Engineering of a Microbial Cell Factory for the Extracellular Production of Catalytically Active Phospholipase A2 of Streptomyces violaceoruberopen access
- Authors
- Lee, Hyun-Jae; Cho, Ara; Hwang, Yeji; Park, Jin-Byung; Kim, Sun-Ki
- Issue Date
- Aug-2020
- Publisher
- NLM (Medline)
- Keywords
- Escherichia coli; extracellular production; Phospholipase A₂; Pichia pastoris
- Citation
- Journal of microbiology and biotechnology, v.30, no.8, pp 1244 - 1251
- Pages
- 8
- Journal Title
- Journal of microbiology and biotechnology
- Volume
- 30
- Number
- 8
- Start Page
- 1244
- End Page
- 1251
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/53632
- DOI
- 10.4014/jmb.2001.01052
- ISSN
- 1017-7825
1738-8872
- Abstract
- Phospholipase A2 (PLA2) from Streptomyces violaceoruber is a lipolytic enzyme used in a wide range of industrial applications including production of lysolecithins and enzymatic degumming of edible oils. We have therefore investigated expression and secretion of PLA2 in two workhorse microbes, Pichia pastoris and Escherichia coli. The PLA2 was produced to an activity of 0.517 ± 0.012 U/ml in the culture broth of the recombinant P. pastoris. On the other hand, recombinant E. coli BL21 star (DE3), overexpressing the authentic PLA2 (P-PLA2), showed activity of 17.0 ± 1.3 U/ml in the intracellular fraction and 21.7 ± 0.7 U/ml in the culture broth. The extracellular PLA2 activity obtained with the recombinant E. coli system was 3.2-fold higher than the corresponding value reached in a previous study, which employed recombinant E. coli BL21 (DE3) overexpressing codon-optimized PLA2. Finally, we observed that the extracellular PLA2 from the recombinant E. coli P-PLA2 culture was able to hydrolyze 31.1 g/l of crude soybean lecithin, an industrial substrate, to a conversion yield of approximately 95%. The newly developed E. coli-based PLA2 expression system led to extracellular production of PLA2 to a productivity of 678 U/l·h, corresponding to 157-fold higher than that obtained with the P. pastoris-based system. This study will contribute to the extracellular production of a catalytically active PLA2.
- Files in This Item
-
- Appears in
Collections - ETC > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/53632)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.