Enhancing production of lipase MAS1 from marine Streptomyces sp. strain in Pichia pastoris by chaperones co-expression

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• 作者：Dongming Lan^a ; ¹ ; Man Qu^a ; ¹ ; Bo Yang^b ; Yonghua Wang^a ; ^{yonghw@scut.edu.cn" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Fermentation optimization ; Methanol fed-batch ; Protein disulfide isomerase ; Vitreoscilla hemoglobin
• 刊名：Electronic Journal of Biotechnology
• 出版年：2016
• 出版时间：July 2016
• 年：2016
• 卷：22
• 期：Complete
• 页码：62-67
• 全文大小：674 K

文摘

A thermostable lipase MAS1 from marine Streptomyces sp. strain was considered as a potential biocatalyst for industrial application, but its production level was relatively low. Here, the effect of chaperones co-expression on the secretory expression of lipase MAS1 in Pichia pastoris was investigated.

Result

Co-expression of protein disulfide isomerase (PDI), HAC1 and immunoglobulin binding protein could increase the expression level of lipase MAS1, whereas co-expression of Vitreoscilla hemoglobin showed a negative effect to the lipase MAS1 production. Among them, PDI co-expression increased lipase MAS1 expression level by 1.7-fold compared to the control strain harboring only the MAS1 gene. Furthermore, optimizing production of lipase MAS1 with Pichia pastoris strain X-33/MAS1-PDI in a 30-L bioreactor were conducted. Lower induction temperature was found to have a benefit effect for lipase MAS1 production. Lipase activity at 24 and 22°C showed 1.7 and 2.1-fold to that at 30°C, respectively. Among the induction pH tested, the highest lipase activity was obtained at pH 6.0 with activity of 440 U/mL after 144 h fermentation.

Conclusion

Our work showed a good example for improving the production of recombinant enzymes in Pichia pastoris via chaperon co-expression and fermentation condition optimization.