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Quek, J. P.

Publications and source records attributed to Quek, J. P..

2 recordsLinked to original sources

Valorisation of spent cultivated meat media for recombinant FGF2 production in GRAS Lactococcus lactis

Innovative strategies for sustainable utilization of waste resources are imperative in the pursuit of a circular economy. Recently, the idea of utilizing mammalian spent media as a valuable resource is gaining traction, offering significant opportunities for innovative uses as a food-grade feedstock for microbial fermentation, especially in the production of alternative proteins for research and food purposes. In this study, we aim to repurpose spent mammalian culture media for production of valuable proteins. Growth factors (GFs) are a family of high-value proteins that naturally stimulate cell proliferation or differentiation. More importantly, these factors also present significant costs for cell culture. Here, we successfully demonstrate the use of spent mammalian culture media for the recombinant production of fibroblast growth factor 2 (FGF2-G3) in Lactococcus lactis. Bioreactor fermentation at a 1 L scale confirmed purified yields of 2.6 mg/L of recombinant FGF2-G3 using spent media. Further functional testing indicated that the recombinant FGF2-G3 can promote cell proliferation on an Anguilla japonica (Japanese eel) pre-adipocytic cell line, suggesting its potential for cultivated meat production. Based on the preliminary results of this study, our calculations indicate that fermenting 1 L spent mammalian waste could yield enough growth factors to efficiently grow approximately 52 L of cultivated meat through fermentation. This prediction emphasizes the potential of waste valorisation to sustainably produce protein, thus contributing to environmental preservation and economic viability. HighlightsO_LISpent mammalian culture media can be repurposed for microbial fermentation. C_LIO_LIGRAS L. lactis was used to express FGF2-G3 in an optimized spent media formulation. C_LIO_LIFunctional FGF2-G3 expression was demonstrated in controlled 1-L bioreactor runs. C_LI

microbiology↗

Crystal structure of the Rubella virus protease reveals a unique papain-like protease fold

Rubella is well-controlled due to an effective vaccine, but outbreaks are still occurring without any available antiviral treatments. There is still much to learn about the rubella virus (RUBV) papain-like protease (RubPro) that could be a potential drug target. This protease is crucial to RUBV replication, cleaving the non-structural polyprotein p200 into 2 multi-functional proteins, p150 and p90. Here we report a novel crystal structure of RubPro at 1.64 [A] resolution. It has a similar catalytic core structure to that of SARS-CoV-2 and foot-mouth-disease virus (FMDV) proteases. RubPro has well-conserved sequence motifs that are also found in its newly discovered Rubivirus relatives. The RubPro construct was shown to have protease activity in trans against a construct of RUBV protease-helicase and fluorogenic peptide. A protease-helicase construct was also cleaved in E. coli expression. RubPro was demonstrated to possess deubiquitylation activity, suggesting a potential role of RubPro in modulating the hosts innate immune responses. The structural and functional insights of the RubPro will advance our current understanding of its function and point to more structure-based research into the RUBV replication machinery, in hopes of developing antiviral therapeutics in the future.

microbiology↗