Molecular characterization and function of β-N-acetylglucosaminidase from ridgetail white prawn Exopalaemon carinicauda
作者： Yuying Sun , Jiquan Zhang , Jianhai Xiang
DOI: 10.1016/J.GENE.2018.01.046
关键词: Vibrio parahaemolyticus 、 Open reading frame 、 Recombinant DNA 、 Chitinase 、 Complementary DNA 、 Biology 、 Peptide sequence 、 Pichia pastoris 、 Hepatopancreas 、 Biochemistry
摘要: Abstract Chitin degradation is catalyzed by a two-component chitinolytic enzyme system, chitinase and β-N-acetylglucosaminidase (NAGase). In this paper, the full-length cDNA sequence encoding NAGase (EcNAG) was obtained from Exopalaemon carinicauda. The deduced amino acid of EcNAG open reading frame (ORF) contained one Glycohydro_20b2 domain Glyco_hydro_20 domain. Based on sequence, genomic structure characterized it composed six exons five introns. mRNA majorly expressed in hepatopancreas epidermis. During molting stages, expression well-regulated its reached highest level at stage E. addition, recombinant Pichia pastoris partial enzymatic characterization confirmed. After being challenged with Vibrio parahaemolyticus Aeromonas hydrophila, up-regulated significantly 6 h peak 12 h. And then, began to down-regulated came normal 72 h. It helpful research relationship between molt-related hormones chitinlytic enzymes.
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