Improving the Secretory Expression of Laccase in Pichia pastoris by Co-Expressing Chaperones

doi:10.3969/j.issn.1673-1689.2019.11.001

Home > Archive>Volume 38, Issue 11, 2019 >1-8. DOI:10.3969/j.issn.1673-1689.2019.11.001

Improving the Secretory Expression of Laccase in Pichia pastoris by Co-Expressing Chaperones
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                        10.3969/j.issn.1673-1689.2019.11.001
                    
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In this study，the co-expression of chaperones was used to improve the production of laccase in Pichia pastoris. According to the codon bias of Pichia pastoris，the gene of laccase from Cerrena sp. WR1 was optimized and cloned into pPIC9K. The resulted plasmid was transformed into Pichia pastoris GS115，yielding the strain PP-L. In the PP-L，we co-expressed six chaperones，relating to protein folding（BIP and ERO1），transportation（SEC53 and SEC1） and stress response（HAC1 and GCN4）. The results indicated that the co-expressions of chaperones had no effect on the cell growth of strain PP-L. Expression of BIP increased the extracellular enzyme activities by 359% while ERO1 decreased that by 22%. The other four chaperones increased the extracellular activities by 18%~53%. In contrast to strain PP-L，simultaneous co-expression of BIP and HAC1（strain P1） increased 602% of the extracellular activities，reaching 3 896 U/L. It was suggested that the overexpression of BIP in endoplasmic reticulum improved the ability of protein folding，thus improving the secretion efficiency of laccase. The results obtained here may improve the industrialization of laccase.

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WANG Chenlei, LIU Song, DU Guocheng, CHEN Jian. Improving the Secretory Expression of Laccase in Pichia pastoris by Co-Expressing Chaperones[J]. Journal of Food Science and Biotechnology,2019,38(11):1-8.

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