Engineering of oat proteins towards improved functionality. Dr Nesli Sözer Principal Investigator VTT Technical Research Centre of Finland Ltd
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1 Engineering of oat proteins towards improved functionality Dr Nesli Sözer Principal Investigator VTT Technical Research Centre of Finland Ltd
2 Why plant proteins?
3 How to feed the protein demand of 9 M people? Animal proteins: Red and white meat, dairy, eggs, farmed fish and insects The protein system Alternative proteins: Microalgae, bacteria, mycoprotein, synthetic proteins Plant proteins: Pulses, nuts, seeds, legumes and grains
4 Global livestock production (Mton) A trend towards lower production rate for pork and beef beef pork poultry Data based on FAO: Year
5 EU meat consumption (kg/capita, retail weight) Meat consumption will decline Economic crisis & lack of supply Today Year
6 Plant proteins are a megatrend: the number of flexitarians and vegetarians is on the rise
7 Challenges
8 Challenges of plant proteins in food production Technological functionality Solubility Water retention Foaming / emulsifying agents Gelling Heat stability ph stability Sensory quality Bitter taste - peptides, impurities, processing history Astringency originates from interactions with saliva proteins Nutritional requirements Amino acid composition Anti-nutritional factors Protein digestibility Toxicity Allergenicity
9 Oat protein
10 Oat proteins High protein content Distinct protein composition compared to other cereals Digestibility comparable to rice and corn Oat protein fractions according to Osborne protein solubility % of total protein* pi Solubility Similar to soy glycinin and other legumin-like (11S) storage proteins Globulins mostly 5.5 -polypeptide polypeptide Albumins (mostly enzymes ) soluble in dilute salt solutions water soluble Prolamins (avenin) soluble in aqueous ethanol Glutelins (residue) <10 - soluble in dilute acids or alkalis *shows wide differences depending on the cultivar and growth conditions (climate, soil quality etc.)
11 Oat fractionation technology for protein and β-glucan concentration Oat grains Extraction Lipids Distribution density, % Milling and air classification Distribution density, % Betaglucan Starch Protein VTT patent: US A1
12 Soluble protein (%) The Oatpro concentrate was in native form and more soluble than the commercial oat protein Commercially available oat protein concentrate vs. high protein oat fraction from SC-CO 2 extracted oats Protein concentration range between 20 60%. Rest is mainly starch or maltodextrin. 50 ph 6.5, 1 M NaCl ^exo OPC_BIOVELOP 75 kost :52:31 Differential scanning calorimetry (DSC) thermogram Commercial BIOVELOP 75% kost., :13:30 BIOVELOP 75% kost., 9,0570 mg Oatpro conc VTT OPC 75% kost., :54:39 VTT OPC 75% kost., 8,9350 mg Integral -0,98 mj normalized -0,11 Jg^-1 Peak 92,55 C 20 2 mw Integral -18,77 mj normalized -2,10 Jg^-1 Peak 63,81 C Starch gelatinisation 64 C Integral -5,70 mj normalized -0,64 Jg^-1 Peak 89,70 C 10 0 Commercial Oatpro conc Lab: METTLER Integral -62,76 mj normalized -7,02 Jg^-1 Peak 110,91 C Protein denaturation 111 C C min STAR e SW 9.30
13 Oat protein is alkaline soluble Oat protein isolate (OPI) was obtained from SC-CO 2 extracted oat protein concentrate by alkaline extraction + isoelectric precipitation ph
14 Oat protein functionalization
15 Strategies to modify oat protein functionality Hydrolysis Cross-linking Net charge (electrostatic stabilisation) Conjugation with polyelectrolytes (steric stabilisation) Homogenization (high pressure microfluidization) Heat treatment High hydrostatic pressure
16 Crosslinking by transglutaminase (TG) improved colloidal stability of oat protein isolate (OPI) nkat TG /g protein Control TG -treated Ercili-Cura et al., 2015, Nivala et al., 2017
17 Crosslinking by TG improved the foaming properties of OPI Foaming properties (foam height and foam stability) of oat protein isolate improved upon TG treatment. Tyrosinase treatment caused decreased foam height in oat protein foams, which may be attributed to decreased solubility with crosslinking. Nivala et al., 2017
18 Addition of pectin improved dispersion stability at acidic ph Oat protein isolate dispersion was mixed with different concentrations of pectin Solubility of proteins at isoelectric point was greatly increased. Protein particles were negatively charged. Without pectin + With pectin
19 What happens in a less pure system? Gel-like structure for Dispersed oat protein concentrate Protein conc.: 2.4 % 4.6% 8.5% 12% 20% High hydrostatic pressure Pressure: 300, 600 MPa Temperature: C Duration: 15 minutes Heat Temperature: 40, 60, 80 C Duration: 15 minutes 12% protein OPC at 600 MPa Microfluidizer Homogenization pretreatment Pressure: 50 MPa Number of cycles: 1-2 Channel size: µm
20 Thermal treatment Microfluidizer High Hydrostatic Pressure Microstructure 80 C required to gelatinise all starch 60 C enough for 12% concentration or lower Majority of starch gelatinised with one cycle 600 MPa required to gelatinise all starch Phase separation Sedimentation for 60 & 80 C treatment More stable in comparison to other method of treatment Quick sedimentation Particle size Increased with higher temperature Reduced 2 Cycle gave smaller diameter Increased with higher pressure, bigger particles compared to thermal treatment Solubility Increased at 60 C Increased by homogeniser Increased at 300 MPa Decreased at 600 MPa Hydrophobicity Highest increase at 80 C, 60 C at 8.5% protein concentration Increased by homogeniser but reduced by microfluidizer Highest increase at 600 MPa Viscosity Increased with higher temperature Reduced by homogeniser increased by microfluidizer Increased with higher pressure 20
21 Conclusions Concentration of oat beta-glucan in a dry fractionation process produces also a stream rich in oat protein. The oat proteins obtained from this process preserved in their native state in both OPC and OPI. Oat proteins have several challenges, related to their limited solubility and technofunctionality. The techno-functional challenges can be overcome by modifications at different structural level depending on the different applications. The colloidal or dispersion stability and foaming properties of OPI suspensions can be improved by either by TG treatment or steric stabilization by using pectins. For less pure system such as OPC, which contains starch as the other major component can be utilized in food applications where the gelatinization of starch can be exploited for structure formation or stabilization.
22 THANK YOU! Join us in leading R&D&I #vttpeople Nesli.Sozer@vtt.fi
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