How do structural changes of dairy proteins affect the functionality of bioactive compounds in complex food matrices?

• Grant number: 17/09214-4
• Support Opportunities: Research Grants - Young Investigators Grants
• Start date: March 01, 2018
• End date: February 28, 2023
• Field of knowledge: Agronomical Sciences - Food Science and Technology - Food Science
• Principal Investigator: Guilherme Miranda Tavares
• Grantee: Guilherme Miranda Tavares
• Host Institution: Faculdade de Engenharia de Alimentos (FEA). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
• Associated researchers: Lusânia Maria Greggi Antunes
• Associated research grant(s): 18/03822-5 - Multi-user equipment approved in grant 2017/09214-4: preparative chromatography system - Akta pure (Ge healthcare), AP.EMU
• Associated scholarship(s): 19/15143-8 - Distribution of carotenoids in complex protein matrices: an approach by heat maps, BP.MS; 18/24481-1 - Purification of milk proteins at pilot scale using membrane filtration and preparative chromatography, BP.IC; 18/09304-6 - Interaction between carotenoids and native and non-native globular proteins from milk: structural and functional effects in mono and multi protein systems, BP.DD

Abstract

Milk proteins represent around 30% of the total protein ingested by adult from western countries. Although in their native state these proteins have as one of their functions the transport of molecules, they are present in foods in various structural states, reflecting the diversity of processes applied by food industries. Even if the impact of the structural changes of milk proteins on the technical-functional properties of foods (e.g. viscosity) is known, the understanding of their effect on the functional properties (health claims) of these foods is still under construction. It is agreed that food matrices are not inert to the addition of bioactive compounds; however, generally, the development of functional foods is based on the simple incorporation of these compounds into food matrices, ignoring the interaction between the food matrix and the bioactive compound. Thus, to guide the development of functional foods and ensure the associated health claims, it is crucial to understand how the structural changes induced to protein-rich food matrices affect the biological activity of bioactive compounds. In this framework, this research project proposes a reverse engineering strategy to generate knowledge that allows predicting the behavior of carotenoids in protein-rich matrices submitted to different industrial processes. By means of the association of results obtained in real and model matrices it is expected to establish generic rules for the behavior (interaction/biological activity) of carotenoids in complex multi-protein matrices. In addition to the scientific community, the knowledge generated by this project will also interest companies in the area of functional foods, as well as regulatory committees. (AU)

Scientific publications

(10)

(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)

NUNES, LAUANE; TAVARES, GUILHERME M.. Thermal treatments and emerging technologies: Impacts on the structure and techno-functional properties of milk proteins. TRENDS IN FOOD SCIENCE & TECHNOLOGY, v. 90, p. 88-99, AUG 2019. (17/09214-4)

VIDOTTO, DANILO C.; TAVARES, GUILHERME M.. Impact of Dry Heating in an Alkaline Environment on the Structure and Foaming Properties of Whey Proteins. Food and Bioprocess Technology, v. 13, n. 10, AUG 2020. (17/09214-4, 18/09304-6, 18/03822-5)

RODRIGUEZ, MARTIN DANIEL AYA; VIDOTTO, DANILO C.; XAVIER, ANA AUGUSTA O.; MANTOVANI, RAPHAELA A.; TAVARES, GUILHERME M.. Does the protein structure of ?-lactoglobulin impact its complex coacervation with type A gelatin and the ability of the complexes to entrap lutein?. FOOD HYDROCOLLOIDS, v. 140, p. 10-pg., 2023-03-08. (18/03822-5, 17/09214-4, 18/23752-1)

VIDOTTO, DANILO C. C.; MANTOVANI, RAPHAELA A. A.; TAVARES, GUILHERME M. M.. High-pressure microfluidization of whey proteins: Impact on protein structure and ability to bind and protect lutein. Food Chemistry, v. 382, p. 8-pg., 2022-07-15. (17/09214-4, 18/23752-1, 17/26237-8, 18/09304-6, 18/03822-5)

MANTOVANI, RAPHAELA ARAUJO; HAMON, PASCALINE; ROUSSEAU, FLORENCE; TAVARES, GUILHERME M.; MERCADANTE, ADRIANA ZERLOTTI; CROGUENNEC, THOMAS; BOUHALLAB, SAID. Unraveling the molecular mechanisms underlying interactions between caseins and lutein. Food Research International, v. 138, n. B, DEC 2020. (17/26237-8, 18/18374-8, 13/07914-8, 17/09214-4)

VIDOTTO, DANILO C.; TAVARES, GUILHERME M.. Simultaneous binding of folic acid and lutein to ?-lactoglobulin and ?-lactalbumin: A spectroscopic and molecular docking study. FOOD BIOSCIENCE, v. 50, p. 9-pg., 2022-12-01. (18/03822-5, 17/09214-4, 18/09304-6, 18/23752-1)

MANTOVANI, RAPHAELA A.; XAVIER, ANA AUGUSTA O.; TAVARES, GUILHERME M.; MERCADANTE, ADRIANA Z.. Lutein bioaccessibility in casein-stabilized emulsions is influenced by the free to acylated carotenoid ratio, but not by the casein aggregation state. Food Research International, v. 161, p. 15-pg., 2022-08-27. (14/14457-5, 17/09214-4, 17/26237-8, 13/07914-8, 18/23752-1)

NUNES, LAUANE; HASHEMI, NEGIN; GREGERSEN, SANDRA BEYER; TAVARES, GUILHERME M.; CORREDIG, MILENA. Compartmentalization of lutein in simple and double emulsions containing protein nanoparticles: Effects on stability and bioaccessibility. Food Research International, v. 173, p. 9-pg., 2023-09-01. (17/09214-4)

RASERA, MARIANA L.; DE MARIA, ANA LUIZA A.; TAVARES, GUILHERME M.. Co-aggregation between whey proteins and carotenoids from yellow mombin (Spondias mombin): Impact of carotenoids' self-aggregation. Food Research International, v. 169, p. 11-pg., 2023-04-27. (18/03822-5, 17/09214-4, 19/15143-8, 18/23752-1)

MANTOVANI, RAPHAELA ARAUJO; HAMON, PASCALINE; ROUSSEAU, FLORENCE; TAVARES, GUILHERME M.; MERCADANTE, ADRIANA ZERLOTTI; CROGUENNEC, THOMAS; BOUHALLAB, SAID. Unraveling the molecular mechanisms underlying interactions between caseins and lutein. Food Research International, v. 138, p. 9-pg., 2020-12-01. (18/18374-8, 17/26237-8, 17/09214-4, 13/07914-8)