Recent developments in heterologous production of cellulases and xylanases using the Pichia pastoris expression system

文献类型： 外文期刊

第一作者： Ullah, Hayat

作者： Ullah, Hayat;Madadi, Meysam;Hu, Yun;Sun, Fubao;Asadollahi, Mohammad Ali;Dou, Shaohua;Yan, Junshu;Huan, Hailin;Madadi, Meysam;Sun, Fubao

作者机构：

关键词： cellulase; CRISPR/Cas9; genetic engineering strategies; P. pastoris; AOX1 promoter; xylanase

期刊名称：JOURNAL OF CHEMICAL TECHNOLOGY AND BIOTECHNOLOGY （ 影响因子：3.4； 五年影响因子：3.2 ）

ISSN： 0268-2575

年卷期： 2024 年 99 卷 3 期

页码：

收录情况： SCI

摘要： The yeast expression system, Pichia pastoris, is one of the most robust and versatile expression systems in biotechnology and molecular biology, generally considered as a safe host for heterologous protein expression, especially for producing cellulases and xylanases at the industrial level. Despite the high recombinant protein expression rate, the potential of the P. pastoris expression system has still not been fully explored. Cultivation of P. pastoris under optimized conditions greatly relies on the strain and is associated with certain problems such as promoter strength, sensitivity to methanol, and oxygen demand. To address these issues, different genetic engineering strategies have been employed. Advancements in promoter engineering, optimization of gene dosage and codon usage, recombinant plasmid engineering using CRISPR/Cas9 system, and directed evolution strategies have proven beneficial to the yield of cellulase expression levels. This study will systemically review recent progress in various genetic engineering strategies to enhance cellulase and xylanase expression in the P. pastoris expression system. The utilization of alcohol oxidase 1 promoter (pAOX1), methanol-free system, and recombinant plasmid engineering for improved production of these enzymes are highlighted. Additionally, we discuss the recent advancements in the P. pastoris expression system toolbox for improved cellulase and xylanase production, thus providing a deep insight into how P. pastoris is becoming the indispensable platform for heterologous protein production. (c) 2023 Society of Chemical Industry (SCI).

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