| Code |
12477
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| Year |
1
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| Semester |
S1
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| ECTS Credits |
6
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| Workload |
PL(30H)/T(30H)
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| Scientific area |
Biotecnologia
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Entry requirements |
Not applicable.
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Mode of delivery |
Presential
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Work placements |
Not applicable.
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Learning outcomes |
Know and describe the main methods of enzyme immobilization. Understanding the importance of application of adimension numbers in fixed systems. Characterization and modulation of unconventional systems (organic solvents, ionic liquids, supercritical fluids). Scale immobilized reactors: design equations, normalized residence time and degree of conversion. Develop enzyme deactivation calculation models. Acquiring laboratory handling in the preparation of immobilized cell systems. Carry out, evaluate and compare the intrinsic kinetic parameters of free and immobilized enzyme systems. Develop creative, integrative and innovative capacity in solving problems in enzyme biotechnology.
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Syllabus |
Theoretical: Enzyme immobilization methods (crosslinking, adsorption, ionic bond, covalent bond, microencapsulation and occlusion). Effects conformational, stereochemical, partition. Mass transfer (Damkhöler, Biot, internal and external effectiveness factor). Catalysis in unconventional systems: (1) Organic solvents (selection, toxicity, concentration profiles), (2) ionic liquids (structure, chemical and physical properties, CO2-sc extraction, applications), (3) Supercritical fluids (physics and chemistry characterization, diffusivity, toxicity, environmental impact, removal), (4) Nanobiocatálise (gold particles). Modelling discontinuous enzymatic reactors and continuous flow type piston. Enzyme deactivation. Pratical: Saccharomyces cerevisiae immobilized in sodium alginate microspheres. Sucrose hydrolysis kinetics.Immobilization of Tirocinase Pyrocatecol for conversion of L-DOPA.
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Main Bibliography |
1-”Engenharia Enzimática”, Joaquim M.S. Cabral, Maria Raquel Aires-Barros, Lidel, 2003. 2-”Biochemical Engineering”, Harvey W. Blanch, Douglas S. Clark MARCEL DEKKER 1997. 3- Principles of Fermentation Technology, 2nd Edition, Stanbury, Whitaker & Hall, BH 1995. 4- Homaei A. Enzyme Immobilization and its Application in the Food Industry. Advances in Food Biotechnology, 2016, doi:10.1002/9781118864463.ch09. 5- Potdar MK, Kelso GF, Schwarz L, Zhang C, Hearn MTW. Recent Developments in Chemical Synthesis with Biocatalysts in Ionic Liquids, 2015, Molecules, 20: 16788-16816; doi:10.3390/molecules200916788. 6- Gomes et al., ”Tyrosinase immobilization in nickel-crosslinked gellan microspheres and conversion of L-DOPA to dopachrome”, Journal of Chemical Education, 2021. 7- Sojitra UV, Nadar SS, Rathod VK. A magnetic tri-enzyme nanobiocatalyst for fruit juice clarification, 2016, Food Chemistry, 213: 296-305.
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Teaching Methodologies and Assessment Criteria |
Theoretical in a face-to-face model and with a weight of 65% in the final classification. During the teaching-learning period (TLP), the minimum grade to pass the theoretical component is 9.5, after the arithmetic average of the two tests to be carried out (November 5, 2024 and December 20, 2024).
The minimum classification for admission to the final exam is 9.5 points in the practical component.
- Practices in person have a weight of 35% in the final classification. Practical test (December 10, 2024) with 50 questions on the topics taught with a discount of 0.10 values on PEM type questions, without any type of discount on multiple answer questions (True/False and multiple answers). Practical test (30%) and laboratory performance (5%).
It is mandatory to pass practical classes, with a minimum grade of 9.5.
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Language |
Portuguese. Tutorial support is available in English.
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