Objective
The main goal of the project is to unveil the potential of the method of limited proteolysis as a tool for conferring added value and targeted properties to proteins obtained from crops (pea, faba bean, lupin and sunflower) cultivated both in INTAS and NIS countries. Main storage seed proteins of the aforementioned crops (11S globulins of pea, faba bean, lupin and sunflower and a group of 7S globulins of lupin) will be the research objects.
Two main groups of compounds will be studied:
i. proteins, both native and modified through the limited proteolysis, and;
ii. peptides, which are liberated in the course of the limited proteolysis (Task1).
In the first case, thermodynamic parameters of thermal denaturation, rate constants of the co-operative hydrolysis, surface hydrophobicity, surface tension, surface rheological properties as well as a set of functional properties will be determined (Tasks 3, 5, 8). To explain the peculiarities of thermodynamic and kinetic characteristics of legumins (11S globulins of pea, faba bean and lupin), the hydrophobic cluster distribution along the polypeptide chains and the probable sites of enzyme attack will be analysed (Tasks 2, 4). The studies carried out will shed light on the structural changes of the proteins during their limited and superlimited (Task 7) proteolysis and the effects of these changes on their functional properties. Along with individual proteins, globulins from pea and faba bean meals modified through induced autolysis, the biotechnological process developed by one of the participating teams, will be studied. The possibility to use the method of the limited proteolysis for the improvement of functional properties of sunflower protein isolates produced from industrial solvent cake will also be elucidated (Task 1). The composition and amino acid sequences of peptides liberated during the limited proteolysis of pea, faba bean and lupin globulins with trypsin will be determined and their potential biological activity will be checked by means of the data bank (Task6). Screening tests showing up a potency of those peptides, as well as low-molecular mass products of the induced autolysis of pea and faba bean meals, to influence proliferation and viability of cultured transformed cells will allow establishing the most complete set of biological activities. The chelating and binding properties toward metal ions and other peptides respectively will also be investigated (Task 9).
The realization of tasks 2-4 will give the phenomenological picture of the limited proteolysis effects on the physico-chemical and functional properties of the selected seed proteins and will reveal the changes in protein structure, which underlie these effects.
Thus, the implementation of the project will:
i. substantially increase our understanding of limited proteolysis effects on the structure, physico-chemical and functional properties of seed proteins, including the products of industrial treatment of seeds, and of the impact of these modifications on potential food and non-food applications and;
ii. show the possibility of using low-molecular products of the limited proteolysis of selected proteins, including protein components of modified meals of grain legumes, as components of functional foods, nutraceuticals and clinically active substances.
The teams, which will take part to the project, have complementary experience in studies on physical chemistry and biochemistry of seed proteins (CO, CR1, CR2, CR3, CR4, see below) and structure analysis and biological activity of peptides (CO,CR5, see below).
Teams which participate to the project:
CO-Dipartimento di Scienze Molecolari Agroalimentari, State University, Milano, Italy
CR1-PROCHEM - Institute of Applied Protein Chemistry, Kleinmachnow, Germany
CR2-Lab. of Food Chemistry and Technology, Aristotle University, Thessaloniki, Greece
CR3-Lab. of Protein Chemistry, State University of Moldova, Kishinev, Moldova
CR4-Lab. of Food Biotechnology, Institute of Biochemical Physics, RAS Moscow, Russia
CR5-Lab. of Regulatory Peptides, Institute of Bioorganic Chemistry, RAS Moscow, Russia
Call for proposal
Data not availableFunding Scheme
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20133 Milano
Italy