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BIOCHEMISTRY AND BIOTECHNOLOGY OF PROTEINS
FABIO TANFANI

Seat Scienze
A.A. 2016/2017
Credits 8
Hours 64
Period 1^ semestre
Language ENG
U-gov code SM04 5S423

Prerequisites

Gary Walsh. Proteins, Biochemistry and Biotechnology. John Wiley and Sons, LTD

Development of the course

The course consists of eight credits (64 hours). The course is implemented both through classroom lectures using power point presentations (seven credits) handed out to students, as well as through seminars prepared by small groups of students on topics proposed by the teacher, and seminars on specialized topics given by the teacher and/or his colleagues (one credit).
The course aims to teach students about protein biochemistry and about strategies for the purification of soluble and membrane proteins on laboratory and industrial scale. Moreover, the course aims to teach students about the application of non-catalytic proteins and enzymes in the food, pharmaceutical, and chemical industries.

Learning outcomes

Knowledge:
At the end of the course, the students will be familiar with protein biochemistry, with factors that stabilise/destabilise proteins, and methods used to purify membrane proteins, non-catalytic proteins and enzymes on laboratory and industrial scale. Moreover, the students will be familiar with the applications of different classes of non-catalytic proteins and enzymes in the food, pharmaceutical, and chemical industries.

Ability to apply the knowledge:
The students should be able to plan purification methods for membrane proteins, non-catalytic proteins and enzymes bearing in mind the protein biochemistry, the wanted degree of purification, the costs, and the use of a specific protein in a particular field of industry. Moreover, the students should be able to ponder possible and potential applications of a specific protein in a particular industrial sector.

Soft skills:
The students should be able to communicate clearly the knowledge and the related rationale. The communication ability, the capacity to work in groups and the ability to analyse and summarise information will be experienced through seminars prepared by small groups of students on topics given by the teacher. The preparation of the seminars and their presentation in the lecture room will encourage students to interact and communicate between themselves and with the teacher.

Program

Cells as factories for the production of proteins for biomedical, analytical and industrial applications.
Globular, fibrous and membrane proteins. Post-translational modification. Importance of side-chains on structure-function of proteins. Folding, misfolding, denaturation. Destabilising factors of protein structure: detergents, organic solvents, oxidant and chaotropic agents, temperature, pH, freezing/thawing. Stabilisation and storage of proteins: stabilising agents, cooling, freeze-drying, spray drying, sterilization, preservation.
Protein sources: proteins from animals, plants, and from mesophilic and extremophile organisms; protein production from genetically engineered organisms. Screening of new enzymes. Homogenization of tissues and cells on a laboratory and industrial scale.
Strategies for the purification of soluble proteins. Solubility and fractional precipitation with temperature and pH changes, with the addition of organic solvents, salting-out and salting-in. Main chromatographic techniques for the purification of proteins on a laboratory and industrial scale. Methods for purification of membrane proteins and for their reconstitution into liposomes.
Purification of exocellular and endocellular proteins of industrial, biomedical, pharmaceutical and analytical interest. Scale-up of the protein extraction and purification process. Proteins as inclusion bodies: solubilisation and refolding methods. Technical and economic implications for different strategies of protein purification.
Proteins and enzymes for industrial applications: Immobilized enzymes, immobilization techniques, bioreactors. Biosensors: principles and applications. Proteases: classification and industrial uses. Carbohydrases: applications of alpha-amylase, beta-amylase, glucoamylase, alpha-(1-6) glucosidase, and glucose isomerase. Enzymes able to hydrolyse cellulose, hemicellulose, and pectin. Lipases and their applications. Milk proteins. 
Enzymes and proteins for medical, pharmacological, analytical, and food applications. Microbial, viral, and pyrogenic contaminants. Blood products, enzymes and antibodies for analytical and therapeutic applications, hormones, growth factors, cytokines, tumoral necrosis factors, interferons, interleukins. 

Development of the examination

Methods for assessing learning outcomes:
The assessment method is an oral examination that takes 30-40 minutes.

Criteria for assessing learning outcomes: 
The assessment method is an oral examination directed to evaluate the knowledge and understanding of protein biochemistry and of the other course topics necessary to solve problems related to the course objectives.

Criteria for measuring learning outcomes:
The final mark is out of 30. Successful completion of the examination will lead to grades ranging from 18 to 30, and 30 cum laude.

Criteria for conferring final mark:The final mark is attributed on the basis of the answers to three questions and on the basis of the quality of the seminars given by the students. The student seminars will contribute to the final mark for not more than two points. The laude is attributed when the student demonstrates complete mastery of the matter.

Recommended reading

Gary Walsh. Proteins, Biochemistry and Biotechnology. John Wiley and Sons, LTD;

Courses

• Biologia molecolare e applicata