut genome through phylogenetic analysis, chromosomal localization, protein structure, and promoter cis-element identification. Enzyme activity assays and transcript profiling revealed distinct expression patterns among the <em>CmPAL</em> genes, with <em>CmPAL1</em> showing the highest expression in roots, whereas <em>CmPAL2</em>, <em>CmPAL3</em>, and <em>CmPAL4</em> showed relatively high expression in old leaves and low expression in kernels. To validate their enzymatic functions, <em>CmPAL1</em> and <em>CmPAL2</em> were transiently overexpressed in <em>Nicotiana benthamiana</em> and heterologously expressed in <em>Escherichia coli</em> BL21. Both approaches confirmed their ability to catalyze the conversion of <em>L</em>-phenylalanine into trans-cinnamic acid. Additionally, enzyme activity and transcript levels of <em>CmPAL</em> genes were significantly induced under abiotic stresses (drought, cold, heat, and salt), hormonal treatments methyl jasmonate (MeJA) and salicylic acid (SA), and <em>Blumeria farreri</em> (Bf) infection. Notably, CmPAL activity and expression were significantly higher in Bf-infected samples treated with 10 mM MeJA than with either treatment alone, suggesting an additive effect in enhancing PAL-mediated defense responses. Overall, our findings indicate that <em>CmPAL1</em> and <em>CmPAL2</em> are involved in phenylpropanoid metabolism and may contribute to powdery mildew resistance through MeJA signaling.</div></div>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":"364 ","pages":"Article 152360"},"PeriodicalIF":8.5,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147831900","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}
Boyan Jin , Yapeng Liu , Chunfang Ma , Yuanyuan Sun , Linyi Zhou , Cuiping Han , Qingfeng Ban , Zengwang Guo , Zhongjiang Wang
{"title":"Investigation of the formation mechanism of the oxidized soybean protein/linoleic acid aggregates: Effect of heating treatment on the soybean protein emulsion structure, antioxidant properties and accessibility of vitamin D3","authors":"Boyan Jin , Yapeng Liu , Chunfang Ma , Yuanyuan Sun , Linyi Zhou , Cuiping Han , Qingfeng Ban , Zengwang Guo , Zhongjiang Wang","doi":"10.1016/j.ijbiomac.2026.151887","DOIUrl":"10.1016/j.ijbiomac.2026.151887","url":null,"abstract":"<div><div>The aim of this study was to investigate the effects of heating-induced conjugation between soybean protein isolate (SPI) and linoleic acid (LA) on the structural modifications of the protein, the antioxidant activity of the oxidized protein, and the bioaccessibility of vitamin D<sub>3</sub>. The results revealed that the LA facilitated the formation of oxidized soy protein aggregates, which demonstrated that the protein oxidation degree increased. The simultaneous rheology and fourier transform infrared spectroscopy measurements made an analysis of the structural changes of proteins caused by oxidation, the α-helix decreased and the β-fold increased, indicating that oxidation changed the structure of SPI and increased its flexibility. The confocal laser scanning microscopy revealed that oxidized soybean protein isolate treated at 60 °C (OSPI-60) exhibited minimal particle size with optimal structural characteristics. Following in <em>vitro</em> digestion, the OSPI-60 demonstrated ABTS and DPPH radical scavenging capacities that were 19.18% and 16.61% higher than those of SPI, respectively. Evaluation of the constructed SPI and LA emulsion revealed that the OSPI-60 exhibited superior stability, with the highest in <em>vitro</em> accessibility (90.23%) for the encapsulated vitamin D<sub>3</sub>. This study provides new insights into developing nutritionally fortified soybean flour matrices and extending their application as a wall material for delivering lipophilic nutrients in powdered foods.</div></div>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":"363 ","pages":"Article 151887"},"PeriodicalIF":8.5,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147643542","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}
Muhammad Zafar Iqbal , Pengfei He , Pengbo He , Min Huang , Yixin Wu , Guowen Tang , Ping Tang , Shahzad Munir , Yueqiu He
{"title":"Functional role of rpoS gene in cross-kingdom pathogenicity of Klebsiella pneumoniae in maize-murine pathosystem","authors":"Muhammad Zafar Iqbal , Pengfei He , Pengbo He , Min Huang , Yixin Wu , Guowen Tang , Ping Tang , Shahzad Munir , Yueqiu He","doi":"10.1016/j.ijbiomac.2026.151931","DOIUrl":"10.1016/j.ijbiomac.2026.151931","url":null,"abstract":"<div><div>The systematic study particularly those affected by the cross-kingdom pathogen <em>Klebsiella pneumoniae</em>, remains exclusive in a special domain. We unravel the dynamics of the cross-kingdom interactions involving mice and maize plants. Here, we constructed <em>rpoS</em> mutants from three different strains of <em>K. pneumoniae</em> [WKpE4 (from environment), WKpC4 (from maize plant) and WKp138 (clinical)], examining maize and murine response to disease after pathogen inoculation. The integrated approach utilized phenotypic and visual assay of both organisms and histopathological assays with the Murine Grimace Scale (MGS) to gain unprecedented insights into mice subjective pain experiences. We distinguished the mutant from the wild-type response to environmental and virulence factors, demonstrating ΔKpE4 is more sensitive to acid, UV, while ΔKpC4 is more sensitive to temperature, oxidative, osmotic and starvation stress. Mutant strains, particularly ΔKpC4 enhanced growth rates in plants comparable to parental wild strains. ΔKpC4 is less virulent in mice, causing less pain with higher bacterial recovery in various organs. ΔKp138 showed more sensitive towards stress assays whereas less disease occurrence in both plants and mice compared to WKp138 strains. These cross-kingdom findings facilitated the crucial role of <em>rpoS</em> in weakening defense against diseases in organisms. In addition, it bridges existing knowledge gaps in understanding <em>rpoS</em> responses across different organisms, their host-pathogen interactions, adaptive responses to stresses, and food borne illness in animals providing new avenues for therapeutic interventions and management approaches in pathosystem.</div></div>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":"363 ","pages":"Article 151931"},"PeriodicalIF":8.5,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147653542","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":"Robust gelatin/dialdehyde starch biofoams via yeast-induced in situ foaming: fabrication and properties","authors":"Yu Duan , Zhen Zhang , Long Zhang","doi":"10.1016/j.ijbiomac.2026.152102","DOIUrl":"10.1016/j.ijbiomac.2026.152102","url":null,"abstract":"<div><div>Bio-based porous carriers are widely used for controlled release, but pores formed under mild conditions in natural polymer matrices often come at the cost of structural integrity. In addition, conventional chemical foaming and crosslinking can introduce safety concerns. Here we couple yeast fermentation–driven foaming with Schiff-base crosslinking between gelatin and dialdehyde starch (DAS), so that the evolving bubble-derived pore structure can be progressively retained while pore walls consolidate into a three-dimensionally porous composite (GDS). FT-IR indicated imine formation between DAS aldehydes and gelatin ε-amino groups, with strong hydrogen-bonding interactions also evidenced. SEM showed an open, honey<sub>co</sub>mb-like network with a maximum porosity of 72.6%, whereas the yeast-free control reached only ∼19%. Even at high porosity, the crosslinked walls preserved shape after swelling, and the GDS samples showed improved thermal stability, reflected by a shift of the main degradation region toward higher temperatures. Aspirin (ASP) loading in the optimized matrix (ASP@GDS-4/70/6) produced biphasic release in PBS (pH 7.4): an early fraction (M<sub>1h</sub> = 35.4%), close to a commercial 75 mg sustained-release aspirin tablet (30.6%), followed by a longer sustained-release phase (t<sub>95</sub> = 8 h vs 6 h). Overall release followed a first-order model (R<sup>2</sup> = 0.993). For M<sub>t</sub>/M<sub>∞</sub> ≤ 0.60, Korsmeyer–Peppas fitting gave <em>n</em> = 0.66 (R<sup>2</sup> = 0.967), consistent with non-Fickian transport arising from coupled diffusion and polymer relaxation. This coupled foaming-and-crosslinking approach offers a mild route to interconnected porosity in natural polymer matrices.</div></div>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":"364 ","pages":"Article 152102"},"PeriodicalIF":8.5,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147727878","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}