Enzymatic properties and the primary structure of a β-1,3-glucanase from the digestive fluid of the Pacific abalone Haliotis discus hannai
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概要
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A β-1,3-glucanase (EC 3.2.1.6) with a molecular mass of 33 kDa was isolated from the digestive fluid of the Pacific abalone Haliotis discus hannai by ammonium sulfate fractionation followed by conventional column chromatography. This enzyme, named HdLam33 in the present study, degraded laminarin and laminarioligosaccharides to laminaribiose and glucose with the optimal temperature and pH at 50℃ and 6.0, respectively. HdLam33 possessed transglycosylation activity, a characteristic property of glucan hydrolases that split glycoside linkage with a retaining manner. By the transglycosylation reaction of HdLam33, the laminaribiose unit in the non-reducing terminus of laminaritriose (donor substrate) was transferred to a free laminaribiose (acceptor substrate) resulting laminaritetraose and glucose. The resulted laminaritetraose was subsequently hydrolyzed by HdLam33 into two moles of glucose and one mole of laminaribiose. The primary structure of HdLam33 was analyzed by the cDNA method. The deduced amino-acid sequence of 329 residues corresponding to the catalytic domain of HdLam33 showed 56-61% amino-acid identity with those of other molluscan β-1,3-glucanases which have been identified as glycoside hydrolase family 16 enzymes.
論文 | ランダム
- 明神礁の海底地形が明らかに
- 海底火山の活動監視 : 人工衛星とハイドロホンの可能性
- マルチバンドカメラによる変色水調査(シートゥルースとの対比) : 日本火山学会1983年度秋季大会
- ランドサットデ-タによる火山性変色水の調査
- ランドサットデータによる海底火山活動調査 : 日本火山学会1980年秋季大会