High-Level Production of Bacteriotoxic Phospholipase Al in Bacterial Host Pseudomonas fluorescens via ABC Transporter-Mediated Secretion and Inducible Expression

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Bacterial phospholipase A1 (PLA1) is used in various industrial fields because it can catalyze the hydrolysis, esterification, and transesterification of phospholipids to their functional derivatives. It also has a role in the degumming process of crude plant oils. However, bacterial expression of the foreign PLA1-encoding gene was generally hampered because intracellularly expressed PLA1 is inherently toxic and damages the phospholipid membrane. In this study, we report that secretion-based production of recombinant P1aA, a bacterial PLA1 gene, or co-expression of P1aS, an accessory gene, minimizes this harmful effect. We were able to achieve high-level P1aA production via secretion-based protein production. Here, T1iD/T1iE/T1iF, an ABC transporter complex of Pseudomonas fluorescens SIK-W1, was used to secrete recombinant proteins to the extracellular medium. In order to control the protein expression with induction, a new strain of P. fluorescens, which had the lac operon repressor gene lad, was constructed and named ZYAI strain. The bacteriotoxic P1aA protein was successfully produced in a bacterial host, with help from ABC transporter-mediated secretion, induction-controlled protein expression, and fermentation. The final protein product is capable of degumming oil efficiently, signifying its application potential.
Publisher
MDPI
Issue Date
2020-02
Language
English
Article Type
Article
Citation

MICROORGANISMS, v.8, no.2

ISSN
2076-2607
DOI
10.3390/microorganisms8020239
URI
http://hdl.handle.net/10203/273900
Appears in Collection
BS-Journal Papers(저널논문)
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