Efficient conversion of α-chitin by multi-modular chitinase from Chitiniphilus shinanonensis with KOH and KOH-urea pretreatment
Copyright © 2020 Elsevier Ltd. All rights reserved..
Enzymatic conversion of α-chitin to high-value chitooligosaccharides (COS) was up to 7.2 % by a slow-acting endo-chitinase (uni-modular) after KOH or KOH-urea pretreatment. Here, we report a better source for efficient conversion of α-chitin, with KOH/KOH-urea (20K2 or 20KU2) pretreatment, by a multi-modular chitinase (CsChiG) from Chitiniphilus shinanonensis. The CsChiG and its catalytic domain (Cat-CsChiG) converted 20KU2 substrate to soluble COS with an efficiency of 43.1 % and 11.8 %, respectively. Deletion of the chitin binding domain has reduced the conversion of untreated and colloidal chitin substrates by 4-5 folds, and for 20K2 and 20KU2 substrates it was only two folds decrease. A combination of KOH or KOH-urea pretreatment, followed by enzymatic hydrolysis with multi-modular chitinases, thus appears a promising approach to convert the abundantly available chitin to highly useful COS.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2020 |
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| Erschienen: |
2020 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:250 |
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| Enthalten in: |
Carbohydrate polymers - 250(2020) vom: 15. Dez., Seite 116923 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Sivaramakrishna, Dokku [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 01.04.2021 Date Revised 04.12.2021 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.carbpol.2020.116923 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 520 | |a Enzymatic conversion of α-chitin to high-value chitooligosaccharides (COS) was up to 7.2 % by a slow-acting endo-chitinase (uni-modular) after KOH or KOH-urea pretreatment. Here, we report a better source for efficient conversion of α-chitin, with KOH/KOH-urea (20K2 or 20KU2) pretreatment, by a multi-modular chitinase (CsChiG) from Chitiniphilus shinanonensis. The CsChiG and its catalytic domain (Cat-CsChiG) converted 20KU2 substrate to soluble COS with an efficiency of 43.1 % and 11.8 %, respectively. Deletion of the chitin binding domain has reduced the conversion of untreated and colloidal chitin substrates by 4-5 folds, and for 20K2 and 20KU2 substrates it was only two folds decrease. A combination of KOH or KOH-urea pretreatment, followed by enzymatic hydrolysis with multi-modular chitinases, thus appears a promising approach to convert the abundantly available chitin to highly useful COS | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Chitin-binding domains | |
| 650 | 4 | |a Chitinase | |
| 650 | 4 | |a Chitooligosaccharides | |
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| 650 | 4 | |a KOH-urea treatment | |
| 650 | 4 | |a α-Chitin | |
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