Institutional Repository of Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences
Molecular characterization and function of beta-N-acetylglucosaminidase from ridgetail white prawn Exopalaemon carinicauda | |
Sun, Yuying1,3; Zhang, Jiquan1,2; Xiang, Jianhai2,4![]() | |
2018-03-30 | |
Source Publication | GENE
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ISSN | 0378-1119 |
Volume | 648Pages:12-20 |
Corresponding Author | Zhang, Jiquan(zhangjiquan@qdio.ac.cn) |
Abstract | Chitin degradation is catalyzed by a two-component chitinolytic enzyme system, chitinase and beta-N-acetylglucosaminidase (NAGase). In this paper, the full-length cDNA sequence encoding NAGase (EcNAG) was obtained from Exopalaemon carinicauda. The deduced amino acid sequence of EcNAG open reading frame (ORF) contained one Glycohydro_20b2 domain and one Glyco_hydro_20 domain. Based on the cDNA sequence, the genomic structure of EcNAG was characterized and it was composed of six exons and five introns. EcNAG mRNA majorly expressed in the hepatopancreas and epidermis. During the molting stages, EcNAG mRNA expression was well-regulated and its expression reached the highest level at the molting stage E. In addition, EcNAG was recombinant expressed in Pichia pastoris and the partial enzymatic characterization of recombinant EcNAG was confirmed. After being challenged with Vibrio parahaemolyticus and Aeromonas hydrophila, the expression of EcNAG was up-regulated significantly at 6 h and reached the peak at 12 h. And then, the expression began to down-regulated and came to the normal level at 72 h. It is helpful to research the relationship between the molt related hormones and chitinlytic enzymes. |
Keyword | beta-N-acetylglucosaminidase Exopalaemon carinicauda Pichia pastoris Recombinant expression |
DOI | 10.1016/j.gene.2018.01.046 |
Indexed By | SCI |
Language | 英语 |
Funding Project | National Natural Science Foundation of China[31172449] ; National Natural Science Foundation of China[41376165] ; National High Technology Research and Development Program of China[2012AA10A401] ; National Natural Science Foundation of China[31172449] ; National Natural Science Foundation of China[41376165] ; National High Technology Research and Development Program of China[2012AA10A401] |
WOS Research Area | Genetics & Heredity |
WOS Subject | Genetics & Heredity |
WOS ID | WOS:000426410200003 |
Publisher | ELSEVIER SCIENCE BV |
Citation statistics | |
Document Type | 期刊论文 |
Identifier | http://ir.qdio.ac.cn/handle/337002/158060 |
Collection | 实验海洋生物学重点实验室 |
Corresponding Author | Zhang, Jiquan |
Affiliation | 1.Hebei Univ, Coll Life Sci, Baoding 071002, Hebei, Peoples R China 2.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China 3.Huaihai Inst Technol, Coll Marine Life & Fisheries, 59 Cangum Rd, Lianyungang 222005, Peoples R China 4.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao 266000, Peoples R China |
Corresponding Author Affilication | Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences |
Recommended Citation GB/T 7714 | Sun, Yuying,Zhang, Jiquan,Xiang, Jianhai. Molecular characterization and function of beta-N-acetylglucosaminidase from ridgetail white prawn Exopalaemon carinicauda[J]. GENE,2018,648:12-20. |
APA | Sun, Yuying,Zhang, Jiquan,&Xiang, Jianhai.(2018).Molecular characterization and function of beta-N-acetylglucosaminidase from ridgetail white prawn Exopalaemon carinicauda.GENE,648,12-20. |
MLA | Sun, Yuying,et al."Molecular characterization and function of beta-N-acetylglucosaminidase from ridgetail white prawn Exopalaemon carinicauda".GENE 648(2018):12-20. |
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