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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 PublicationGENE
ISSN0378-1119
Volume648Pages:12-20
Corresponding AuthorZhang, Jiquan(zhangjiquan@qdio.ac.cn)
AbstractChitin 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.
Keywordbeta-N-acetylglucosaminidase Exopalaemon carinicauda Pichia pastoris Recombinant expression
DOI10.1016/j.gene.2018.01.046
Indexed BySCI
Language英语
Funding ProjectNational 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 AreaGenetics & Heredity
WOS SubjectGenetics & Heredity
WOS IDWOS:000426410200003
PublisherELSEVIER SCIENCE BV
Citation statistics
Cited Times:1[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.qdio.ac.cn/handle/337002/158060
Collection实验海洋生物学重点实验室
Corresponding AuthorZhang, Jiquan
Affiliation1.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 AffilicationKey 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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