Browsing by Subject "SOY PROTEIN"

Sort by: Order: Results:

Now showing items 1-6 of 6
  • Marzbani, Pouya; Azadfallah, Mohammad; Yousefzadeh, Maryam; Najafi, Farhood; Pourbabaee, Ahmad Ali; Koivula, Hanna; Ritala, Mikko (2021)
    Application of barrier dispersion coatings on paperboards, which must have proper moisture and grease resistance for food applications, has always been an interesting subject for the packaging industry. In this study, paperboards were coated with a novel dispersion barrier coating prepared through mixing soy protein isolate (SPI) and polyethylene wax (PE-wax). Different characterization methods were used to study the effects of coating and its composition on the physical, mechanical, and barrier characteristics of paperboards. The results indicated that the incorporation of PE-wax into the coating formulation caused significant reduction of the viscosity of coating slurries. It had no effect on the coating weight of the samples but increased the thickness of the coated paperboards as compared with those coated with SPI only. The increase of the wax content led to a reduction of 5-16% in the tensile strength values in comparison with the uncoated paperboards. Barrier characteristics, i.e., water vapor permeability (WVP), surface wettability, and water resistance, improved by adding PE-wax. In addition, it was found that there was a critical level for the addition of PE-wax, 50% of SPI, as no oil migration was detected when the paperboards coated with SPI coatings contained less than 50% PE-wax.
  • Liu, Chang; Damodaran, Srinivasan; Heinonen, Irma Marina (2019)
    The potential use of microbial transglutaminase (MTG)-treated faba bean protein isolate (FBPI) as emulsifiers to maintain physical and oxidative stability of oil-in-water (O/W) emulsion was investigated. MTG-treated FBPIs (MTG-FBPIs) were prepared by incubating with MTG for 60, 120 or 240 min. O/W emulsions were stabilized by 3% (w/v) of MTG-FBPIs or control-FBPI (treated with inactive MTG) and stored at 37 degrees C for 7 days. MTG treatments induced cross-linking in FBPI, raised the protein net surface charges by 5%-8%, and increased the emulsion particle size by 19%-135%. MTG treatment for 120 and 240 min but not 60 min induced excessive surface hydrophobicity, resulting in decreased emulsifying activity and physical stability of emulsion. By day 7, all MTG-treated FBPIs showed similar inhibiting effects against lipid oxidation in emulsion, indicated by less conjugated dienes and hexanal production. MTG-FBPIs moderately promoted protein oxidation (120 min > 240 min approximate to 60 min). Thus, prolonged MTG treatment should be avoided to prevent accelerated protein oxidation and droplets coalescence. MTG treatment for 60 min makes FBPI a potential emulsifier to maintain physical stability while improving lipid oxidative stability in emulsion, potentially attributed to thicker interfacial layer, larger droplet size, and protective effect of protein.
  • Ramos-Diaz, Jose Martin; Kantanen, Katja Annika; Edelmann, Minnamari; Suhonen, Heikki; Sontag-Strohm, Tuula; Jouppila, Kirsi; Piironen, Vieno (2022)
    A new generation of plant-based texturized meat analogues attempts to boost the consumption of dietary fiber. In the present study, oat fiber concentrate (OFC) and pea protein isolate (PPI) were combined (30:70; 50:50; 70:30) and processed with high-moisture extrusion (long cooling die temperature [LCDT]: 40, 60 and 80 °C; screw speed [SS]: 300, 400 and 500 rpm) to obtain meat-mimicking fibrous meat analogues (FMAs). The results showed that OFC reduced the structural strength (e.g., hardness, chewiness) of the FMAs, whereas LCDT strengthened the structure. Microtomography imaging revealed that FMAs containing more OFC presented smaller void thickness, thus reducing the FMAs' water holding capacity. An in-vitro gastrointestinal model showed that the extractability and viscosity of β-glucan were well preserved, particularly at low LCDT. Overall, it was possible to add substantial amounts of OFC (30–50%) to FMAs while maintaining fibrous meat-mimicking structures and retaining the oat fiber's viscous properties.
  • Ma, Kai Kai; Greis, Maija; Lu, Jiakai; Nolden, Alissa A.; McClements, David Julian; Kinchla, Amanda J. (2022)
    Increasingly, consumers are moving towards a more plant-based diet. However, some consumers are avoiding common plant proteins such as soy and gluten due to their potential allergenicity. Therefore, alternative protein sources are being explored as functional ingredients in foods, including pea, chickpea, and other legume proteins. The factors affecting the functional performance of plant proteins are outlined, including cultivars, genotypes, extraction and drying methods, protein level, and preparation methods (commercial versus laboratory). Current methods to characterize protein functionality are highlighted, including water and oil holding capacity, protein solubility, emulsifying, foaming, and gelling properties. We propose a series of analytical tests to better predict plant protein performance in foods. Representative applications are discussed to demonstrate how the functional attributes of plant proteins affect the physicochemical properties of plant-based foods. Increasing the protein content of plant protein ingredients enhances their water and oil holding capacity and foaming stability. Industrially produced plant proteins often have lower solubility and worse functionality than laboratory-produced ones due to protein denaturation and aggregation during commercial isolation processes. To better predict the functional performance of plant proteins, it would be useful to use computer modeling approaches, such as quantitative structural activity relationships (QSAR).
  • Kantanen, Katja Annika; Oksanen, Anni; Edelmann, Minnamari; Suhonen, Heikki; Sontag-Strohm, Tuula; Piironen, Vieno; Ramos-Diaz, Jose Martin; Jouppila, Kirsi (2022)
    Faba bean is a potential ingredient due to its high protein yield and its possible cultivation in colder climate regions. In this study, meat analogues made from faba bean protein isolate (FPI) and concentrate (FPC) blends were produced using high moisture extrusion. The aim of this study was to investigate the effect of the FPI content (FPIc), feed water content (FWC), and temperature of the long cooling die (LT) during extrusion on the mechanical and physicochemical properties as well as on the structure of the meat analogues. Increased FPIc resulted in higher values in hardness, gumminess, chewiness, and cutting strengths as well as in darker colour and decreased water absorption capacity. The effect of increased FWC on these properties was weaker and the opposite. Images from microtomography revealed that higher FPIc led to a less organised fibrous structure. In conclusion, fibrous structures can be achieved by utilising a mixture of faba bean protein ingredients, and a higher FPC content seemed to promote fibre formation in the meat analogue.
  • Immonen, Mika; Chandrakusuma, Angga; Sibakov, Juhani; Poikelispaa, Minna; Sontag-Strohm, Tuula (2021)
    Grain protein fractions have great potential as ingredients that contain high amounts of valuable nutritional components. The aim of this study was to study the rheological behavior of destarched oat and pea proteins and their blends in extrusion-like conditions with a closed cavity rheometer. Additionally, the possibility of producing fibrous structures with high-moisture extrusion from a blend of destarched oat and pea protein was investigated. In the temperature sweep measurement (60-160 degrees C) of the destarched oat protein concentrate and pea protein isolate blend, three denaturation and polymerization sections were observed. In addition, polymerization as a function of time was recorded in the time sweep measurements. The melting temperature of grain proteins was an important factor when producing texturized structures with a high-moisture extrusion. The formation of fibrillar structures was investigated with high-moisture extrusion from the destarched oat and pea protein blend at temperatures ranging from 140 to 170 degrees C. The protein-protein interactions were significantly influenced in the extruded samples. This was due to a decrease in the amount of extractable protein in selective buffers. In particular, there was a decrease in non-covalent and covalent bonds due to the formation of insoluble protein complexes.