CAS 37278-89-0 Xylanase - Analytical Products / Alfa Chemistry

CAT	AP37278890
CAS	37278-89-0
MDL Number	MFCD00132594
EC Number	253-439-7

Description	powder, ≥2500 units/g, recombinant, expressed in Aspergillus oryzae
Form	powder
Size	10G, 50G
Storage Conditions	2-8°C

Co-expression of cellulase and xylanase genes in Sacchromyces cerevisiae toward enhanced bioethanol production from corn stover

Wenjing Xiao, Huanan Li, Wucheng Xia, Yuxian Yang, Pan Hu, Shanna Zhou, Yanmei Hu, Xiaopeng Liu, Yujun Dai, Zhengbing Jiang

Bioengineered. 2019 Dec;10(1):513-521.

PMID: 31661645

Direct Recovery of Bacillus Subtilis Xylanase From Fermentation Broth With an alcohol/salt Aqueous Biphasic System

Hui Suan Ng, Cindy Xin Yi Chai, Yin Hui Chow, Wai Leng Carmen Loh, Hip Seng Yim, Joo Shun Tan, John Chi-Wei Lan

J Biosci Bioeng. 2018 May;125(5):585-589.

PMID: 29339003

Immobilization of Xylanase and xylanase-β-cyclodextrin Complex in Polyvinyl Alcohol via Electrospinning Improves Enzyme Activity at a Wide pH and Temperature Range

Jaqueline Pozzada Dos Santos, Elessandra da Rosa Zavareze, Alvaro Renato Guerra Dias, Nathan Levien Vanier

Int J Biol Macromol. 2018 Oct 15;118(Pt B):1676-1684.

PMID: 29981822

Immobilization of Xylanase Using a Protein-Inorganic Hybrid System

Ashok Kumar, Sanjay K S Patel, Bharat Mardan, Raviteja Pagolu, Rowina Lestari, Seong-Hoon Jeong, Taedoo Kim, Jung Rim Haw, Sang-Yong Kim, In-Won Kim, Jung-Kul Lee

J Microbiol Biotechnol. 2018 Apr 28;28(4):638-644.

PMID: 29385669

Optimization of the Cellulase Free Xylanase Production by Immobilized Bacillus Pumilus

Aditi Kundu, Bijan Majumdar

Iran J Biotechnol. 2018 Dec 12;16(4):e1658.

PMID: 31457031

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Case Study

Xylanase Used for Covalent Immobilization on Cyanuric Chloride-Activated Magnetic Nanoparticles for Enhanced Biocatalytic Performance

Soozanipour, Asieh, Asghar Taheri-Kafrani, and Amir Landarani Isfahani. Chemical Engineering Journal 270 (2015): 235-243.

This study demonstrates the covalent immobilization of xylanase on silica-coated magnetite nanoparticles (Fe₃O₄@SiO₂) functionalized with cyanuric chloride to enhance enzymatic stability, activity, and reusability. The immobilization process began with the synthesis of Fe₃O₄ nanoparticles, followed by silica coating to obtain Fe₃O₄@SiO₂. Surface modification was carried out by refluxing Fe₃O₄@SiO₂ with APTES in dry toluene at 70 °C for 24 h. The amine-functionalized particles were then reacted with cyanuric chloride in dry THF at 0 °C to introduce reactive triazine moieties.
Immobilization was performed by dispersing 5 mg of the functionalized nanoparticles in phosphate buffer (pH 6.5), followed by the addition of xylanase solution (4 mg/mL). The suspension was gently shaken at room temperature for 16 h. The resulting xylanase-MNPs exhibited a core-shell structure with ~9 nm diameter and high magnetization (46.56 emu/g), ensuring facile magnetic recovery.
FTIR, XPS, TEM, TGA, and VSM confirmed successful covalent binding and structural integrity. The immobilized enzyme retained 80% of the native activity, exhibited improved thermal and pH stability, and maintained 65% activity after 9 reuse cycles. These results underscore the utility of xylanase immobilized on cyanuric chloride-functionalized Fe₃O₄@SiO₂ as a robust and recyclable biocatalyst suitable for industrial and biotechnological applications.

Xylanase Used for the Preparation of Magnetically Recoverable Enzyme Nanoassemblies via EDC/NHS Coupling Strategy

Salem, Karima, et al. ACS Sustainable Chemistry & Engineering 9.11 (2021): 4054-4063.

In this study, xylanase (XAn11) was immobilized on magnetic nanoparticles (MNPs) to enhance its operational stability and enable magnetic recovery for repeated use in industrial applications. Two immobilization strategies were evaluated-electrostatic interaction and covalent bonding-using two types of MNPs: biomimetic MamC-mediated MNPs (BMNPs) and conventional inorganic MNPs.
For covalent immobilization, 5 mg of MNPs was dispersed in 1 mL of oxygen-free 50 mM MES buffer (pH 5.5) and activated with 0.1 M EDC and 0.7 M NHS. After stirring at 20 °C for 1 h, 25 μM of purified XAn11 was added and incubated for 24 h at 4 °C. The coupling reaction was quenched with 0.1 M Tris, and the immobilized enzyme (XAn11-MNPs-E/N) was magnetically recovered, followed by triple washing with NaClO₄ (pH 3.5). Protein quantification via UV absorbance at 280 nm confirmed an immobilization efficiency of 87%.
Xylanase immobilized via this EDC/NHS protocol exhibited enhanced thermal and storage stability and retained high catalytic activity over eight consecutive reuse cycles. Compared to the free enzyme, the immobilized form demonstrated superior robustness under varying physicochemical conditions, underscoring its utility in biotechnological processes. This work highlights the feasibility of using covalently immobilized xylanase for magnetically separable, recyclable, and efficient biocatalysis.

Xylanase Used for the Preparation of Hyperbranched Polyglycerol-Functionalized Magnetic Biocatalysts

Landarani-Isfahani, Amir, et al. Langmuir 31.33 (2015): 9219-9227.

Xylanase was effectively immobilized onto hyperbranched polyglycerol-functionalized magnetic nanoparticles (MNP/HPG) and their citric acid-modified derivative (MNP/HPG-CA), offering a promising route for enhanced biocatalyst performance. This novel immobilization strategy leverages the high surface functionality and hydrophilicity of dendritic polymers, enabling robust enzyme-support interactions.
In the immobilization procedure, 5 mg of MNP/HPG or MNP/HPG-CA was dispersed in 2 mL phosphate buffer (20 mM, pH 6.5), followed by the addition of xylanase solution (4 mg/mL). The mixture was agitated at room temperature for 8 h to facilitate enzyme binding. The resulting conjugates-MNP/HPG/Xy and MNP/HPG-CA/Xy-were magnetically separated and washed three times to remove unbound enzyme.
Comprehensive physicochemical analyses confirmed successful xylanase loading and uniform nanoparticle morphology. Compared to the free enzyme, immobilized xylanase demonstrated significantly improved stability and reusability, retaining catalytic activity after multiple operational cycles. The citric acid-modified support further enhanced immobilization efficiency and enzyme retention.
This study highlights the potential of dendritic polymer-coated MNPs as advanced enzyme carriers, offering a scalable and efficient platform for industrial biocatalysis. Xylanase immobilized via MNP/HPG systems not only ensures simplified recovery by magnetic separation but also opens pathways for greener and more sustainable enzymatic processes.