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Characterization of a β-D-mannosidase from a marine gastropod, Aplysia kurodai

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Title: Characterization of a β-D-mannosidase from a marine gastropod, Aplysia kurodai
Authors: Zahura, Umme Afsari Browse this author
Rahman, Mohammad Matiur Browse this author
Inoue, Akira Browse this author →KAKEN DB
Ojima, Takao Browse this author →KAKEN DB
Keywords: Aplysia kurodai
Issue Date: May-2012
Publisher: Elsevier
Journal Title: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
Volume: 162
Issue: 1-3
Start Page: 24
End Page: 33
Publisher DOI: 10.1016/j.cbpb.2012.02.003
PMID: 22366551
Abstract: A β-D-mannosidase (EC with a molecular mass of approximately 100 kDa was purified from the digestive fluid of a marine gastropod Aplysia kurodai by ammonium sulfate fractionation followed by column chromatographies on TOYOPEARL Butyl-650 M, TOYOPEARL DEAE-650 M, and Superdex 200 10/300 GL. This enzyme, named AkMnsd in the present study, showed optimal activities at pH 4.5 and 40℃ and was stable at the acidic pH range from 2.0 to 6.7 and the temperature below 38℃. The Km and Vmax values for AkMnsd determined at pH 6.0 and 30℃ with p-nitrophenyl β-D-mannopyranoside were 0.10 mM and 3.75 μmol/min/mg, respectively. AkMnsd degraded various polymer mannans as well as mannooligosaccharides liberating mannose as a major degradation product. Linear mannan from green alga Codium fragile was completely depolymerized by AkMnsd in the presence of AkMan, an endolytic β-mannanase, which we previously isolated from the same animal (Zahura et al., Comp. Biochem. Physiol. B 157, 137-148 (2010)). A cDNA encoding AkMnsd was amplified from the Aplysia hepatopancreas cDNA by the PCR using degenerated primers designed on the basis of N-terminal and internal amino-acid sequences of AkMnsd. The cloned AkMnsd cDNA consisted of 2985 bp and encoded an amino-acid sequence of 931 residues with the calculated molecular mass of 101970 Da. The deduced sequence of AkMnsd showed 20-43% amino-acid identity to those of glycoside-hydrolase-family 2 (GHF2) β-mannosidases. The catalytically important amino-acid residues determined in GHF2 enzymes were completely conserved in AkMnsd. Thus, AkMnsd is regarded as a new member of GHF2 mannosidase from marine gastropod.
Type: article (author version)
Appears in Collections:水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 尾島 孝男

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