A thermostable xylanase hydrolyzes several polysaccharides from Bacillus altitudinis JYY-02 showing promise for industrial applications
Copyright © 2024 Elsevier Ltd. All rights reserved..
Polysaccharides have attracted immense attention as the largest source of bioactive compounds. Its bioavailability and bioactivity can be improved by utilizing degradation enzymes to reduce their molecular weight and viscosity. In this study, a 654 bp gene encoding xylanase was screened from the genome of Bacillus altitudinis JYY-02 and overexpressed in Escherichia coli Rosetta (DE3). The recombinant xylanase with a molecular weight of 27.98 kDa was purified (11.7-fold) using Ni-NTA affinity chromatography, with a 43.6% final yield. Through molecular docking, Glu, Arg, Tyr, and Trp were found to be the main amino acids involved in the interaction between xylanase and xylobiose. The effects of pH, temperature, metal ions, and substrates on xylanase activity were determined, and the results showed that the highest catalytic activity was displayed at pH 6.5, 50 °C temperature, with Cu2+ as an activator and xylan as the substrate. The Km (substrate concentration that yields a half-maximal velocity) and Vmax (maximum velocity) of recombinant xylanase were 6.876 mg/mL and 10984.183 μmol/mg∙pr/min, respectively. The recombinant xylanase was thermostable, with 85% and 39% of the enzymatic activity retained after 1 h at 60 °C and 1 h at 90 °C, respectively. The recombinant xylanase demonstrated a significant clarifying effect on fruit juices.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:538 |
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| Enthalten in: |
Carbohydrate research - 538(2024) vom: 15. Apr., Seite 109080 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Tai, Hongzheng [VerfasserIn] |
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| Links: |
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| Themen: |
Bacillus altitudinis JYY-02 |
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| Anmerkungen: |
Date Completed 15.04.2024 Date Revised 15.04.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.carres.2024.109080 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 520 | |a Polysaccharides have attracted immense attention as the largest source of bioactive compounds. Its bioavailability and bioactivity can be improved by utilizing degradation enzymes to reduce their molecular weight and viscosity. In this study, a 654 bp gene encoding xylanase was screened from the genome of Bacillus altitudinis JYY-02 and overexpressed in Escherichia coli Rosetta (DE3). The recombinant xylanase with a molecular weight of 27.98 kDa was purified (11.7-fold) using Ni-NTA affinity chromatography, with a 43.6% final yield. Through molecular docking, Glu, Arg, Tyr, and Trp were found to be the main amino acids involved in the interaction between xylanase and xylobiose. The effects of pH, temperature, metal ions, and substrates on xylanase activity were determined, and the results showed that the highest catalytic activity was displayed at pH 6.5, 50 °C temperature, with Cu2+ as an activator and xylan as the substrate. The Km (substrate concentration that yields a half-maximal velocity) and Vmax (maximum velocity) of recombinant xylanase were 6.876 mg/mL and 10984.183 μmol/mg∙pr/min, respectively. The recombinant xylanase was thermostable, with 85% and 39% of the enzymatic activity retained after 1 h at 60 °C and 1 h at 90 °C, respectively. The recombinant xylanase demonstrated a significant clarifying effect on fruit juices | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Bacillus altitudinis JYY-02 | |
| 650 | 4 | |a Enzymatic properties | |
| 650 | 4 | |a Juice clarification | |
| 650 | 4 | |a Polysaccharide degradation | |
| 650 | 4 | |a Recombinant xylanase | |
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| 700 | 1 | |a Guo, Qunqun |e verfasserin |4 aut | |
| 700 | 1 | |a Zhao, Jiamin |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Yandong |e verfasserin |4 aut | |
| 700 | 1 | |a Yu, Hao |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Yili |e verfasserin |4 aut | |
| 700 | 1 | |a Qu, Yifan |e verfasserin |4 aut | |
| 700 | 1 | |a Du, Guicai |e verfasserin |4 aut | |
| 700 | 1 | |a Li, Ronggui |e verfasserin |4 aut | |
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