Distribution of Chitinolytic Enzymes in the Organs and cDNA Cloning of Chitinase Isozymes from the Liver of Golden Cuttlefish <i>Sepia esculenta</i> — Oak Academic Publishing
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Distribution of Chitinolytic Enzymes in the Organs and cDNA Cloning of Chitinase Isozymes from the Liver of Golden Cuttlefish <i>Sepia esculenta</i>
Department of Marine Science and Resources, College of Bioresource Sciences, Nihon University, Fujisawa, Kanagawa, Japan
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Department of Marine Science and Resources, College of Bioresource Sciences, Nihon University, Fujisawa, Kanagawa, Japan
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Department of Marine Science and Resources, College of Bioresource Sciences, Nihon University, Fujisawa, Kanagawa, Japan
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Department of Marine Science and Resources, College of Bioresource Sciences, Nihon University, Fujisawa, Kanagawa, Japan
1 Department of Marine Science and Resources, College of Bioresource Sciences, Nihon University, Fujisawa, Kanagawa, Japan
2 Department of Marine Science and Resources, College of Bioresource Sciences, Nihon University, Fujisawa, Kanagawa, Japan
3 Department of Marine Science and Resources, College of Bioresource Sciences, Nihon University, Fujisawa, Kanagawa, Japan
4 Department of Marine Science and Resources, College of Bioresource Sciences, Nihon University, Fujisawa, Kanagawa, Japan
The distribution of chitinolytic enzymes in eight organs of the golden cuttlefish <i> Sepia esculenta </i> was determined. Chitinase activity (activity of endo-type chitinolytic enzyme) was measured using <i> p </i> NP-(GlcNAc) n (n = 2, 3) as substrates, with high activity detected in the liver, posterior salivary gland, and stomach. <i> β - N </i> -acetylhexosaminidase (Hex) activity (activity of exo-type chitinolytic enzyme) was determined using <i> p </i> NP-(GlcNAc) as a substrate, and high activity was observed in six organs, including the liver, branchial heart, posterior salivary gland, and stomach. In addition, two chitin-binding proteins (CBP-A, CBP-B) were isolated from the liver using a chitin affinity column. Two full-length cDNAs ( <i> SeChi </i> -1: 1484 bp; <i> SeChi </i> -2: 1748 bp) encoding chitinases were obtained from the liver of <i> S. esculenta </i> . <i> SeChi </i> -1 contained a 1377-bp open reading frame (ORF) encoding 459 amino acids, and <i> SeChi </i> -2 contained a 1656-bp ORF encoding 552 amino acids. Domain structures predicted from the deduced amino acid sequences of <i> SeChi </i> -1 and <i> SeChi </i> -2 (SeChi-1, SeChi-2) contained signal peptides, a GH Family 18 catalytic domain, one chitin binding domain (CBD) in SeChi-1, and two CBDs in SeChi-2. Proteome analysis revealed that 125 peptide residues of CBP-A were present in SeChi-1, and 116 peptide residues of CBP-B were present in SeChi-2. Organ expression analysis revealed that <i> SeChi </i> -1 and <i> SeChi </i> -2 were expressed only in the liver of <i> S. esculenta </i> . Phylogenetic analysis of SeChi-1, SeChi-2, and GH family 18 chitinases revealed that SeChi-2 belongs to a group of previously reported squid chitinases, whil e SeChi-1 does not belong to any previously reported group of mollusk chitinases.
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