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xylanase
INDUSTRIAL CROPS AND PRODUCTS · 2023 · IF 5.9

Fabrication of immobilized xylanase by a novel 3D electrostatic printing as an excellent catalyst for corn straw degradation

Caixia Cui,Xinying Wang,Xin Sha,Zhao Zhang,Hong Ming,Hui Cao

Extrusion-based 3D printing has been widely utilized in enzyme immobilization to obtain the desired shape, even though the result is less fine. Here, we report a novel 3D electrostatic printing (3DEP) technology that combines the technologies of electrospinning and 3D printing to manufacture fiber membranes that are finer and uniform and used them for xylanase immobilization. After optimizing the preparation conditions for the 3DEP immobilization carrier, the finer, uniform fiber membranes were printed by using a ratio of 10:1 polyvinyl alcohol (PVA) and chitosan (Cs) under a constant voltage (5 kV) and feed rate (0.001 mm/s). Additionally, 50% glutaraldehyde (GA) vapor was used for cross-linking Cs in order to improve the water insolubility of the support. The 3DEP immobilized xylanase was then prepared by mixing xylanase and the printed materials. The resulting immobilized xylanase exhibited excellent stability, with over 95% of enzyme activity following storage for 28 days, and 53% xylan conversion was still retained after reuse over 8 batches. Finally, the 3DEP immobilized xylanase featured good catalytic efficiency in degrading corn straw. Collectively, the results of this study show that 3DEP offered a finer carrier manufacturing technology and could improve the catalytic efficiency of the immobilized enzyme .

CAS / MDL: 111-30-8
研究领域: 生物技术 · 材料科学 · 酶学
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WOOD SCIENCE AND TECHNOLOGY · 2026 ·Vol. 60 ·期 3 ·48 · IF 3.2

Kinetic and environmental effects of xylanase-pectinase pretreatment-mediated weakly alkaline hydrogen peroxide bleaching of poplar chemi-thermomechanical pulp

Li Jing,Zha Yu-Ning,Wang Han-Min,Hou Qing-Xi

The pulp and paper industry faces growing challenges arising from fiber shortages and environmental concerns. High yield pulping technology has emerged as a key solution, but the high lignin content in high yield pulp (HYP) restricts its brightness, posing a significant challenge for the bleaching process. Although traditional strong alkaline hydrogen peroxide (H 2 O 2 ) bleaching of HYP is effective, it results in fiber yield loss and the generation of anionic impurities, thereby bringing about additional environmental burdens. In contrast, weakly alkaline H 2 O 2 bleaching is more environmentally friendly and preserves a high pulp yield, but it struggles to achieve the desired brightness due to the reduced reactivity of lignin. This work addresses these challenges by investigating the effect of xylanase-pectinase (XP) pretreatment combined with weakly alkaline H 2 O 2 bleaching to improve both bleaching efficiency and environmental benefits in the bleaching of poplar chemi-thermomechanical pulp (CTMP). The kinetic analysis reveals that the XP pretreatment significantly enhanced the efficiency of weakly alkaline H 2 O 2 bleaching, accelerating lignin removal and increasing pulp brightness. The XP pretreatment effectively reduced the electrical conductivity, cationic demand, and chemical oxygen demand of the bleaching effluent. The mechanism studies demonstrate that the XP pretreatment effectively cleaved lignin-carbohydrate complex linkages and degraded hemicelluloses side chains, significantly increasing the accessibility and reactivity of the residual lignin. The integration of XP pretreatment with weakly alkaline H 2 O 2 bleaching can offer a sustainable and efficient process for poplar CTMP upgrading, simultaneously enhancing the bleaching efficiency and mitigating the environmental footprint.

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FOOD CHEMISTRY · 2024 · IF 8.5

Characterization of a novel multifunctional β-glucosidase/xylanase/feruloyl esterase and its effects on improving the quality of Longjing tea

Hongling Wang,Xianghui Qi,Song Gao,Guoshi Kan,Lkhagvasuren Damdindorj,Yingfeng An,Fuping Lu

Herein, a novel multifunctional enzyme β-glucosidase/xylanase/feruloyl esterase (GXF) was constructed by fusion of β-glucosidase and bifunctional xylanase/feruloyl esterase. The activities of β-glucosidase, xylanase, feruloyl esterase and acetyl xylan esterase displayed by GXF were 67.18 %, 49.54 %, 38.92 % and 23.54 %, respectively, higher than that of the corresponding single functional enzymes. Moreover, the GXF performed better in enhancing aroma and quality of Longjing tea than the single functional enzymes and their mixtures. After treatment with GXF , the grassy and floral odors of tea infusion were significantly improved. Moreover, GXF treatment could improve concentrations of flavonoid aglycones of myricetin, kaempferol and quercetin by 68.1-, 81.42- and 77.39-fold, respectively. In addition, GXF could accelerate the release of reducing sugars, ferulic acid and xylo -oligosaccharides by 9.48-, 8.25- and 4.11-fold, respectively. This multifunctional enzyme may have potential applications in other fields such as food production and biomass degradation.

研究领域: 酶学 · 食品科学 · 茶叶技术 · 生物技术
✓ 已验证 DOI PubMed 高影响因子
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NEW JOURNAL OF CHEMISTRY · 2024 · IF 2.7

Thermo- and pH-tolerance xylanase immobilized magnetic responsive Zr-MOFs composites as recyclable biocatalyst for the degradation of corn straw

Qingtai Chen,Chongchong Wu,Shujie Hu,Lizhi Cui,Yong Zhang,Peng Hu,Zhi Xu,Pei Yu,Miao Yu

Xylanase is a natural and high-efficiency catalyst for the degradation of xylan to reducing sugar. However, the catalytic performance of xylanase is greatly limited by its poor activity and stability at the harsh condition. To overcome this issue, covalent immobilization of xylanase on a magnetic porous MOFs material with core-shell structure, UIO-66-NH2 carrier was applied to improve the catalytic activity and stability of xylanase. Several tools were employed to monitor the preparation and immobilization processes, magnetic properties, and the structural/chemical characteristics of the biocatalyst. 77.9% of the activity for xylanase was retained after immobilization. Moreover, the thermal stability in terms of half-life of the immobilized enzyme was three times higher than that in free form, and which had higher catalytic efficiency for hydrolysis of xylan. Furthermore, the greater temperature and wider pH ranges of the activity stability were achieved for the immobilized xylanase in compared with free one. Notably, the biocatalyst exhibits both excellent storage stability and could be easily separated using a magnet, which is conducive for its reusability. And nearly 70% of its initial activity was retained after seven recycles during the hydrolysis of corn straw. These features indicate that the present immobilization method is promising prospect for the industrial application of enzyme.

研究领域: 生物技术 · 酶工程 · 材料科学 · 环境科学
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TEXTILE RESEARCH JOURNAL · 2017 · IF 1.443

A novel endo-β-1,4-xylanase GH30 from Dickeya dadantii DCE-01: Clone, expression, characterization, and ramie biological degumming function

Ruijun Wang,Zhengchu Liu,Lifeng Cheng,Shengwen Duan,Xiangyuan Feng,Ke Zheng,Yi Cheng,Jie Zeng

Xylanase plays an important role in the hydrolysis of hemicellulose and has gained much attention in the field of biological degumming. The research for xylanases with cellulase-free and high activity for biological degumming has intensified in recent years. In the present research, heterologous expression of a novel endo-β-1,4-xylanase (GH30) from Dickeya dadantii DCE-01 in Escherichia coli BL21 (DE3) was reported. Biochemical characterization of the enzyme and a potential application in ramie biological degumming was discussed. The results showed that the xylanase gene consists of 1251 nucleotides, belonging to glycoside hydrolase family 30 (GH30). The optimal activity of the xylanase was observed at 50℃ and a pH value of 6.4. The Km and Vmax values for beechwood xylan were 14.25 mg/mL and 296.6 μmol/mg, respectively. The catalytic activity was enhanced by addition of 1 mM Cu2+, Ca2+, Mg2+, and K+. The recombinant enzyme was specific for xylan substrates. The enzyme exhibited hydrolytic activity toward ramie hemicellulose. The recombinant xylanase could be effectively applied to ramie degumming.

研究领域: 生物化学 · 生物技术 · 酶学 · 纺织科学
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Frontiers in Bioengineering and Biotechnology · 2023 · IF 5.7

Analysis of the effect of metal ions on the ability of Xylanase to hydrolyze wheat bran by molecular dynamics simulations

Hou Mingrui,Liang Chuanqi,Fei Yanan,Yang Dan,Zhang Ningjing,Lu Yujie,Wang Lei,Xing Zhiqiang,Zhao Zongpei

Introduction: Wheat bran is the main by-product of wheat processing, containing about 30% pentosan and 0.4%–0.7% ferulic acid. Wheat bran is the main raw material used to prepare feruloyl oligosaccharides by hydrolysis of Xylanase, we discovered that the ability of Xylanase to hydrolyze wheat bran could be affected in the presence of different metal ions.Methods: In the present study, we have probed the effects of different metal ions on the hydrolysis activity of Xylanase on wheat bran and tried to analyze the effect of Mn2+ and Xylanase by molecular dynamic (MD) simulation.Results: Our results suggested that Mn2+ had improved the Xylanase hydrolyzing wheat bran to obtain feruloyl oligosaccharides. Particularly when the concentration of Mn2+ reached 4 mmol/L, the optimal product has been obtained 2.8 times higher to compare with no addition. Through the MD simulation analysis, our results reveal that Mn2+ can induce structural change in the active site, which enlarges the substrate binding pocket. The simulation results also revealed that the addition of Mn2+ resulted in a low RMSD value compared with the absence of Mn2+ and helped stabilize the complex.Conclusion: Mn2+ could increase the enzymatic activity of Xylanase in the hydrolysis of feruloyl oligosaccharides in wheat bran. The finding could have significant implications for the preparation of feruloyl oligosaccharides from wheat bran.

研究领域: 生物化学 · 酶工程 · 食品科学
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Frontiers in Microbiology · 2022 · IF 6.064

Biochemical characterization of a novel acidophilic β-xylanase from Trichoderma asperellum ND-1 and its synergistic hydrolysis of beechwood xylan

Zheng Fengzhen,Basit Abdul,Zhuang Huan,Chen Jun,Zhang Jianfen,Chen Weiqing

Acidophilic β-xylanases have attracted considerable attention due to their excellent activity under extreme acidic environments and potential industrial utilizations. In this study, a novel β-xylanase gene (Xyl11) of glycoside hydrolase family 11, was cloned from Trichoderma asperellum ND-1 and efficiently expressed in Pichia pastoris (a 2.0-fold increase). Xyl11 displayed a maximum activity of 121.99 U/ml at pH 3.0 and 50°C, and exhibited strict substrate specificity toward beechwood xylan (Km = 9.06 mg/ml, Vmax = 608.65 μmol/min/mg). The Xyl11 retained over 80% activity at pH 2.0–5.0 after pretreatment at 4°C for 1 h. Analysis of the hydrolytic pattern revealed that Xyl11 could rapidly convert xylan to xylobiose via hydrolysis activity as well as transglycosylation. Moreover, the results of site-directed mutagenesis suggested that the Xyl11 residues, Glu127, Glu164, and Glu216, are essential catalytic sites, with Asp138 having an auxiliary function. Additionally, a high degree of synergy (15.02) was observed when Xyl11 was used in association with commercial β-xylosidase. This study provided a novel acidophilic β-xylanase that exhibits excellent characteristics and can, therefore, be considered a suitable candidate for extensive applications, especially in food and animal feed industries.

CAS / MDL: 9014-63-5
研究领域: 酶学 · 生物技术 · 微生物学
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INDUSTRIAL CROPS AND PRODUCTS · 2023 · IF 5.9

Xylanase-assisted adsorption process for high purity sugar stream development from hydrolysis liquor of kraft-based dissolving pulp production process

Minjie Hou,Leiming Wang,Chenfeng Yang,Tianyuan Xiao,Yanning Sun,Yanzhu Guo,Xueru Sheng,Jie Lu,Fengshan Zhang,Pedram Fatehi,Haiqiang Shi

This paper proposed a novel xylanase-assisted activated carbon process to produce a high-purity sugar stream from pre-hydrolysis liquid (PHL) of the kraft-based dissolving pulp production process. The results showed that the enzymatic hydrolysis could effectively improve the lignin removal and sugar purity at pH 5 and 50 °C. It was observed that the cleavage of lignin-carbohydrate complex (LCC) by enzyme led to more sugar and soluble lignin production in PHL. The main mechanisms involved are the reduced pore clog due to the lignin converted from colloidal to dissolved state at higher pH, lower sugar loss obtained by the reduction of polymerization degree of poly-sugars in PHL and also the removal of the lignin disconnected from the LCC. FTIR NMR, particle size, BET, and SEM analyses confirmed that the induced soluble lignin could be adsorbed by activated carbon effectively without blocking its pores, which improved the selectivity and productivity of activated carbon for removing lignin and generating higher purity sugar stream (97.5 wt. %). Based on the promising results and simplicity of the proposed operations, the introduced process may be attractive to the industry for generating high-purity sugars at an industrial scale.

CAS / MDL: 7440-44-0 64365-11-3
研究领域: 生物技术 · 制浆造纸工程
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Foods · 2023 ·Vol. 12 ·期 12 ·2424 · IF 5.2

Thermodynamics and Physicochemical Properties of Immobilized Maleic Anhydride-Modified Xylanase and Its Application in the Extraction of Oligosaccharides from Wheat Bran

Yang Zhao,Xinrui Li,Shuo Guo,Jingwen Xu,Yan Cui,Mingzhu Zheng,Jingsheng Liu

Xylanases are the preferred enzymes for the extracting of oligosaccharides from wheat bran. However, free xylanases have poor stability and are difficult to reuse, which limit their industrial application. In the present study, we covalently immobilized free maleic anhydride-modified xylanase (FMA-XY) to improve its reusability and stability. The immobilized maleic anhydride-modified xylanase (IMA-XY) exhibited better stability compared with the free enzyme. After six repeated uses, 52.24% of the activity of the immobilized enzyme remained. The wheat bran oligosaccharides extracted using IMA-XY were mainly xylopentoses, xylohexoses, and xyloheptoses, which were the β-configurational units and α-configurational units of xylose. The oligosaccharides also exhibited good antioxidant properties. The results indicated that FMA-XY can easily be recycled and can remain stable after immobilization; therefore, it has good prospects for future industrial applications.Keywords:immobilized enzymes;kinetics;thermodynamics;wheat bran;oligosaccharide

CAS / MDL: 609-99-4 9014-63-5
研究领域: 生物化学 · 酶学 · 食品科学 · 热力学
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APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY · 2026 · IF 3.5

Characterization of a GH11 Xylanase from Endophytic Chaetomium globosum DX-THS3 with Excellent pH Stability and its Role in Enhancing Lignocellulose Degradation

Ji Runzhen,Hua Qijing,Dong Yamin,Zhu Du,Xiao Yiwen,Gao Boliang

Xylanase is the core enzyme responsible for degrading xylan, a major component of lignocellulose, and holds significant application value in fields such as food, feed, and biorefining. In this study, a xylanase gene, Xyn108 , was identified from the genome of the lignocellulose-degrading endophytic fungus Chaetomium globosum DX-THS3 and successfully expressed in Pichia pastoris . The xylanase Xyn108 belongs to glycoside hydrolase family 11 (GH11), with a molecular weight of approximately 38 kDa. The enzyme exhibited optimal activity at pH 6.0 and 40 °C, and demonstrated good stability within pH 3.0–9.0 and at temperatures below 50 °C (retaining > 50% residual activity after 180 min incubation). Xyn108 displayed high enzymatic activity towards beechwood xylan and possessed hydrolytic capacity toward microcrystalline cellulose. Crucially, Xyn108 exhibited significant synergistic effects with the commercial cellulase Cellic CTec2 in hydrolyzing pretreated rice straw. The highest synergistic degrees, reaching 1.34 and 1.24 for NaOH-pretreated and H₂SO₄-pretreated straw, respectively, were achieved at a xylanase/cellulase activity ratio of 1:3. The enzyme’s excellent pH adaptability, low-temperature activity, and remarkable synergistic effects highlight its significant application potential in industrial sectors such as feed processing, paper manufacturing, and biofuel production.

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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2024 · IF 7.7

Efficient production of xylobiose and xylotriose from xylan in moso bamboo by the combination of pH-controlled lactic acid and xylanase hydrolysis

Baojun Feng,Hong Liao,Wenjun Ying,Junhua Zhang,Zhangjing Chen

Short-chain xylo-oligosaccharides (XOS) such as xylobiose (X2) and xylotriose (X3) have higher biological activities. Therefore, it is interesting to produce highly active XOS enriched with X2 and X3. In this work, pH-controlled lactic acid (LA) hydrolysis was used to produce XOS from xylan in moso bamboo and xylanase was used to convert high DP XOS into low DP XOS to increase the percentage of X2 + X3 in XOS. A 33.1 % XOS yield was obtained from 2 % LA hydrolysis (pH = 3.2). After xylanase hydrolysis of the LA hydrolysate, the total XOS yield reached 64.1 %, with X2 + X3 yield reaching 58.4 %. The percentage of X2 + X3 increased from 52.3 % to a high level of 91.0 %. The deep eutectic solvent pretreatment removed 87.2 % lignin from the residue and the glucose yield of the delignified residue hydrolyzed by cellulase was 96.9 %. The results suggested that the integrated process of LA and xylanase hydrolysis could effectively produce X2 + X3 from xylan in moso bamboo.

研究领域: 生物化学 · 可再生资源与环境科学
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2026 · IF 8.7

Fabrication and characterization of edible composite films derived from xylanase-enzymatic flaxseed gum and citric acid-modified soybean protein isolate: Intermolecular interactions and functional efficacy

Jiashu Xiao,Yi Zhao,Junhan Zhang,Jiaxin Shi,Ji Kang,Qiaomei Zhu,Huanhuan Liu,Qingbin Guo,Zhenjing Li

Acidified soy protein acts as an intrinsic plasticizer to improve film flexibility. • The composite films exhibit excellent antioxidant and antibacterial activities. • Synergistic co-assembly creates a compact and stable composite network. • The film minimizes weight loss and delays softening of blueberries. Polysaccharide based edible films often exhibit high brittleness and poor extensibility, limiting their widespread application in food preservation. To address these limitations, plasticizer-free polysaccharide-protein composite films were fabricated from xylanase hydrolyzed flaxseed gum (EFG) and citric acid modified soybean protein isolate (ASPI). This approach aimed to concurrently enhance the flexibility, structural stability, and preservation performance of the target films. Structural characterization using FTIR and SEM confirmed the formation of a compact three-dimensional network driven by changed intermolecular hydrogen bonding, evidenced by a shift of the O H stretching band to 3430 cm −1 . The FSF matrices exhibited notable bioactivity, showing strong antioxidant capacity with hydroxyl and ABTS radical scavenging rates of 97.24% ± 5.96% and 36.64% ± 0.72%, respectively, at 2 mg/mL. The films also demonstrated effective antibacterial activity against Escherichia coli and Staphylococcus aureus . Fuzzy comprehensive evaluation identified FSF-4 as the optimal formulation (membership score: 0.698), achieving a balanced combination of mechanical strength and barrier performance. FSF-4 displayed a tensile strength of 2.87 ± 0.22 MPa, elongation at break of 85.44% ± 1.45%, and water vapor permeability of 1095.73 ± 22.01 g/(m 2 ·24 h). Application tests showed that FSF-4 effectively preserved blueberry quality during 21 days of storage, maintaining higher firmness and weight retention than the uncoated control. Although FSF-1 exhibited greater tensile strength, FSF-4 provided superior overall performance by integrating flexibility, barrier properties, and bioactivity. These films achieved high functionality without external plasticizers, relying on the intrinsic plasticizing effect of ASPI, highlighting their potential as environmentally sustainable food-packaging materials.

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