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澳洲麦考瑞大学Enzymatic synthesis和Smart peptides方向招收CSC博士生已有2人参与
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PROJECT 1: Smart peptides for the design of functional proteinbased nanoparticles PROJECT DESCRIPTION: The overexpression of recombinant proteins in E. coli often leads to their aggregation into protein deposits or inclusion bodies. These insoluble protein aggregates are highly pure protein deposits that in some cases may represent up to 95% of the cell total protein content. Insoluble bacterial protein aggregates are very interesting since they can act as protein-based nanoparticles. In recent years, the practical application of protein-based nanoparticles has expanded rapidly into areas like drug delivery, vaccine development, and biocatalysis. This project will exploit the aggregating property of a unique protein domain to design modular proteins structures that contain at least two functionally distinct regions; (a) an aggregating part capable of forming insoluble protein-based nanoparticles and (b) a biomolecule (enzyme, peptide, antibodybinding protein, etc) displayed on the surface of the protein-based nanoparticle. The project will utilise several molecular and protein biochemistry techniques to develop modular protein-based nanoparticles with several functionalities for applications in biocatalysis, nanobiotechnology and biomedicine. PROJECT 2: Cell-free enzymatic synthesis of platform chemicals PROJECT DESCRIPTION: The enzyme-catalysed transformation (biocatalysis) of cheap, renewable substrates into valuable bulk or specialty chemicals is a promising technology for sustainable and green manufacturing. Advances in enzyme expression systems, enzyme engineering, in silico modelling and prediction of enzyme kinetics has facilitated the assembly of enzyme into synthetic and highly efficient production pathways. This concept has recently been implemented to design enzyme pathways in a cell-free context as opposed to the traditional approach of utilising microbial hosts. Cell-free biotechnology is one of the promising approaches that offer complementary advantages to in vivo metabolic engineering, allowing for high control over reaction conditions, enzyme ratios and pathway flux. We have recently established two novel cell-free multi-enzyme pathways for the bioconversion of renewable organic waste into valuable bio-based building blocks for industrial applications. This PhD project will deal with the combination, optimisation and/or modification of the developed pathways to improve substrate utilisation and product yields. The project will use an array of biochemical methods such as: discovery or design of new enzymes, enzyme engineering, high throughput flux analysis, kinetic modelling and bioprocess engineering. CANDIDATE REQUIREMENTS: The successful student will join a dynamic and motivated team with a multidisciplinary approach to research. The ideal candidate must have a strong background in molecular biology and/or synthetic biology, biotechnology or biochemistry. Practical expertise in protein expression and purification, enzyme kinetics and characterisation as well as HPLC analysis is highly desirable. In addition, the applicant will have a demonstrated aptitude for undertaking and managing laboratory work independently, an understanding of the field, and excellent communication skills. APPLICATION PROCESS: China Scholarship Council (CSC) - Macquarie University Joint Postgraduate Scholarship Program. The deadline for submission is January 31, 2019. More information can be found here: https://www.mq.edu.au/research/p ... /scholarshipsearch/ data/china-scholarship Please apply ONLY if you have: • Completed a 2-years Master of Research and examined Master’s Thesis • Excellent academic records • Evidence of peer-reviewed research activity, such as publications and/or conference presentations • Proof of English Proficiency either through an academic IELTS or a TOEFL test. Please see here the required levels of English proficiency. Send your detailed CV and transcripts for assessment to: A/Prof Anwar Sunna (anwar.sunna@mq.edu.au). For more information visit www.sunnalab.org |
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