Project Focus: This study examines glycosylation which is a key post-translational modification and its impact on enzyme stability and activity. We will investigate two industrially relevant classes: glycosyl hydrolases and metalloproteases. Emphasis will be on glycosylation patterns to identify strategies that enhance structural integrity, protease resistance, and performance in home-care formulations.

Glycosylation is one of the most critical PTMs, involving the attachment of sugar moieties (glycans) to proteins. The two most common types are:

• N-linked glycosylation: Glycans are attached to the nitrogen atom of asparagine residues.
• O-linked glycosylation: Glycans are attached to the oxygen atom of serine or threonine residues.

Industrial Relevance: Enzymes are widely used across industries from pulp and paper to biofuels. In home-care applications, enzymes play a key role in sustainable cleaning, reducing reliance on fossil fuels and lowering the carbon footprint. However, many wild-type enzymes are unstable in home-care formulations due to surfactants and other cleaning ingredients like proteases, significantly lowering enzyme efficacy; therefore, methods to enhance stability are pertinent.

Hypotheses:

1. Glycosylation enhances structural and proteolytic stability of enzymes.
2. The type, size, and extent of glycosylation significantly influence enzyme activity and stability.
3. Specific glycosylation patterns can optimize both stability and activity.

Methodology: To test these hypotheses, we will use glycoproteomics, biochemical assays, structural bioinformatics, and enzyme activity measurements.

Please apply via this link: https://unidla.org/apply/. You should follow all instructions in the form on this webpage.

Anonymised applications will be reviewed by a panel of academic staff following the closing date.

Guidance for applicants is available here: https://unidla.org/unidla-guidance-for-applicants/.

Successful applicants only will be advised to submit a formal application through the University of Liverpool Application Portal at the relevant time.

This project is funded by BBSRC and Unilever for Home students.

Stipend

Students will receive a tax-free stipend for each year of study. The stipend amount will be the UKRI minimum rates (£21,805 for 2026/27) plus an annual Unilever-funded supplement of £4500. Additionally, £2,000 per annum London Weighting Allowance will be offered for students registered in London-based Universities.

Tuition fees

All home tuition fees will be fully covered by the studentship.

Research Training and Support Grant (RTSG)

A generous allowance will be provided for research consumables and for attending UK and international conferences, and specialist training, as required.

Project Focus: This study examines glycosylation which is a key post-translational modification and its impact on enzyme stability and activity. We will investigate two industrially relevant classes: glycosyl hydrolases and metalloproteases. Emphasis will be on glycosylation patterns to identify strategies that enhance structural integrity, protease resistance, and performance in home-care formulations.

Glycosylation is one of the most critical PTMs, involving the attachment of sugar moieties (glycans) to proteins. The two most common types are:

• N-linked glycosylation: Glycans are attached to the nitrogen atom of asparagine residues.
• O-linked glycosylation: Glycans are attached to the oxygen atom of serine or threonine residues.

Industrial Relevance: Enzymes are widely used across industries from pulp and paper to biofuels. In home-care applications, enzymes play a key role in sustainable cleaning, reducing reliance on fossil fuels and lowering the carbon footprint. However, many wild-type enzymes are unstable in home-care formulations due to surfactants and other cleaning ingredients like proteases, significantly lowering enzyme efficacy; therefore, methods to enhance stability are pertinent.

Hypotheses:

1. Glycosylation enhances structural and proteolytic stability of enzymes.
2. The type, size, and extent of glycosylation significantly influence enzyme activity and stability.
3. Specific glycosylation patterns can optimize both stability and activity.

Methodology: To test these hypotheses, we will use glycoproteomics, biochemical assays, structural bioinformatics, and enzyme activity measurements.

Please apply via this link: https://unidla.org/apply/. You should follow all instructions in the form on this webpage.

Anonymised applications will be reviewed by a panel of academic staff following the closing date.

Guidance for applicants is available here: https://unidla.org/unidla-guidance-for-applicants/.

Successful applicants only will be advised to submit a formal application through the University of Liverpool Application Portal at the relevant time.

This project is funded by BBSRC and Unilever for Home students.

Stipend

Students will receive a tax-free stipend for each year of study. The stipend amount will be the UKRI minimum rates (£21,805 for 2026/27) plus an annual Unilever-funded supplement of £4500. Additionally, £2,000 per annum London Weighting Allowance will be offered for students registered in London-based Universities.

Tuition fees

All home tuition fees will be fully covered by the studentship.

Research Training and Support Grant (RTSG)

A generous allowance will be provided for research consumables and for attending UK and international conferences, and specialist training, as required.