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Purification, Identification, and Characterization of a Glycoside Hydrolase Family 11-Xylanase with High Activity from Aspergillus niger VTCC 017.

التفاصيل البيبلوغرافية
العنوان: Purification, Identification, and Characterization of a Glycoside Hydrolase Family 11-Xylanase with High Activity from Aspergillus niger VTCC 017.
المؤلفون: Dao TMA; Department of Biochemistry, Hanoi University of Pharmacy, Hanoi, Vietnam., Cuong NT; Institute of Biotechnology, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet Road, Caugiay District, 10600, Hanoi, Vietnam., Nguyen TT; Graduate University of Science and Technology, Vietnam Academy of Science and Technology, Hanoi, Vietnam., Nguyen NPD; Tay Nguyen University, Buon Ma Thuot, Dak Lak, Vietnam., Tuyen DT; Institute of Biotechnology, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet Road, Caugiay District, 10600, Hanoi, Vietnam. dttuyen@ibt.ac.vn.; Graduate University of Science and Technology, Vietnam Academy of Science and Technology, Hanoi, Vietnam. dttuyen@ibt.ac.vn.
المصدر: Molecular biotechnology [Mol Biotechnol] 2022 Feb; Vol. 64 (2), pp. 187-198. Date of Electronic Publication: 2021 Sep 27.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Springer Country of Publication: Switzerland NLM ID: 9423533 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1559-0305 (Electronic) Linking ISSN: 10736085 NLM ISO Abbreviation: Mol Biotechnol Subsets: MEDLINE
أسماء مطبوعة: Publication: [Cham] : Springer
Original Publication: Totowa, NJ : Humana Press, c1994-
مواضيع طبية MeSH: Aspergillus niger/*enzymology , Fungal Proteins/*isolation & purification , Xylosidases/*isolation & purification , Xylosidases/*metabolism, Detergents/chemistry ; Dextrans ; Electrophoresis, Polyacrylamide Gel ; Enzyme Stability ; Filtration/methods ; Fungal Proteins/chemistry ; Fungal Proteins/metabolism ; Hydrogen-Ion Concentration ; Kinetics ; Metals/chemistry ; Solvents/chemistry ; Temperature ; Xylosidases/chemistry
مستخلص: Xylanases (EC 3.2.1.8) have been considered as a potential green solution for the sustainable development of a wide range of industries including pulp and paper, food and beverages, animal feed, pharmaceuticals, and biofuels because they are the key enzymes that degrade the xylosidic linkages of xylan, the major component of the second most abundant raw material worldwide. Therefore, there is a critical need for the industrialized xylanases which must have high specific activity, be tolerant to organic solvent or detergent and be active during a wide range of conditions, such as high temperature and pH. In this study, an extracellular xylanase was purified from the culture broth of Aspergillus niger VTCC 017 for primary structure determination and properties characterization. The successive steps of purification comprised centrifugation, Sephadex G-100 filtration, and DEAE-Sephadex chromatography. The purified xylanase (specific activity reached 6596.79 UI/mg protein) was a monomer with a molecular weight of 37 kDa estimating from SDS electrophoresis. The results of LC/MS suggested that the purified protein is indeed an endo-1,4-β-D-xylanase. The purified xylanase showed the optimal temperature of 55 °C, and pH 6.5 with a stable xylanolytic activity within the temperature range of 45-50 °C, and within the pH range of 5.0-8.0. Most divalent metal cations including Zn 2+ , Fe 2+ , Mg 2+ , Cu 2+ , Mn 2+ showed some inhibition of xylanase activity while the monovalent metal cations such as K + and Ag + exhibited slight stimulating effects on the enzyme activity. The introduction of 10-30% different organic solvents (n-butanol, acetone, isopropanol) and several detergents (Triton X-100, Tween 20, and SDS) slightly reduced the enzyme activity. Moreover, the purified xylanase seemed to be tolerant to methanol and ethanol and was even stimulated by Tween 80. Overall, with these distinctive properties, the putative xylanase could be a successful candidate for numerous industrial uses.
(© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.)
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معلومات مُعتمدة: 106.02-2018.347 Nafosted
فهرسة مساهمة: Keywords: Aspergillus niger VTCC 017; High-active GH11 xylanase; Industrial enzyme; Purification and characterization
المشرفين على المادة: 0 (Detergents)
0 (Dextrans)
0 (Fungal Proteins)
0 (Metals)
0 (Solvents)
9014-76-0 (sephadex)
EC 3.2.1.- (Xylosidases)
تواريخ الأحداث: Date Created: 20210928 Date Completed: 20220325 Latest Revision: 20220325
رمز التحديث: 20231215
DOI: 10.1007/s12033-021-00395-8
PMID: 34580814
قاعدة البيانات: MEDLINE
الوصف
تدمد:1559-0305
DOI:10.1007/s12033-021-00395-8