Due to an increasing demand of fossil fuels, the search for alternative bioenergy has gained much attention from the scientific community and the general population.
During recent years, this research has been focused on the called second-generation biofuels, where waste or by-products are used as raw materials for the ethanol production, comparing to the first-generation, where sugars and starch were used. The use of agro-industrial wastes, such as corn, wheat straw or bagasse, has gained much attention to be an alternative source, obtaining eco-friendly fuels. The main challenge of utilizing this agro-industrial wastes is to obtain an efficient sugar release, mainly from cellulose. In order to achieve this, an efficient pre-treatment step followed by enzymatic hydrolysis have to be applied (1). Generally, the pre-treatment process contributes to increased costs of the whole process (1).
In addition, the production of robust enzymes, mainly cellulases, has become a problem because of the need of thermostable proteins to overcome the increase in the temperature obtained in the process.
Coffee is one of the most consumed beverages worldwide. The direct discharge of coffee residue waste (CRW) into the environment without treatment could lead to serious environmental problems.
Extremophiles from several parts of the world represent excellent sources of potential enzymes for the Bioethanol production.
In this proposal, we will dissect the ability of extremophiles to degrade cellulose and galactomannan from coffee waste. We will identify the enzymes involved in the metabolism of these glycans with the long-term goal to understand and improve the anaerobic conversion of coffee waste materials into bioethanol.
• Isolate the different glycans in coffee waste, including cellulose and galactomannan.
• Define the ability of diverse extremophiles on different glycans from coffee wastes.
• Identify and characterize the genes involved in this metabolism through enzyme kinetics and structural biology.
(1) Abo et al. (2019) Reviews on Environmental Health 34, 57-68.
Eligibility and How to Apply:
Please note eligibility requirement:
• Academic excellence of the proposed student i.e. 2:1 (or equivalent GPA from non-UK universities [preference for 1st class honours]); or a Masters (preference for Merit or above); or APEL evidence of substantial practitioner achievement.
• Appropriate IELTS score, if required.
• Applicants cannot apply for this funding if currently engaged in Doctoral study at Northumbria or elsewhere.
For further details of how to apply, entry requirements and the application form, see https://www.northumbria.ac.uk/research/postgraduate-research-degrees/how-to-apply/
Please note: Applications should include a covering letter that includes a short summary (500 words max.) of a relevant piece of research that you have previously completed and the reasons you consider yourself suited to the project. Applications that do not include the advert reference (e.g. SF20/…) will not be considered.
Deadline for applications: 1st July for October start, or 1st December for March start
Start Date: October or March
Northumbria University takes pride in, and values, the quality and diversity of our staff. We welcome applications from all members of the community. The University holds an Athena SWAN Bronze award in recognition of our commitment to improving employment practices for the advancement of gender equality.
Please direct enquiries to Dr Jose Munoz ([email protected]
Manzano-Nicolas, J.; Marin-Iniesta, F.; Taboada- Rodriguez, A.; Garcia-Canovas, F.; Tudela-Serrano, J; and Muñoz- Muñoz, J. (2019) Development of a method to measure laccase activity on methoxyphenolic food ingredients and isomers. Int. J. Biol. Macromol. Accepted.
Ndeh, D.; Muñoz-Muñoz, J.L.; Cartmell, A.; Bulmer, D.; Wills, C.; Henrissat, B.; Gray, J. (2018). The human gut microbe Bacteroides thetaiotaomicron encodes the founder member of a novel glycosaminoglycan-degrading polysaccharide lyase family PL29. J. Biol. Chem. 293(46):17906-17916 (doi: 10.1074/jbc.RA118.004510.).
Muñoz-Muñoz, J.L.; Cartmell, A.; Terrapon, N.; Henrissat, B. and Gilbert, H.J. (2017) An evolutionarily distinct family of polysaccharide lyases removes rhamnose capping of complex arabinogalactan proteins. J. Biol. Chem. 292 (32) 13271-13283.
Muñoz-Muñoz, J.L.; Cartmell, A.; Terrapon, N.; Henrissat, B. and Gilbert, H.J. (2017). Unusual active-site location and catalytic apparatus in a glycoside hydrolase family. Proc Natl Acad Sci 114 (19) 4936-4941.