Abstract
To improve starch processing as well as enrich the enzyme resources, an amylopullulanase (CEApu) from Caldisericum exile was heterologously expressed and characterized. CEApu was identified as a glycoside hydrolase from glycoside hydrolase (GH) family 57. The optimal temperature and optimal pH were determined to be 75 °C, and pH 5.5 and 8.5, respectively. CEApu had a wide pH adaptation and activity, retaining >50% activity from pH 4.5–10.0. CEApu also had broad substrate specificity, as it could hydrolyze α-1,4/α-1,6 glycosidic linkages in starch, dextrin, oligosaccharide (degree of polymerization (DP) > 3), pullulan, and even γ-cyclodextrin (γ-CD), but not α-cyclodextrin (α-CD) and β-cyclodextrin (β-CD). The maximum reducing sugar content was 103 mg/g released from gelatinized cassava starch. CEApu was a biocatalyst that may be used for the preparation of starch sugars, resistant starches or linear dextrins. These results confirmed that CEApu was a thermostable amylopullulanase with a strong application potential.
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