4.7 Article

Rationally engineered chitin deacetylase from Arthrobacter sp. AW19M34-1 with improved catalytic activity toward crystalline chitin

期刊

CARBOHYDRATE POLYMERS
卷 274, 期 -, 页码 -

出版社

ELSEVIER SCI LTD
DOI: 10.1016/j.carbpol.2021.118637

关键词

Rational design; Chitin deacetylase; Crystalline chitin; Chitosan

资金

  1. National Natural Science Foundation of China [31772016]
  2. Jiangsu Province Marine Science and Technology Innovation Project [JSZRHYKJ202008, HY2018-10]
  3. Priority Academic Program Development of Jiangsu Higher Education Institutions
  4. Key Natural Science Foundation of the Jiangsu Higher Education Institutions of China [20KJA550001]
  5. National Natural Science Foundation of Jiangsu Ocean University [KQ20041]
  6. Project333 of Jiangsu Province
  7. Open-end Funds of Jiangsu Key Laboratory of Marine Bioresources and Environment [SH20191204]
  8. Jangsu Province College Students' innovation and entrepreneurship training program [SZ202111641638001]
  9. 521 high-level talents training project in Lianyungang

向作者/读者索取更多资源

The study enhanced the deacetylation activity of chitin deacetylases from Arthrobacter through site-directed mutagenesis, leading to improved deacetylation efficiency on crystalline chitin. The mutant Mut-2-8 was found to have potential applications in the chitosan industry.
Chitin and its derivatives have anticoagulant, antimicrobial, and antioxidant properties, but the poor solubility of chitin limits its application in different fields. In this study, site-directed mutagenesis was performed to enhance the deacetylation activity of chitin deacetylases CDA from Arthrobacter (ArCE4). The mutant Mut-2-8 with Y172E/E200S/Y201W showed a 2.84- fold and 1.39-fold increase in catalytic efficiency (kcat/Km) for the deacetylation of (GluNAc)5 and alpha-chitin, respectively. These results demonstrated that the mutations significantly improved the activation of ArCE4 on crystalline chitin. The molecular docking study confirmed that the enhancement of catalytic efficiency is due to the extra two hydrogen bonds and one acetyl group. In summary, the activity of Mut-2-8 to insoluble chitin was significantly improved by reactional design, which is beneficial to resolve the issues of the expensive cost of the enzymes and low efficiency. Mut-2-8 exhibits potential applications in the chitosan industry.

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