Identification of a novel type I pullulanase from Fervidobacterium nodosum Rt17-B1, with high thermostability and suitable optimal pH

文献类型： 外文期刊

第一作者： Yang, Yang

作者： Yang, Yang;Obaroakpo, Joy Ujiroghene;Zhang, Shuwen;Lu, Jing;Yang, Lan;Pang, Xiaoyang;Lv, Jiaping;Pang, Xiaoyang;Zhu, Yingying;Ni, Dawei

作者机构：

关键词： Pullulanase; Thermostability; Heterologous expression; Characterization

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：6.953； 五年影响因子：6.737 ）

ISSN： 0141-8130

年卷期： 2020 年 143 卷

页码：

收录情况： SCI

摘要： Pullulanase could be used in many industrial processes due to its ability to hydrolyze alpha-1,6-glucosidic linkage. During the use of high temperature conditions in industrial production, pullulanase requires high resistance of heat. In this study, a novel type I pullulanase from Fervidobacterium nodosum Rt17-B1 (FN-pullulanase) with a suitable optimal pH and thermostability was discovered. Sequence analysis of FN-pullulanase showed that the enzyme had the typical motif of type I pullulanase (YNWGYDP). The recombinant FN-pullulanase, expressed in Escherichia coli, was purified as a single band on SDS-PAGE with a molecular mass of about 95 kDa. The enzyme showed optimum activity at pH 5.0 and 80 degrees C, and its specific activity was 25.93 U/mg. FN-pullulanase also exhibited good pH stability and thermostability. More than 80% of its initial activity was retained after incubated on ice at pH 3.5-9.0 for 24 h. Its half-life at 65 degrees C was 115.5 h. The enzyme could completely convert pullulan to maltotriose, as well as hydrolyze soluble starch or amylopectin to maltose, maltotriose, maltotetraose, maltopentaose and maltohexaose (G2-G6). Generally, this study identified a novel FN-pullulanase with both high thermostability and suitable optimum pH, which had the potential to be used in starch conversion process. (C) 2019 Published by Elsevier B.V.

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