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N-terminal truncated phospholipase A1 accessory protein PlaS from Serratia marcescens alleviates inhibitory on host cell growth and enhances PlaA1 enzymatic activity

 Phospholipase A1 (PLA1) is a phospholipid hydrolase widely used in food, medical, and textile industries. However, its expression and enzymatic activity are limited. This study elucidates the role of PlaS in enhancing the expression and activity of PlaA1 through N-terminal truncation. It was demonstrated that truncating the N-terminal region of PlaS effectively overcomes its inhibitory effect on the host cells, resulting in improved cell growth and increased protein solubility. The two-hybrid assay confirms the interaction between PlaA1 and N-terminal truncated PlaS (∆N27 PlaS), highlighting their binding capabilities. Furthermore, in vitro studies using Biacore analysis reveal a concentration-dependent and specific binding between PlaA1 and ∆N27 PlaS, exhibiting high affinity. Molecular docking analysis provides insights into the hydrogen bond interactions between ∆N27 PlaS and PlaA1, identifying key amino acid residues crucial for their binding.


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Bioresources and Bioprocessing (BIOB) is a peer-reviewed open access journal published under the brand SpringerOpen. BIOB aims at providing an international academic platform for exchanging views on and promoting research to support bioresource development, processing and utilization in a sustainable manner. As an application-oriented research journal, BIOB covers not only the application and management of bioresource technology but also the design and development of bioprocesses that will lead to new and sustainable production processes.

BIOB publishes original and review articles on most topics relating to bioresource and bioprocess engineering, including:

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