Interactions structures & functionalities team objectives

HAL Id: hal-02097221

https://hal.archives-ouvertes.fr/hal-02097221

Submitted on 4 Jun 2020

HAL is a multi-disciplinary open access archive for the deposit and dissemination of sci- entific research documents, whether they are pub- lished or not. The documents may come from

L’archive ouverte pluridisciplinaire HAL, est destinée au dépôt et à la diffusion de documents scientifiques de niveau recherche, publiés ou non, émanant des établissements d’enseignement et de

To cite this version:

Said Bouhallab. Interactions structures & functionalities team objectives. STLOpendays, Institut

National de Recherche Agronomique (INRA). UMR UMR INRA / AgroCampus Rennes : Science et

Technologie du Lait et de l’?uf (1253)., Mar 2019, Rennes, France. �hal-02097221�

Interactions-Structures Functionalities

team objectives

Saïd BOUHALLAB - STLO

STLOpen Days 19-21 March 2019

Id card of the ISF team

2

Pascaline H. Stéphane P. Marie-Hélène F.

Valérie B.B. Thomas C. Fanny G.

 14-16 persons

- 9 permanent staff (6 scientists)

Amira H. Julien B. Raphaela M.

(PhD) (PhD) (PostDoc)

Dimitri W. Tatiana M.

(Contractual projects)

Currently : 5 young scientists

- 5 to 8 non-permanent staff

STLOpen Days 19-21 March 2019

Id card ISF team: strengths

3

 Skills / expertise

Biochemistry Physico-chemistry Rheology - Interface

Spectroscopy - Microscopy

 Knowledge / know-how

Milk and egg proteins: purification - structures Phase separation – osmotic pressure

Molecular interactions (proteins// ligands) Multiscale characterizations

Statistics and data treatments

Id card ISF team: partnership

 Relevant collaborations

- National: INRA (BIA Nantes; UMET-Lille); IPR, Rennes 1; Oniris, Nantes;

IMMM, Univ. Le Mans; ESPCI, Paris; Synchrotron Soleil; LLB-Saclay (neutrons)

- International: Univ. Campinas & Viçosa, Brazil; Univ. Laval, Canada; NRC, Ottawa, Canada; Teokem-Univ. Lund, Sweden; Univ. Aberystwyth, Wales - Research network: Biophysics Great West Network (regional); Soft matter

national network (GDR SLAMM)

 Industrial partnership

- BBA, The consortium of ten French dairy companies (pre-competitive) - French national inter-professional center for the dairy industry (CNIEL) - Chr. Hansen, bioscience company

 15-20 publications/year

(Food / Dairy science; Interfaces; Physico-chemistry of colloids, polymers)

STLOpen Days 19-21 March 2019

Id card ISF Team: Funding

5 CNIEL

Chr. Hansen

 Ongoing private funding

Brittany Region Government Foundation

 Public funding (Research expenses; thesis & postdoc scholarships)

Profil: a six year interregional research project on protein functionalities (partners: public lab. & BBA; coord.: INRA) Research and Innovation in the Mediterranean Area

6

Research field & objectives

Relationship

interactions – assemblies - functionalities of proteins (caseins, globular proteins)

 Objectives

deliver fundamental knowledge, new functional structures and application concepts for academic and industrial partners;

obtain new knowledge on the interactions and assemblies of proteins, to enable more effective innovations;

elaborate type of assemblies that provide optimal properties at macroscopic scale (product);

relate the macroscopic to the molecular scale. A scientifically challenging

objective from a physics point of view.

7 1. Process-induced protein assemblies

Generation of ingredients with various functional properties Irreversible associations (covalent interactions)

Aggregation mechanisms and kinetics are well-described in model systems 2. Spontaneous proteins assemblies

Fundamental characteristic of biological systems (regulation, activity,…) Reversible associations (non-covalent interactions)

Important field in biology. Increasing interest in food science

Functional properties (assembly/disassembly of food products)

Improve/create

Nano-micro biomaterials (protection/vectorization)

design

Motivations of studying food protein interactions and

assemblies?

Research context

Our research strategy: Two round-trip approaches

Systems with increasing complexity

Real matrices

Basic

knowledge Applications

Macroscopic

Molecular

Our facilities

9

Equipements At lab In collaboration

Separation/

analyses

Chromatography, membrane filtration

Field Flow Fractionation - Malls

Multiscale structural Characterisations

Spectroscopy (UV, IRTF) Rheology /Texture Mass spectrometry Light scattering (DLS)

Microscopy (optical, confocal, AFM)

Turbiscan DSC

▪ Microscopy (TEM, SEM, Brewster angle)

▪ Interfacial tools

▪ Scattering (RX, light, neutrons)

▪ NMR

Interactions Calorimetry (ITC) Fluorescence

AFM

Simulation/molecular &

mesoscopic modelling

Fractal (50-200 nm) Microgel

(100-400)

Fibrils microparticles

(…100 µm)

Complex coacervates

(5 µm) CN/WP complexes (…200 nm)

Structural changes Interactions

Processing

Physico-chemical environment

General research lines & ambition

10

Globular proteins Casein micelles

Oil-water interface

Emulsions

Encapsulation/

Protection/

Delivery

Air-water interface

Foams

Sol-Gel transitions

Texture

Yogourt

Cheese

Nutritional quality

Relative Digestibility

11

 General topics



Interaction mechanisms in highly concentrated protein systems



Interfacial behaviour and foaming properties



Protein Interactions/assemblies and subsequent properties

Topics and Research projects

Simplified systems

 Specific projects



Mechanisms behind heteroprotein complex coacervation (liq/liq) and subsequent application for encapsulation of small bioactives



Understanding interactions between caseins and carotenoids at molecular level



Swelling of dry heated protein microparticles in different physico- chemical conditions



Heat treatment - physicochemical properties and nutritional quality of proteins (coll. BN team)



Balance of inter and intra casein micelle interactions during enzymatic coagulation of milk



Changes of the physicochemical characteristics of the casein micelles and related -acid/rennet- gelling properties upon successive thermal treatments

Complex Systems

Real matrices

Examples of research activity

interfacial and foaming properties of proteins to illustrate the soft matter approach

Four posters

13

THANK YOU

MERCI

13

STLOpen Days 19-21 March 2019

Miranda-Tavares, G. et al. (2014). Milk proteins as encapsulation devices and delivery vehicles: Applications and trends.doi.org/10.1016/j.tifs.2014.02.008.Trends in Food Science and Technology, 37, 5-20.

Guyomarc'h, F. et al. (2015). Current ways to modify the structure of whey proteins for specific functionalities-a review.Doi 10.1007/s13594-014-0190-5. Dairy Science and Technology, 95, 795-814.

Schong, E., Famelart, M.H. (2017). Dry heating of whey proteins.doi.org/10.1016/j.foodres.2017.08.057.

Food Research International, 100, 31-44.

Croguennec, T., et al. (2017). Heteroprotein complex coacervation: A generic process.

doi.org/10.1016/j.cis.2016.06.009.Advances in Colloid and Interface Science, 239, 115-126.

Boire, A. et al. (2019). Soft Matter Approaches for Food Proteins Interactions & Assemblies.

doi.org/10.1146/annurev-food-032818-121907.Annual Review of Food Science & Technology.

Gagnaire, V. et al. (2019). The role of proteins in the development of food structure. F. Spyropoulos et al.

(Eds.). Handbook of Food Structure Development. RSC, London.To be published soon.

Recent relevant reviews