The Experts below are selected from a list of 318 Experts worldwide ranked by ideXlab platform
Lingyun Chen - One of the best experts on this subject based on the ideXlab platform.
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Oat Protein-shellac nanoparticles as a delivery vehicle for resveratrol to improve bioavailability in vitro and in vivo.
Nanomedicine (London England), 2019Co-Authors: Chen Yang, Yi Xiang Wang, Yike Xie, Guangyu Liu, Lingyun ChenAbstract:Aim: Oat Protein-shellac nanoparticles (NPs) were developed as a delivery system for resveratrol to improve bioavailability. Materials & methods: The NPs were prepared from w/w emulsion followed by cold-gelation. In vitro release and cell uptake mechanism of NPs were estimated by HPLC and confocal laser scanning microscopy. In vivo bioavailability and hepatoprotective activity of encapsulated resveratrol were studied using rat models. Results & conclusion: NPs (90-300 nm) protected resveratrol in gastric fluid, while allowing controlled release into small intestine in vitro. The optimized NPs showed improvement in resveratrol cell uptake and transport when compared with free resveratrol. NP-100S increased resveratrol bioavailability up to 72.4%, and the absorbed resveratrol effectively prevented CCl4-induced hepatotoxicity by attenuating oxidative stress.
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Oat Protein-shellac beads: Superior protection and delivery carriers for sensitive bioactive compounds
Food Hydrocolloids, 2018Co-Authors: Chen Yang, Yi Xiang Wang, Larry D. Unsworth, Le Luo Guan, Lingyun ChenAbstract:Abstract The purpose of this work was to better understand the interactions between Oat Protein (OPI) and shellac to form Oat Protein-shellac based gels at near neutral pH as carrier to protect and deliver sensitive bioactive compounds. There were moderate interactions between OPI and shellac with a binding constant (Ka) of 2.088 × 103 M−1 via hydrophobic interactions and hydrogen bonding as revealed by Isothermal Titration Calorimeter (ITC) and Fourier Transform Infrared Spectroscopy (FTIR). Such interactions allowed the formation of a gel-like mixture with good compatibility that only one endothermic peak and Tg value for OPI-shellac mixture as demonstrated by differential scanning calorimetry (DSC) analysis. Novel core (OPI)-shell (OPI-shellac mixture) beads were then developed by a cold-gelation method at near neural pH and ambient temperature. The optimized samples possessed a homogeneous, smooth and integrated shell structure. This structure could effectively restrict the swelling of the shell and prevent premature diffusion of the contained riboflavin. Also, this structure could efficiently protect the survival of L. acidophilus as 85.5% and the activity of amylase as 80.0% in the harsh environment of simulated gastric fluids after 1 h. When transferred to a simulated intestinal tract, riboflavin and L. acidophilus were sustainably released. Since the beads are easily prepared using a simple extrusion method at near neutral pH and ambient temperature, they are excellent candidates for natural delivery systems for sensitive bioactive compounds in the food and biomedical industries.
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Fabrication, characterization and controlled release properties of Oat Protein gels with percolating structure induced by cold gelation
Food Hydrocolloids, 2017Co-Authors: Chen Yang, Yi Xiang Wang, Lingyun ChenAbstract:Cold-set Oat Protein isolate (OPI) gels possessing a percolating network structure were successfully prepared using a glucono-δ-lactone (GDL) induced acidification method. The polymer-like percolating structures were established by active OPI monomers as small building block units through abundant cross-linking points. By increasing the GDL concentration, more intra-floc linkages and greater particle volume fractions were created at the supramolecular level, resulting in a dense rough gel wall with superior mechanical properties. In particular, at a 10% GDL content the gel was generated at the OPI isoelectric point (IEP). This OPI gel had a compact network structure with small pores and a thick wall, with an excellent water holding capacity (90%) and comparable mechanical strength (30 kPa) to egg white gel (22–32 kPa). Also, the cold-set OPI gels could resist acidic juice and pepsin digestion, which protected both α-amylase enzyme activity and the viability of probiotics in harsh gastric conditions. The in vitro release experiment demonstrated that OPI gels had the capacity to prevent the premature release of bioactive compounds in simulated gastric fluids, and yet still allowed their gradual release in a simulated intestinal environment where they normally would be absorbed. A convenient and non-toxic method to prepare OPI gels with superior performance has been described. These gels have the potential to act as delivery vehicles for sensitive compounds in food and non-food applications.
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improved thermal gelation of Oat Protein with the formation of controlled phase separated networks using dextrin and carrageenan polysaccharides
Food Research International, 2016Co-Authors: Talina Vanessa Nieto Nieto, Yi Xiang Wang, L. Ozimek, Lingyun ChenAbstract:Abstract The thermal gelation of Oat Protein (OP) was investigated in the presence of polysaccharides at different pHs. The compressive stress dramatically increased in these phase-separated Protein–polysaccharides gels due to an apparent increase in Protein concentration. The polysaccharide structure significantly affected the degree of phase-separation and gel mechanical properties. The observed two-fold increase in gel compressive stress can be attributed to strong repulsive forces caused by carrageenan molecules. These resulted in a greater degree of phase-separation with the formation of carrageenan rich domains embedded in the Protein phase, and a highly ordered Protein network, stabilized by hydrogen and hydrophobic interactions. In the case of OP-dextrin gels, the rate of phase separation was slower than the rate of Protein aggregation, thus the dextrin particles were uniformly distributed within the Protein network. This research contributes to the basic understanding required for designing textures for novel plant-based Protein products.
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Inulin at low concentrations significantly improves the gelling properties of Oat Protein - A molecular mechanism study
Food Hydrocolloids, 2015Co-Authors: Talina Vanessa Nieto-nieto, Yi Xiang Wang, L. Ozimek, Lingyun ChenAbstract:The effect of inulin addition at low concentrations (0.1-0.5%) on the thermal gelation of Oat Protein gels was investigated using textural profile analysis, rheological measurements and microstructure observation through scanning electron microscopy (SEM) and confocal laser scanning microscopy (CLSM). Results indicate that Oat Protein hexamers were dissociated with heat into monomers, which then became the reactive units involved in the development of a unique percolating network. The major forces responsible for the establishment of the structure were disulphide bonds, as well as hydrogen bonds and hydrophobic forces. A small amount of inulin can greatly increase the compressive stress of the gels prepared at pH 7 from 13.93 to 22.98kPa. This is related to the phase separation phenomena produced during heating, which increased the apparent Protein concentration. Moreover, inulin formed nanoparticles in the void spaces of the Protein network performing a filling effect and creating junction zones. Localized interactions such as hydrogen and hydrophobic bonds were possible between Protein and inulin at the borders of junction zones. This research has provided a new approach to make strong Oat Protein gels at neutral pH. Future applications may promote the utilization of Oat Protein as a plant derived gelling ingredient in a wide range of food applications.
Jiajia Rao - One of the best experts on this subject based on the ideXlab platform.
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structure and functionality of Oat Protein extracted by choline chloride dihydric alcohol deep eutectic solvent and its water binary mixtures
Food Hydrocolloids, 2021Co-Authors: Jianxiong Yue, Zhenbao Zhu, Yang Lan, Bingcan Chen, Jiajia RaoAbstract:Abstract This research reports an eco-friendly Oat Protein extraction method using choline chloride (ChCl)–butanediol deep eutectic solvents (DESs) and DES/water binary mixtures. Eighteen formulas consisting of ChCl with butanediol isomer (1,2-butanediol, 1,4-butanediol, or 2, 3-butanediol) in the absence or presence of water at different molar ratio were examined for the synthesis of DESs and binary mixtures. We found that 6 formulae can be fabricated at a ChCl–butanediol molar ratio of 1:3 independent of water presence, and that they had better Oat extraction performance with 90 min extraction at 80 °C. Under the optimal conditions, we further assessed the impact of butanediol isomers and water addition on the structure characteristics and functionalities of extracted Oat Protein. The results suggested that Oat Protein extracted by ChCl−1,4-butanediol/water binary mixture had highest Protein content, solubility, foaming capacity and stability. Our pilot findings provide crucial support to our hypothesis that the isomer of hydrogen bond donor is critically involved in the properties of Oat Protein the DES and the binary mixtures extracted, which pave the way for the future application of DES in Protein extraction.
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Structure and functionality of Oat Protein extracted by choline chloride‒dihydric alcohol deep eutectic solvent and its water binary mixtures
Food Hydrocolloids, 1Co-Authors: Jianxiong Yue, Zhenbao Zhu, Yang Lan, Bingcan Chen, Jiajia RaoAbstract:Abstract This research reports an eco-friendly Oat Protein extraction method using choline chloride (ChCl)–butanediol deep eutectic solvents (DESs) and DES/water binary mixtures. Eighteen formulas consisting of ChCl with butanediol isomer (1,2-butanediol, 1,4-butanediol, or 2, 3-butanediol) in the absence or presence of water at different molar ratio were examined for the synthesis of DESs and binary mixtures. We found that 6 formulae can be fabricated at a ChCl–butanediol molar ratio of 1:3 independent of water presence, and that they had better Oat extraction performance with 90 min extraction at 80 °C. Under the optimal conditions, we further assessed the impact of butanediol isomers and water addition on the structure characteristics and functionalities of extracted Oat Protein. The results suggested that Oat Protein extracted by ChCl−1,4-butanediol/water binary mixture had highest Protein content, solubility, foaming capacity and stability. Our pilot findings provide crucial support to our hypothesis that the isomer of hydrogen bond donor is critically involved in the properties of Oat Protein the DES and the binary mixtures extracted, which pave the way for the future application of DES in Protein extraction.
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Impact of defatting treatment and Oat varieties on structural, functional properties, and aromatic profile of Oat Protein
Food Hydrocolloids, 1Co-Authors: Jianxiong Yue, Zhenbao Zhu, Bingcan Chen, Jae-bom Ohm, Jiajia RaoAbstract:Abstract In this study, two naked (ND04034 and Paul) and two hulled (Beach and CDC Minstrel) Oat varieties were selected to determine the impact of varieties and flour defatting treatment on extraction performance, structural and functional properties, and aromatic profiles of the extracted Oat Proteins. The results showed that Oat Protein extracted from defatted flour (DF) had a higher Oat Protein content (>86.93%) but a lower extraction yield and recovery yield compared to that from non-defatted flour (NDF) of same variety. Amino acid (AA) analysis indicated that the relative percent of individual AA showed a great similarity among the samples, while Oat Protein from hulled Oat varieties had higher essential AA. SDS-PAGE results suggested the higher proportion of 7S globulins in Oat Proteins from DF. Both circular dichroism and FT-IR confirmed β-sheet, α-helix and β-turn were the main secondary structures in Oat Proteins. Differential scanning calorimetry (DSC) results showed that Oat Proteins from DF had better thermal stability. Scanning electron microscopy (SEM) observed the big flaky plate like structures in Oat Proteins from DF which may account for the improved solubility. Moreover, Oat Proteins from DF exhibited better functionalities, including solubility, foaming capacity and emulsifying properties. Principal component analysis (PCA) and hierarchical cluster analysis (HCA) classified Oat Proteins into 3 groups/clusters on account of aromatic components. Venn diagram allowed us to differentiate Oat Proteins from different varieties via the aroma makers identified. The findings endow a great potential of preparing Oat Proteins with superior functionality and aromatic profiles for food applications.
Jianxiong Yue - One of the best experts on this subject based on the ideXlab platform.
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structure and functionality of Oat Protein extracted by choline chloride dihydric alcohol deep eutectic solvent and its water binary mixtures
Food Hydrocolloids, 2021Co-Authors: Jianxiong Yue, Zhenbao Zhu, Yang Lan, Bingcan Chen, Jiajia RaoAbstract:Abstract This research reports an eco-friendly Oat Protein extraction method using choline chloride (ChCl)–butanediol deep eutectic solvents (DESs) and DES/water binary mixtures. Eighteen formulas consisting of ChCl with butanediol isomer (1,2-butanediol, 1,4-butanediol, or 2, 3-butanediol) in the absence or presence of water at different molar ratio were examined for the synthesis of DESs and binary mixtures. We found that 6 formulae can be fabricated at a ChCl–butanediol molar ratio of 1:3 independent of water presence, and that they had better Oat extraction performance with 90 min extraction at 80 °C. Under the optimal conditions, we further assessed the impact of butanediol isomers and water addition on the structure characteristics and functionalities of extracted Oat Protein. The results suggested that Oat Protein extracted by ChCl−1,4-butanediol/water binary mixture had highest Protein content, solubility, foaming capacity and stability. Our pilot findings provide crucial support to our hypothesis that the isomer of hydrogen bond donor is critically involved in the properties of Oat Protein the DES and the binary mixtures extracted, which pave the way for the future application of DES in Protein extraction.
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Structure and functionality of Oat Protein extracted by choline chloride‒dihydric alcohol deep eutectic solvent and its water binary mixtures
Food Hydrocolloids, 1Co-Authors: Jianxiong Yue, Zhenbao Zhu, Yang Lan, Bingcan Chen, Jiajia RaoAbstract:Abstract This research reports an eco-friendly Oat Protein extraction method using choline chloride (ChCl)–butanediol deep eutectic solvents (DESs) and DES/water binary mixtures. Eighteen formulas consisting of ChCl with butanediol isomer (1,2-butanediol, 1,4-butanediol, or 2, 3-butanediol) in the absence or presence of water at different molar ratio were examined for the synthesis of DESs and binary mixtures. We found that 6 formulae can be fabricated at a ChCl–butanediol molar ratio of 1:3 independent of water presence, and that they had better Oat extraction performance with 90 min extraction at 80 °C. Under the optimal conditions, we further assessed the impact of butanediol isomers and water addition on the structure characteristics and functionalities of extracted Oat Protein. The results suggested that Oat Protein extracted by ChCl−1,4-butanediol/water binary mixture had highest Protein content, solubility, foaming capacity and stability. Our pilot findings provide crucial support to our hypothesis that the isomer of hydrogen bond donor is critically involved in the properties of Oat Protein the DES and the binary mixtures extracted, which pave the way for the future application of DES in Protein extraction.
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Impact of defatting treatment and Oat varieties on structural, functional properties, and aromatic profile of Oat Protein
Food Hydrocolloids, 1Co-Authors: Jianxiong Yue, Zhenbao Zhu, Bingcan Chen, Jae-bom Ohm, Jiajia RaoAbstract:Abstract In this study, two naked (ND04034 and Paul) and two hulled (Beach and CDC Minstrel) Oat varieties were selected to determine the impact of varieties and flour defatting treatment on extraction performance, structural and functional properties, and aromatic profiles of the extracted Oat Proteins. The results showed that Oat Protein extracted from defatted flour (DF) had a higher Oat Protein content (>86.93%) but a lower extraction yield and recovery yield compared to that from non-defatted flour (NDF) of same variety. Amino acid (AA) analysis indicated that the relative percent of individual AA showed a great similarity among the samples, while Oat Protein from hulled Oat varieties had higher essential AA. SDS-PAGE results suggested the higher proportion of 7S globulins in Oat Proteins from DF. Both circular dichroism and FT-IR confirmed β-sheet, α-helix and β-turn were the main secondary structures in Oat Proteins. Differential scanning calorimetry (DSC) results showed that Oat Proteins from DF had better thermal stability. Scanning electron microscopy (SEM) observed the big flaky plate like structures in Oat Proteins from DF which may account for the improved solubility. Moreover, Oat Proteins from DF exhibited better functionalities, including solubility, foaming capacity and emulsifying properties. Principal component analysis (PCA) and hierarchical cluster analysis (HCA) classified Oat Proteins into 3 groups/clusters on account of aromatic components. Venn diagram allowed us to differentiate Oat Proteins from different varieties via the aroma makers identified. The findings endow a great potential of preparing Oat Proteins with superior functionality and aromatic profiles for food applications.
Yi Xiang Wang - One of the best experts on this subject based on the ideXlab platform.
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Oat Protein-shellac nanoparticles as a delivery vehicle for resveratrol to improve bioavailability in vitro and in vivo.
Nanomedicine (London England), 2019Co-Authors: Chen Yang, Yi Xiang Wang, Yike Xie, Guangyu Liu, Lingyun ChenAbstract:Aim: Oat Protein-shellac nanoparticles (NPs) were developed as a delivery system for resveratrol to improve bioavailability. Materials & methods: The NPs were prepared from w/w emulsion followed by cold-gelation. In vitro release and cell uptake mechanism of NPs were estimated by HPLC and confocal laser scanning microscopy. In vivo bioavailability and hepatoprotective activity of encapsulated resveratrol were studied using rat models. Results & conclusion: NPs (90-300 nm) protected resveratrol in gastric fluid, while allowing controlled release into small intestine in vitro. The optimized NPs showed improvement in resveratrol cell uptake and transport when compared with free resveratrol. NP-100S increased resveratrol bioavailability up to 72.4%, and the absorbed resveratrol effectively prevented CCl4-induced hepatotoxicity by attenuating oxidative stress.
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Oat Protein-shellac beads: Superior protection and delivery carriers for sensitive bioactive compounds
Food Hydrocolloids, 2018Co-Authors: Chen Yang, Yi Xiang Wang, Larry D. Unsworth, Le Luo Guan, Lingyun ChenAbstract:Abstract The purpose of this work was to better understand the interactions between Oat Protein (OPI) and shellac to form Oat Protein-shellac based gels at near neutral pH as carrier to protect and deliver sensitive bioactive compounds. There were moderate interactions between OPI and shellac with a binding constant (Ka) of 2.088 × 103 M−1 via hydrophobic interactions and hydrogen bonding as revealed by Isothermal Titration Calorimeter (ITC) and Fourier Transform Infrared Spectroscopy (FTIR). Such interactions allowed the formation of a gel-like mixture with good compatibility that only one endothermic peak and Tg value for OPI-shellac mixture as demonstrated by differential scanning calorimetry (DSC) analysis. Novel core (OPI)-shell (OPI-shellac mixture) beads were then developed by a cold-gelation method at near neural pH and ambient temperature. The optimized samples possessed a homogeneous, smooth and integrated shell structure. This structure could effectively restrict the swelling of the shell and prevent premature diffusion of the contained riboflavin. Also, this structure could efficiently protect the survival of L. acidophilus as 85.5% and the activity of amylase as 80.0% in the harsh environment of simulated gastric fluids after 1 h. When transferred to a simulated intestinal tract, riboflavin and L. acidophilus were sustainably released. Since the beads are easily prepared using a simple extrusion method at near neutral pH and ambient temperature, they are excellent candidates for natural delivery systems for sensitive bioactive compounds in the food and biomedical industries.
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Fabrication, characterization and controlled release properties of Oat Protein gels with percolating structure induced by cold gelation
Food Hydrocolloids, 2017Co-Authors: Chen Yang, Yi Xiang Wang, Lingyun ChenAbstract:Cold-set Oat Protein isolate (OPI) gels possessing a percolating network structure were successfully prepared using a glucono-δ-lactone (GDL) induced acidification method. The polymer-like percolating structures were established by active OPI monomers as small building block units through abundant cross-linking points. By increasing the GDL concentration, more intra-floc linkages and greater particle volume fractions were created at the supramolecular level, resulting in a dense rough gel wall with superior mechanical properties. In particular, at a 10% GDL content the gel was generated at the OPI isoelectric point (IEP). This OPI gel had a compact network structure with small pores and a thick wall, with an excellent water holding capacity (90%) and comparable mechanical strength (30 kPa) to egg white gel (22–32 kPa). Also, the cold-set OPI gels could resist acidic juice and pepsin digestion, which protected both α-amylase enzyme activity and the viability of probiotics in harsh gastric conditions. The in vitro release experiment demonstrated that OPI gels had the capacity to prevent the premature release of bioactive compounds in simulated gastric fluids, and yet still allowed their gradual release in a simulated intestinal environment where they normally would be absorbed. A convenient and non-toxic method to prepare OPI gels with superior performance has been described. These gels have the potential to act as delivery vehicles for sensitive compounds in food and non-food applications.
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improved thermal gelation of Oat Protein with the formation of controlled phase separated networks using dextrin and carrageenan polysaccharides
Food Research International, 2016Co-Authors: Talina Vanessa Nieto Nieto, Yi Xiang Wang, L. Ozimek, Lingyun ChenAbstract:Abstract The thermal gelation of Oat Protein (OP) was investigated in the presence of polysaccharides at different pHs. The compressive stress dramatically increased in these phase-separated Protein–polysaccharides gels due to an apparent increase in Protein concentration. The polysaccharide structure significantly affected the degree of phase-separation and gel mechanical properties. The observed two-fold increase in gel compressive stress can be attributed to strong repulsive forces caused by carrageenan molecules. These resulted in a greater degree of phase-separation with the formation of carrageenan rich domains embedded in the Protein phase, and a highly ordered Protein network, stabilized by hydrogen and hydrophobic interactions. In the case of OP-dextrin gels, the rate of phase separation was slower than the rate of Protein aggregation, thus the dextrin particles were uniformly distributed within the Protein network. This research contributes to the basic understanding required for designing textures for novel plant-based Protein products.
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Inulin at low concentrations significantly improves the gelling properties of Oat Protein - A molecular mechanism study
Food Hydrocolloids, 2015Co-Authors: Talina Vanessa Nieto-nieto, Yi Xiang Wang, L. Ozimek, Lingyun ChenAbstract:The effect of inulin addition at low concentrations (0.1-0.5%) on the thermal gelation of Oat Protein gels was investigated using textural profile analysis, rheological measurements and microstructure observation through scanning electron microscopy (SEM) and confocal laser scanning microscopy (CLSM). Results indicate that Oat Protein hexamers were dissociated with heat into monomers, which then became the reactive units involved in the development of a unique percolating network. The major forces responsible for the establishment of the structure were disulphide bonds, as well as hydrogen bonds and hydrophobic forces. A small amount of inulin can greatly increase the compressive stress of the gels prepared at pH 7 from 13.93 to 22.98kPa. This is related to the phase separation phenomena produced during heating, which increased the apparent Protein concentration. Moreover, inulin formed nanoparticles in the void spaces of the Protein network performing a filling effect and creating junction zones. Localized interactions such as hydrogen and hydrophobic bonds were possible between Protein and inulin at the borders of junction zones. This research has provided a new approach to make strong Oat Protein gels at neutral pH. Future applications may promote the utilization of Oat Protein as a plant derived gelling ingredient in a wide range of food applications.
Nesli Sozer - One of the best experts on this subject based on the ideXlab platform.
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Potential to reduce GHG emissions and land use by substituting animal-based Proteins by foods containing Oat Protein concentrate
Journal of Cleaner Production, 2020Co-Authors: Lisbeth Mogensen, Nesli Sozer, H. Heusale, Taija Sinkko, K. Poutanen, John E. Hermansen, Marie Trydeman KnudsenAbstract:Abstract The potential to reduce GHG emissions and land use of the diet by replacing animal-based Protein sources with foods containing Oat Protein concentrate (OPC) was analysed by life cycle assessment (LCA) of six different scenarios of daily food intake of one adult. The OPC was used in the preparation of bread and pasta and as a substitute for milk in yoghurt resulting in a higher Protein content of these foods. The present study showed, that dietary-related GHG emissions and land use can be reduced by substituting animal-based Proteins by foods containing Oat Protein. If the Oat Protein (OPC) enriched food items substitute animal based Protein sources in the diet proportionally, GHG emission from the diet could be reduced by 8% and land use by 14%. However, if the OPC enriched food items are used specifically to replace intake of all beef and some pork, GHG emissions from the diet could be reduced by 13% and land use by 26%. Thereby, use of new plant-based Protein ingredients in diets has a considerable potential to mitigate climate change and reduce land use. Even though the presented scenarios are extreme, they clearly demonstrate the potential that OPC food products made it possible to replace some of the animal-based Protein with this plant-based Protein source.
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Carbon footprint and land use of Oat and faba bean Protein concentrates using a life cycle assessment approach
Journal of Cleaner Production, 2020Co-Authors: Hannele Heusala, Nesli Sozer, Lisbeth Mogensen, Taija Sinkko, Eemeli Hytönen, Marie Trydeman KnudsenAbstract:Abstract There is a need to find sustainable alternative Protein sources in order to meet the increasing Protein demand of the growing population. Legumes such as faba beans are underutilized Protein rich sources and can be valorized as hybrid Protein ingredient through dry fractionation technologies. Also, cereal side streams can be interesting sources towards multifunctional Protein ingredients. The aim of this study was to assess the environmental impacts of the production of Oat Protein concentrate (OPC) and faba bean Protein concentrate (FBC) using life cycle assessment (LCA) methodology and to compare the impact per kg Protein to other relevant Proteins. The OPC is obtained as a side stream of the beta glucan extraction process, which also produces valuable Oat oil, while FBC is the only main product obtained from dehulled faba beans. Average European Oat cultivation and faba bean cultivation with low and high yield were modelled. Data for Protein concentrates production was from real factories who have suitable facilities, but are not currently producing concentrates commercially. The major hotspot in the carbon footprint of Oat Protein concentrate comes from energy consumption in processing. For faba bean Protein concentrate, energy consumption in processing is lower and cultivation of faba bean is the main hotspot. The carbon footprint of Oat Protein concentrate is more than 50 percent lower, compared to dairy Proteins per kg Protein, while the carbon footprint of faba bean concentrate Protein is 80–90 percent lower. Compared to legume Protein sources, OPC has four times higher impacts. This is mainly due to the lower amount of processing steps needed to reach high Protein content concentrates from faba beans resulting mainly from relatively lower level of lipids, which enables more energy-efficient dry separation, and high initial Protein content of legumes compared to cereals. Moreover, legume cultivation requires very little nitrogen fertilizers due to symbiotic N2 fixation. This study shows that OPC and FBC have lower carbon footprints than animal Protein sources. However, it should be remembered, that the environmental impacts of OPC are very sensitive to the allocation method and allocation basis. In this study economic allocation was used and prices of the different products (OPC, Oat oil and beta glucan) play a key role in defining the climate impacts of OPC.
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Effect of dry fractionated hybrid Protein ingredients on the structural, textural, thermal and sensory properties of gluten‐free Oat and faba pasta
International Journal of Food Science and Technology, 2019Co-Authors: Denisa Eglantina Duta, Alina Culetu, Nesli SozerAbstract:Protein‐enriched gluten‐free pasta was prepared from Oat starch‐rich endosperm (SRE), which was substituted with different proportions of Oat Protein concentrate (OPC) and/or faba Protein concentrate (FPC) fractions in order to obtain a similar Protein content (18% and 35%). Accordingly, the health claims ‘source of Protein’ and ‘high Protein’ were achieved. Pasta with OPC and FPC had lower optimal cooking time (8 and 6.3 min), cooking loss (6% and 10.2% dm) and water absorption (152% and 147%) than control SRE pasta (9.3 min; 12.3% dm and 185%). Addition of Protein concentrates produced an increase in hardness and chewiness of spaghetti. The glycaemic index of pasta was lowered by the addition of Protein ingredients, the lowest value being achieved with FPC. In vitro Protein digestibility of pasta increased up to 3.5% for OPC and up to 7.1% in case of FPC addition. The most Protein‐digestible pasta was that with FPC addition to reach 35% Protein content.
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Oat Protein concentrate as alternative ingredient for non-dairy yoghurt-type product.
Journal of the science of food and agriculture, 2019Co-Authors: Monika Brückner-gühmann, Alina Culetu, Denisa Eglantina Duta, Nesli Sozer, Elena Vasil’eva, Stephan DruschAbstract:BACKGROUND During the industrial production of β-glucan, a Protein-rich fraction remains as a by-product. Recovery of this Protein as Oat Protein concentrate (OPC) results in a source of cereal Protein for food and improves the overall economy of the process. In this study, a yoghurt-type product is developed by lactic acid fermentation of an OPC suspension after subjection to heat treatment to assure starch gelatinization. RESULTS In detail, the process of yoghurt production involved an initial heating step to 90 °C, followed by 24 h fermentation with a starter culture consisting of Lactobacillus delbrueckii subsp. bulgaricus und Streptococcus thermophilus. The resulting yoghurt-type product was mildly sour (pH 4.2) with a certain amount of lactic acid (3.3 ± 0.2 g kg-1 ) and contained 4.9 × 106 cfu g-1 lactobacillus after 24 h fermentation. Scanning electron microscopy revealed a porous network presumably built up from the gelatinized starch fraction containing aggregated structures, between which were assumed to be aggregated Oat Proteins. Moreover, to a limited extent, proteolysis occurred during fermentation. Thus some of the proteolytic enzymes present in the yoghurt culture cleaved Oat Protein and released peptides. However, the effect on essential amino acids was small. CONCLUSION The results of this study provide a deeper knowledge into the role of starch and Protein in fermented OPC yoghurts. The structure of fermented OPC verifies the applicability of Oat Protein as an alternative source for yoghurt-type products. © 2019 Society of Chemical Industry.
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effect of dry fractionated hybrid Protein ingredients on the structural textural thermal and sensory properties of gluten free Oat and faba pasta
International Journal of Food Science and Technology, 2019Co-Authors: Denisa Eglantina Duta, Alina Culetu, Nesli SozerAbstract:Protein‐enriched gluten‐free pasta was prepared from Oat starch‐rich endosperm (SRE), which was substituted with different proportions of Oat Protein concentrate (OPC) and/or faba Protein concentrate (FPC) fractions in order to obtain a similar Protein content (18% and 35%). Accordingly, the health claims ‘source of Protein’ and ‘high Protein’ were achieved. Pasta with OPC and FPC had lower optimal cooking time (8 and 6.3 min), cooking loss (6% and 10.2% dm) and water absorption (152% and 147%) than control SRE pasta (9.3 min; 12.3% dm and 185%). Addition of Protein concentrates produced an increase in hardness and chewiness of spaghetti. The glycaemic index of pasta was lowered by the addition of Protein ingredients, the lowest value being achieved with FPC. In vitro Protein digestibility of pasta increased up to 3.5% for OPC and up to 7.1% in case of FPC addition. The most Protein‐digestible pasta was that with FPC addition to reach 35% Protein content.
