Pub Date : 2026-02-09DOI: 10.1016/j.biortech.2026.134157
Qiuyan Tang, Xinyi Li, Yinghong Xu, Xiangsheng Han
Efficient utilization of lignocellulosic residues from forestry and agriculture is a critical challenge for sustainable resource management. Conventional cellulose nanofibers often require intensive delignification and purification, leading to high energy consumption and loss of natural functionalities. Lignin containing cellulose nanofibers (LCNFs), produced by partially retaining functional lignin within the cellulose framework, have emerged as a promising alternative. This review systematically summarizes the structural features, preparation strategies, and functional properties of LCNFs. The design of LCNF-based functional materials is further discussed, highlighting how their hierarchical structures and lignin–cellulose interactions govern the structure–performance relationship across applications in flexible electronics, environmental remediation, personal protection, and biomedicine. By emphasizing these mechanistic links, this review provides insightful guidance for the design and development of high-value, sustainable LCNF-based materials.
{"title":"Lignin containing cellulose nanofibers for advanced materials: From hierarchical structure to functional applications","authors":"Qiuyan Tang, Xinyi Li, Yinghong Xu, Xiangsheng Han","doi":"10.1016/j.biortech.2026.134157","DOIUrl":"https://doi.org/10.1016/j.biortech.2026.134157","url":null,"abstract":"Efficient utilization of lignocellulosic residues from forestry and agriculture is a critical challenge for sustainable resource management. Conventional cellulose nanofibers often require intensive delignification and purification, leading to high energy consumption and loss of natural functionalities. Lignin containing cellulose nanofibers (LCNFs), produced by partially retaining functional lignin within the cellulose framework, have emerged as a promising alternative. This review systematically summarizes the structural features, preparation strategies, and functional properties of LCNFs. The design of LCNF-based functional materials is further discussed, highlighting how their hierarchical structures and lignin–cellulose interactions govern the structure–performance relationship across applications in flexible electronics, environmental remediation, personal protection, and biomedicine. By emphasizing these mechanistic links, this review provides insightful guidance for the design and development of high-value, sustainable LCNF-based materials.","PeriodicalId":258,"journal":{"name":"Bioresource Technology","volume":"145 1","pages":""},"PeriodicalIF":11.4,"publicationDate":"2026-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146146369","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"环境科学与生态学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Enzymes are efficient green biocatalysts. However, the complex preparation process, poor stability and non-reusability have hindered their applications. Although the chemically/genetically modification could enhance recyclability, there existed limited strategies to solve all the above problems in one step currently. A novel strategy, namely, the peptide based recyclable homogeneous biocatalyst, was proposed with the ancestral carbonic anhydrase (AncCA19) as an example. Ferritin was fused to the C-terminal of AncCA19 (AncCA19F) to obtain the enzyme-ferritin fusion proteins (EFFPs). They could self-assemble into micron-sized AncCA19F (msAncCA19F) in host cells and achieve low-speed centrifugal separation/purification, which streamlined the purification procedures and improved the yield. Interestingly, the msAncCA19F could spontaneously dissolve into nano-sized AncCA19F (nsAncCA19F) in vitro as pH increased, which functioned as homogeneous biocatalysts with improved performances – the experimental half-life (Et12) increased by 9-fold in artificial seawater and by 2-fold in 25% N-methyldiethanolamine (MDEA). The nsAncCA19F could spontaneously aggregate into msAncCA19F as pH decreased, which functioned as recyclable immobilized biocatalysts: with negligible activity loss (<10%) after 10 cycles. The strategy not only realizes the time-effective and scalable preparation and simple recycling of enzymes, but also improves their stability. The mechanism of AncCA19F with improved performances and their responsive to the variation of pH were also addressed.
酶是高效的绿色生物催化剂。但制备工艺复杂、稳定性差、不可重复使用等问题阻碍了其应用。虽然化学/基因改造可以提高可回收性，但目前解决上述所有问题的策略有限。以祖先的碳酸酐酶（AncCA19）为例，提出了一种新的策略，即肽基可回收均相生物催化剂。将铁蛋白融合到AncCA19的c端（AncCA19F），得到酶-铁蛋白融合蛋白（EFFPs）。它们可以在宿主细胞中自组装成微米级的AncCA19F (msAncCA19F)，并实现低速离心分离/纯化，简化了纯化程序，提高了产量。有趣的是，随着pH的增加，msAncCA19F可以在体外自发溶解成纳米级的AncCA19F (nsAncCA19F)，作为均相生物催化剂，其在人工海水中的实验半衰期（Et12）提高了9倍，在25% n -甲基二乙醇胺（MDEA）中提高了2倍。随着pH的降低，nsAncCA19F可以自发聚集成msAncCA19F，作为可回收的固定化生物催化剂，循环10次后活性损失可忽略不计（10%）。该策略不仅实现了酶的高效、规模化制备和简单回收，而且提高了酶的稳定性。探讨了AncCA19F提高性能的机理及其对pH变化的响应。
{"title":"A pH-Responsive and recyclable homogeneous carbonic anhydrase with 24-polymeric fusion protein: Simple preparation and enhanced catalytic performance","authors":"Chun Yang, Zicheng Wu, Yaxin Chen, Yanhong Zhou, Ruifang Zhang, Wei Jiang, Huihua Ge, Guangya Zhang","doi":"10.1016/j.biortech.2026.134197","DOIUrl":"https://doi.org/10.1016/j.biortech.2026.134197","url":null,"abstract":"Enzymes are efficient green biocatalysts. However, the complex preparation process, poor stability and non-reusability have hindered their applications. Although the chemically/genetically modification could enhance recyclability, there existed limited strategies to solve all the above problems in one step currently. A novel strategy, namely, the peptide based recyclable homogeneous biocatalyst, was proposed with the ancestral carbonic anhydrase (AncCA19) as an example. Ferritin was fused to the C-terminal of AncCA19 (AncCA19F) to obtain the enzyme-ferritin fusion proteins (EFFPs). They could self-assemble into micron-sized AncCA19F (msAncCA19F) in host cells and achieve low-speed centrifugal separation/purification, which streamlined the purification procedures and improved the yield. Interestingly, the msAncCA19F could spontaneously dissolve into nano-sized AncCA19F (nsAncCA19F) in vitro as pH increased, which functioned as homogeneous biocatalysts with improved performances – the experimental half-life (<mml:math altimg=\"si1.svg\"><mml:msub><mml:mrow><mml:mi mathvariant=\"normal\">E</mml:mi><mml:mi mathvariant=\"normal\">t</mml:mi></mml:mrow><mml:mfrac><mml:mn>1</mml:mn><mml:mn>2</mml:mn></mml:mfrac></mml:msub></mml:math>) increased by 9-fold in artificial seawater and by 2-fold in 25% <ce:italic>N</ce:italic>-methyldiethanolamine (MDEA). The nsAncCA19F could spontaneously aggregate into msAncCA19F as pH decreased, which functioned as recyclable immobilized biocatalysts: with negligible activity loss (<10%) after 10 cycles. The strategy not only realizes the time-effective and scalable preparation and simple recycling of enzymes, but also improves their stability. The mechanism of AncCA19F with improved performances and their responsive to the variation of pH were also addressed.","PeriodicalId":258,"journal":{"name":"Bioresource Technology","volume":"11 1","pages":""},"PeriodicalIF":11.4,"publicationDate":"2026-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146146325","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"环境科学与生态学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-09DOI: 10.1016/j.biortech.2026.134177
Glen Pauls, Olli Sorsa, Antti Paajanen, Vaibhav Modi, Sebastien Leclerc, Younes Bouizi, Anthony Dufour, Anna Kalliola, Chamseddine Guizani
The conventional approach to converting kraft lignin (KL) into hard carbons is to start with highly purified, low-ash KL feedstocks and then rely on slow, energy-intensive oxidative stabilization and added crosslinkers to keep melting and foaming associated thermal challenges under control. Herein, we deliberately invert this paradigm. Instead of starting with highly purified KL, we retain pulping inorganics and use them as catalytic centers for oxidative crosslinking and melt suppression of KL. Spherical KL microparticles (KL-MP) were recovered from softwood black liquor by membrane filtration and spray-drying steps, intentionally retaining inorganic sodium (Na) salts as well as organically bound Na in KL-MP, and were compared to acid-precipitated, low-ash reference KL (KL-REF). During thermo-oxidative pretreatment (250 °C, 5 °C/min) in air, KL-MP undergoes inorganic-catalyzed rapid oxidative crosslinking that converts thermoplastic lignin into a rigid network, whereas KL-REF softens, foams, and fuses. Experimental analysis identifies organically bound Na-phenoxide type species as key catalytic sites. Proton magnetic resonance thermal analysis and molecular dynamics simulations reveal strongly reduced segmental mobility and Na-driven ionic clusters acting as physical crosslinking points. After pretreatment, inorganics are removed by a washing step, and the crosslinked KL-MP is carbonized, yielding low-surface-area hard carbons that retain their initial micron size and spherical morphology. As Li-ion battery anodes, the derived hard carbon shows better electrochemical performance than carbons derived from KL-REF. Overall, the work shows how otherwise undesirable inorganic impurities can simplify thermal conversion of KL, with potential for diverse applications where particle size and shape are critical.
将硫酸盐木质素（KL）转化为硬碳的传统方法是从高纯度、低灰分的KL原料开始，然后依靠缓慢的、能源密集型的氧化稳定和添加交联剂来控制融化和发泡相关的热挑战。在这里，我们有意颠倒了这一范式。通过膜过滤和喷雾干燥的步骤，从软木黑液中回收球形KL微粒（KL- mp），有意保留无机钠（Na）盐和有机结合的Na，并将其与酸沉淀、低灰分的参考KL （KL- ref）进行比较。在空气中的热氧化预处理（250 °C, 5 °C/min）过程中，KL-MP经历无机催化的快速氧化交联，将热塑性木质素转化为刚性网络，而KL-REF则软化、发泡和熔断。实验分析确定有机结合的Na-phenoxide型物种是关键的催化位点。质子磁共振热分析和分子动力学模拟表明，节段迁移率大大降低，na驱动的离子团簇充当物理交联点。预处理后，无机物通过洗涤步骤去除，交联的KL-MP被碳化，产生低表面积的硬碳，保留其初始的微米尺寸和球形形貌。作为锂离子电池阳极，衍生硬碳的电化学性能优于KL-REF衍生碳。总的来说，这项工作显示了不需要的无机杂质如何简化KL的热转化，在粒度和形状至关重要的各种应用中具有潜力。
{"title":"Inorganics from kraft black liquor enable rapid oxidative crosslinking and morphology control in lignin derived hard carbons","authors":"Glen Pauls, Olli Sorsa, Antti Paajanen, Vaibhav Modi, Sebastien Leclerc, Younes Bouizi, Anthony Dufour, Anna Kalliola, Chamseddine Guizani","doi":"10.1016/j.biortech.2026.134177","DOIUrl":"https://doi.org/10.1016/j.biortech.2026.134177","url":null,"abstract":"The conventional approach to converting kraft lignin (KL) into hard carbons is to start with highly purified, low-ash KL feedstocks and then rely on slow, energy-intensive oxidative stabilization and added crosslinkers to keep melting and foaming associated thermal challenges under control. Herein, we deliberately invert this paradigm. Instead of starting with highly purified KL, we retain pulping inorganics and use them as catalytic centers for oxidative crosslinking and melt suppression of KL. Spherical KL microparticles (KL-MP) were recovered from softwood black liquor by membrane filtration and spray-drying steps, intentionally retaining inorganic sodium (Na) salts as well as organically bound Na in KL-MP, and were compared to acid-precipitated, low-ash reference KL (KL-REF). During thermo-oxidative pretreatment (250 °C, 5 °C/min) in air, KL-MP undergoes inorganic-catalyzed rapid oxidative crosslinking that converts thermoplastic lignin into a rigid network, whereas KL-REF softens, foams, and fuses. Experimental analysis identifies organically bound Na-phenoxide type species as key catalytic sites. Proton magnetic resonance thermal analysis and molecular dynamics simulations reveal strongly reduced segmental mobility and Na-driven ionic clusters acting as physical crosslinking points. After pretreatment, inorganics are removed by a washing step, and the crosslinked KL-MP is carbonized, yielding low-surface-area hard carbons that retain their initial micron size and spherical morphology. As Li-ion battery anodes, the derived hard carbon shows better electrochemical performance than carbons derived from KL-REF. Overall, the work shows how otherwise undesirable inorganic impurities can simplify thermal conversion of KL, with potential for diverse applications where particle size and shape are critical.","PeriodicalId":258,"journal":{"name":"Bioresource Technology","volume":"315 1","pages":""},"PeriodicalIF":11.4,"publicationDate":"2026-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146146367","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"环境科学与生态学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-08DOI: 10.1016/j.biortech.2026.134174
Rosie Graham, Brooke Wain, Robbie A. Clark, Victoria L. Bemmer, Gustavo P. Borin, Luisana Avilan, Elaine M. Rudge, Ciaran W. Lahive, Michael P. Shaver, Andrew R. Pickford
High solids loading is essential for economically and environmentally viable enzymatic recycling of poly(ethylene terephthalate) (PET), yet performance gains from enzyme–binding module fusions under industrially relevant conditions remain unclear. This study evaluated a rationally designed fusion between the thermophilic Saccharopolyspora flava cutinase and the type A carbohydrate‑binding module from Spirochaeta thermophila, selected for compatible temperature optima and substrate‑morphology preferences. The fusion enzyme retained the thermostability of its constituent domains and sustained activity at 50 °C over extended operation, while rapid loss of kinetic stability above this point accounted for poor performance at elevated temperatures. The fusion enzyme displayed increased enzyme binding capacity on both amorphous and semi‑crystalline PET, while affinity enhancement was substrate‑dependent and greatest for crystalline PET. However, enhanced adsorption on crystalline substrates did not translate into increased hydrolysis, indicating that catalytic turnover is limited by factors beyond binding, consistent with the Sabatier principle. In contrast, substantial improvements in PET depolymerisation were observed for amorphous substrates at industrially relevant (20 wt%) solids loadings under pH‑controlled reactor conditions. The largest enhancement occurred for a pre‑consumer PET textile following amorphisation and micronisation, far exceeding gains observed for amorphous films and powders. These results demonstrate that fusion enzymes have the potential to significantly enhance PET hydrolysis at high solids when substrate morphology permits productive enzyme–polymer interactions. Performance is therefore highly dependent on the specific pairing of enzyme and binding module, and on substrate properties, underscoring the need for evaluation under deployment‑relevant conditions.
{"title":"Enhanced enzymatic hydrolysis of pretreated polyester textile at high solids loading through fusion with a carbohydrate binding module","authors":"Rosie Graham, Brooke Wain, Robbie A. Clark, Victoria L. Bemmer, Gustavo P. Borin, Luisana Avilan, Elaine M. Rudge, Ciaran W. Lahive, Michael P. Shaver, Andrew R. Pickford","doi":"10.1016/j.biortech.2026.134174","DOIUrl":"https://doi.org/10.1016/j.biortech.2026.134174","url":null,"abstract":"High solids loading is essential for economically and environmentally viable enzymatic recycling of poly(ethylene terephthalate) (PET), yet performance gains from enzyme–binding module fusions under industrially relevant conditions remain unclear. This study evaluated a rationally designed fusion between the thermophilic Saccharopolyspora flava cutinase and the type A carbohydrate‑binding module from Spirochaeta thermophila, selected for compatible temperature optima and substrate‑morphology preferences. The fusion enzyme retained the thermostability of its constituent domains and sustained activity at 50 °C over extended operation, while rapid loss of kinetic stability above this point accounted for poor performance at elevated temperatures. The fusion enzyme displayed increased enzyme binding capacity on both amorphous and semi‑crystalline PET, while affinity enhancement was substrate‑dependent and greatest for crystalline PET. However, enhanced adsorption on crystalline substrates did not translate into increased hydrolysis, indicating that catalytic turnover is limited by factors beyond binding, consistent with the Sabatier principle. In contrast, substantial improvements in PET depolymerisation were observed for amorphous substrates at industrially relevant (20 wt%) solids loadings under pH‑controlled reactor conditions. The largest enhancement occurred for a pre‑consumer PET textile following amorphisation and micronisation, far exceeding gains observed for amorphous films and powders. These results demonstrate that fusion enzymes have the potential to significantly enhance PET hydrolysis at high solids when substrate morphology permits productive enzyme–polymer interactions. Performance is therefore highly dependent on the specific pairing of enzyme and binding module, and on substrate properties, underscoring the need for evaluation under deployment‑relevant conditions.","PeriodicalId":258,"journal":{"name":"Bioresource Technology","volume":"34 1","pages":""},"PeriodicalIF":11.4,"publicationDate":"2026-02-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146146399","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"环境科学与生态学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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