Mycoscience
Online ISSN : 1618-2545
Print ISSN : 1340-3540

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Novel acid trehalase belonging to glycoside hydrolase family 37 from Pleurotus sp.: cloning, expression and characterization
Gaku TsutsumiChikako KurokiKengo KameiMizuho KusudaMasami NakazawaTatsuji SakamotoMariko IshikawaShinji HaradaHitoshi KobayashiKenji OuchiSatoshi InatomiMinoru SakaguchiTakeo IwamotoPablo Alvarado
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Keywords: autolysis, trehalose
JOURNAL OPEN ACCESS Advance online publication

Article ID: MYC591

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Abstract

The N-terminal amino acid sequence of the Pleurotus sp. 90 kDa protein was in good agreement with the corresponding sequence of the glycoside hydrolase (GH) family 37 protein (trehalase) from P. ostreatus PC 15 v2.0. The length of the Pleurotus sp. trehalase gene was 2247 bp, encoding a protein of 749 amino acids with a predicted molecular mass of 81.2 kDa. The molecular mass of the recombinant enzyme was estimated to be about 117 kDa by SDS-PAGE. We found that the recombinant enzyme comprised an N-glycosylated sugar chain and that its optimum pH and temperature were 4.5 and 40 ºC, respectively. Moreover, this enzyme exhibited high activity against trehalose exclusively. We found that the enzyme is novel acid trehalase belonging to GH family 37.

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