Biochemical characterization and cleavage specificities analyses of three endo-1,3-fucanases within glycoside hydrolase family 174
Copyright © 2024 Elsevier Ltd. All rights reserved..
Sulfated fucans have garnered extensive research interest in recent decades due to their varied bioactivity. Fucanases are important tools for investigating sulfated fucans. This study reported the bioinformatic analysis and biochemical properties of three GH174 family endo-1,3-fucanases. Wherein, Fun174Rm and Fun174Sb showed the highest optimal reaction temperature among the reported fucanases, and Fun174Sb possessed favorable thermostability and catalysis efficiency. Fun174Rm displayed a random endo-acting manner, while Fun174Ri and Fun174Sb hydrolyzed sulfated fucan in processive manners. UPLC-MS and NMR analyses confirmed that the three enzymes catalyze cleavage of the α(1 → 3)-bonds between Fucp2S and Fucp2S in the sulfated fucan from Isostichopus badionotus. These enzymes demonstrated novel cleavage specificities, which could accept α-Fucp2S residues at subsites -1 and + 1. The acquiring of these biotechnological tools would be beneficial to the in-depth research of sulfated fucans.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:335 |
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| Enthalten in: |
Carbohydrate polymers - 335(2024) vom: 01. Apr., Seite 122083 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Shen, Jingjing [VerfasserIn] |
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| Links: |
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| Themen: |
Biochemical characteristics |
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| Anmerkungen: |
Date Completed 16.04.2024 Date Revised 16.04.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.carbpol.2024.122083 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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NLM371054230 |
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| 520 | |a Copyright © 2024 Elsevier Ltd. All rights reserved. | ||
| 520 | |a Sulfated fucans have garnered extensive research interest in recent decades due to their varied bioactivity. Fucanases are important tools for investigating sulfated fucans. This study reported the bioinformatic analysis and biochemical properties of three GH174 family endo-1,3-fucanases. Wherein, Fun174Rm and Fun174Sb showed the highest optimal reaction temperature among the reported fucanases, and Fun174Sb possessed favorable thermostability and catalysis efficiency. Fun174Rm displayed a random endo-acting manner, while Fun174Ri and Fun174Sb hydrolyzed sulfated fucan in processive manners. UPLC-MS and NMR analyses confirmed that the three enzymes catalyze cleavage of the α(1 → 3)-bonds between Fucp2S and Fucp2S in the sulfated fucan from Isostichopus badionotus. These enzymes demonstrated novel cleavage specificities, which could accept α-Fucp2S residues at subsites -1 and + 1. The acquiring of these biotechnological tools would be beneficial to the in-depth research of sulfated fucans | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Biochemical characteristics | |
| 650 | 4 | |a Cleavage specificity | |
| 650 | 4 | |a Endo-1,3-fucanase | |
| 650 | 4 | |a GH174 | |
| 650 | 4 | |a Hydrolysis pattern | |
| 650 | 4 | |a Sulfated fucan | |
| 650 | 7 | |a Glycoside Hydrolases |2 NLM | |
| 650 | 7 | |a EC 3.2.1.- |2 NLM | |
| 650 | 7 | |a Sulfates |2 NLM | |
| 650 | 7 | |a Sulfur Oxides |2 NLM | |
| 700 | 1 | |a Liu, Guanchen |e verfasserin |4 aut | |
| 700 | 1 | |a Chen, Guangning |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Yuying |e verfasserin |4 aut | |
| 700 | 1 | |a Mei, Xuanwei |e verfasserin |4 aut | |
| 700 | 1 | |a Zheng, Long |e verfasserin |4 aut | |
| 700 | 1 | |a Xue, Changhu |e verfasserin |4 aut | |
| 700 | 1 | |a Chang, Yaoguang |e verfasserin |4 aut | |
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