An endo-β-1,4-mannanase, AkMan, from the common sea hare Aplysia kurodai

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概要

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• A mannan-degrading enzyme was isolated from the digestive fluid of the common sea hare Aplysia kurodaiby ammonium sulfate fractionation followed by conventional column chromatography. The purified enzyme,named AkMan in the present paper, showed a single band with an approximate molecular mass of 40,000 Daon SDS-PAGE and preferably degraded a linear β-1,4-mannan from green algae Codium fragile producing trianddisaccharides. The optimal temperature of AkMan was 55 °C at pH 7.0 and temperature that caused 50%inactivation of AkMan during a 20-min incubation was 52 °C. AkMan retained high activity at pH 4.0–7.5 andwas not inactivated in such acidic pH range by the incubation at 40 °C for 20 min. AkMan could degradeglucomannan from konjak root and galactomannan (tara gum and guar gum) as well as the linear β-1,4-mannan, while not carboxymethyl cellulose, agarose, dextran and xylan. These results indicate that AkMan isa typical endo-β-1,4-mannanase (EC 3.2.1.78) splitting internal β-1,4-mannosyl linkages of mannan. The Nterminaland internal amino-acid sequences of AkMan shared ∼55% amino-acid identity to thecorresponding sequences of an abalone β-1,4-mannanase, HdMan, which belongs to glycosyl hydrolasefamily 5 (GHF5). Thus, AkMan was also regarded as a member of GHF5 β-1,4-mannanases.

著者

• Ojima Takao

  Lab. Of Marine Biotechnology And Microbiology Graduate School Of Fisheries Sciences Hokkaido Univ. H

関連論文

• An endo-β-1,4-mannanase, AkMan, from the common sea hare Aplysia kurodai
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• Heat-stability and primary structure of the major alginate lyase isozyme LbAly35 from Littorina brevicula

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