There is a drive towards developing new, safe and sustainable ingredients for use in consumer goods. Antimicrobial preservatives are centre front in the minds of consumers and regulatory bodies and present an opportunity for Engineering Biology to develop new solutions.
Antimicrobials are abundant in Nature and their identification and derivatisation has given rise to many successful tools including antibiotics (e.g., penicillin), organic acids (e.g., lactic acid) and bacteriophages. Predatory bacteria including Lysobacter sp. hunt and consume other microorganisms secreting metabolites and enzymes which can target their prey and disrupt cellular integrity and viability and their potential as biocontrol agents has been demonstrated for crop protection. Included in their arsenal are enzymes, glucanases and chitinases, which are directed to and degrade fungal cell wall polysaccharides allowing access to the internal nutrients. Driven by breakthroughs in directed evolution, rational design, and more recently AIassisted modelling, enzyme engineering technology in a new and rapidly evolving era. This PhD project will leverage this new capability to investigate and develop glucanase and chitinase enzymes as potential new anti-fungal agents and to explore their performance in consumer good formulations.
The project will employ a wide range of techniques underpinned by high throughput and automated workflows including bioprospecting of recombinant enzyme panels, enzyme assay development and implementation, carbohydrate chemistry/(automated)synthesis, structural biology and rational and directed evolution enzyme engineering.
The successful candidate will be based at the Manchester Institute of Biotechnology (www.mib.ac.uk), the UK’s first purpose-built institute for interdisciplinary research at the interface of the physical and life sciences. The institute is a leader in the field of Engineering Biology and houses several centres of excellence including BioProcess: Biocatalysis and Protein Engineering Centre for Sustainable Synthesis, BioAID: AI-Driven Enzyme Design for Industry Biocatalysis as well as the FBRH: Future Biomanufacturing Research Hub. The institute has state-of-the-art laboratories for both synthetic and molecular biology, as well as the facilities for automated (robotic) biological workflows.
Representative Publications / References
Otsuka Y, Sato K, Yano S, Kanno H, Suyotha W, Konno H, Makabe K, Taira T. GH-16 Type β-1,3-Glucanase from Lysobacter sp. MK9-1 Enhances Antifungal Activity of GH-19 Type Chitinase, and Its Glucan-binding Domain Binds to Fungal Cell-wall. J Appl Glycosci (1999). 2022 Aug 22;69(3):49-56. doi: 10.5458/jag.jag.JAG-2022_0002. PMID: 36304837; PMCID: PMC9534828.
Xu S, Zhang Z, Xie X, Shi Y, Chai A, Fan T, Li B and Li L. Comparative genomics provides insights into the potential biocontrol mechanism of two Lysobacter enzymogenes strains with distinct antagonistic activities. Front. Microbiol. (2022)13:966986. doi: 10.3389/fmicb.2022.966986
Lovelock SL, Crawshaw R, Basler S, Levy C, Baker D, Hilvert D, Green AP. The road to fully programmable protein catalysis. Nature. 2022 Jun;606(7912):49-58. doi: 10.1038/s41586-022-04456-z. Epub 2022 Jun 1. PMID: 35650353.
Li Z, Chawla H, Vagno LD, Cheallaigh AN, Critcher M, Sammon D, Gonzalez-Rodriguez E, Briggs DC, Chung N, Chang V, Mahoney KE, Cioce A, Bineva-Todd G, Wang P-Y, Liu Y-C, Murphy L.D, Chen Y-H, Narimatsu Y, Miller RL, Willems LI, Malaker SA, Huang ML, Miller GJ, Hohenester E, Schumann B. Xylosyltransferase Engineering to Manipulate Proteoglycans in Mammalian Cells. Nat. Chem. Biol. (2026), 1–10. https://doi.org/10.1038/s41589-025-02113-w.