Characterization of genes for chitin catabolism in Haloferax mediterranei

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• 作者：Jing Hou (1) (2)
  Jing Han (1)
  Lei Cai (1) (2)
  Jian Zhou (1)
  Yang Lü (3)
  Cheng Jin (3)
  Jingfang Liu (1)
  Hua Xiang (1)
  
• 关键词：Chitin ; Catabolism ; Haloarchaea ; Bioplastic ; Bioconversion
• 刊名：Applied Microbiology and Biotechnology
• 出版年：2014
• 出版时间：February 2014
• 年：2014
• 卷：98
• 期：3
• 页码：1185-1194
• 全文大小：460 KB
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• 作者单位：Jing Hou (1) (2)
  Jing Han (1)
  Lei Cai (1) (2)
  Jian Zhou (1)
  Yang Lü (3)
  Cheng Jin (3)
  Jingfang Liu (1)
  Hua Xiang (1)
  
  1. State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, People’s Republic of China
  2. University of Chinese Academy of Sciences, Beijing, 100049, People’s Republic of China
  3. State Key Laboratory of Mycology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, People’s Republic of China
  
• ISSN：1432-0614

文摘

Chitin is the second most abundant natural polysaccharide after cellulose. But degradation of chitin has never been reported in haloarchaea. In this study, we revealed that Haloferax mediterranei, a metabolically versatile haloarchaeon, could utilize colloidal or powdered chitin for growth and poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHBV) accumulation, and the gene cluster (HFX_5025-5039) for the chitin catabolism pathway was experimentally identified. First, reverse transcription polymerase chain reaction results showed that the expression of the genes encoding the four putative chitinases (ChiAHme, ChiBHme, ChiCHme, and ChiDHme, HFX_5036-5039), the LmbE-like deacetylase (DacHme, HFX_5027), and the glycosidase (GlyAHme, HFX_5029) was induced by colloidal or powdered chitin, and chiA Hme, chiB Hme, and chiC Hme were cotranscribed. Knockout of chiABC Hme or chiD Hme had a significant effect on cell growth and PHBV production when chitin was used as the sole carbon source, and the chiABCD Hme knockout mutant lost the capability to utilize chitin. Knockout of dac Hme or glyA Hme also decreased PHBV accumulation on chitin. These results suggested that ChiABCDHme, DacHme, and GlyAHme were indeed involved in chitin degradation in H. mediterranei. Additionally, the chitinase assay showed that each chitinase possessed hydrolytic activity toward colloidal or powdered chitin, and the major product of colloidal chitin hydrolysis by ChiABCDHme was diacetylchitobiose, which was likely further degraded to monosaccharides by DacHme, GlyAHme, and other related enzymes for both cell growth and PHBV biosynthesis. Taken together, this study revealed the genes and enzymes involved in chitin catabolism in haloarchaea for the first time and indicated the potential of H. mediterranei as a whole-cell biocatalyst in chitin bioconversion.