Recombinant production of two xylanase-somatostatin fusion proteins retaining somatostatin immunogenicity and xylanase activity in Pichia pastoris
文献类型: 外文期刊
第一作者: Huang, Kunlong
作者: Huang, Kunlong;Qin, Xing;Zhang, Jie;Bai, Yingguo;Wang, Yuan;Luo, Huiying;Huang, Huoqing;Su, Xiaoyun;Chu, Yuefeng
作者机构:
关键词: Somatostatin; Xylanase; Fusion protein; Immunogenicity; Bifunctional
期刊名称:APPLIED MICROBIOLOGY AND BIOTECHNOLOGY ( 影响因子:3.53; 五年影响因子:3.913 )
ISSN: 0175-7598
年卷期:
页码:
收录情况: SCI
摘要: Somatostatin (SS) is one of the peptide hormones that regulate the endocrine system in animals. When SS is used to immunize animals, the correspondingly generated anti-SS antibody neutralizes the SS and, therefore, alleviates its growth inhibiting effects. This is of great value to the livestock industry; however, previously developed methods fail to obtain enough recombinant SS in an economical way. Herein, we describe the employment of a commonly used feed enzyme, i.e., xylanase, as a carrier protein for recombinant expression of SS in large quantity. The SS gene was fused to one of the two xylanase genes (XynCDBFV and BsXynC) and recombinantly expressed in Pichia pastoris. The purified xylanase-SS fusion proteins displayed excellent antigenicity and immunogenicity. In addition, they retained the enzymatic activities and thermostability of the xylanases, indicating that they can catalyze hydrolysis of xylan in plant cell wall of the animal feeds and stand the high temperature in feed pelleting. Thus, the xylanase-SS fusion proteins serve as an excellent candidate chimeric bifunctional vaccine-feed enzyme protein retaining both SS immunogenicity and xylanase activity.
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