Heterologous production of an acidic thermostable lipase with broad-range pH activity from thermophilic fungus Neosartorya fischeri P1

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• 作者：Qiaoqiao Sun¹ ; ² ; ^&Dagger ; ; Hui Wang¹ ; ^&Dagger ; ; Huitu Zhang² ; Huiying Luo¹ ; Pengjun Shi¹ ; Yingguo Bai¹ ; Fuping Lu² ; Bin Yao¹ ; Huoqing Huang¹ ; ^{huanghuoqing@caas.cn" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Lipase ; Broad pH adaptability ; Thermophilic fungus ; Pichia pastoris ; Neosartorya fischeri
• 刊名：Journal of Bioscience and Bioengineering
• 出版年：2016
• 出版时间：November 2016
• 年：2016
• 卷：122
• 期：5
• 页码：539-544
• 全文大小：685 K

文摘

Thermophilic Neosartorya fischeri P1 is an excellent lipase producer and harbors seven lipase genes. All genes were found to be functional after heterologous expression in Escherichia coli. One of them, LIP09, showed high-level expression in Pichia pastoris with the yield of 2.0 g/L in a 3.7-L fermentor. Deduced amino acid sequence of LIP09 consists of a putative signal peptide (residues 1–19) and a mature polypeptide (residues 20–562). Compared with other fungal counterparts, purified recombinant LIP09 has some superior properties. It exhibited maximum activity at 60°C and pH 5.0, had broad pH adaptability (>60% activity at pH 3.5–8.0) and stability (retaining >90% activity after incubation at pH 3.0–7.0 for 1 h at 40°C), and was highly thermostable (retaining >96% activity after incubation at 50°C for 30 min). The r-LIP09 had a preference for the medium-chain length p-nitrophenyl esters (C12) rather than short and long-chain length substrates. The high-level expression and excellent properties make LIP09 a potential enzyme candidate in food and feed industries.