Oat milk has gained widespread consumer acceptance for its creamy texture,β-glucan content,and environmental sustainability.However,its relatively low protein content(typically 2-3 g/serving)presents a nutritional li...Oat milk has gained widespread consumer acceptance for its creamy texture,β-glucan content,and environmental sustainability.However,its relatively low protein content(typically 2-3 g/serving)presents a nutritional limitation,largely due to poor protein solubility.This study investigated how processing conditions influence protein content and functional stability in oat-based systems by applying two treatments:(1)α-amylase enzymatic hydrolysis,and(2)pH-shifting(from pH 7 to 12 and back)with mild heating(50℃for 10 or 30 min).Oat protein solutions were formulated from two sources:oat flour(OF)and oat protein isolate(OPI).Results suggests that α-amylase pretreatment effectively reduced starch-driven viscosity in OF,facilitating better sample handling and centrifugation.Following pH-shifting and heat treatment,both OF and OPI solutions showed significantly improved protein solubility,with protein content increased from 2.0 to~6.5 g/serving.These changes were accompanied by reduced precipitation,smaller particle sizes,and more negative zeta potential values,indicating enhanced colloidal stability.SDS-PAGE analysis revealed the presence of low-molecular-weight protein fractions,supporting increased solubilization.Fluorescence microscopy confirmed the formation of smaller,more uniformly dispersed particles in treated samples compared to controls.However,noticeable darkening or browning occurred under high-pH heating,indicating potential challenges in color control.The findings provide useful information for future industrial applications and product innovation in the plant-based beverage sector.展开更多
The application of potato protein(PP)in food industry has been limited due to its low water solubility,poor emulsification and stability.Herein,it was found that the pH-shifting combined with microwave heating signifi...The application of potato protein(PP)in food industry has been limited due to its low water solubility,poor emulsification and stability.Herein,it was found that the pH-shifting combined with microwave heating significantly increased the solubility of PP(from 24.0%to 89.0%)and surface hydrophobicity(from 125 to 207).The particle size of PP was significantly reduced(from 249.95±1.15 mm to 90.37±1.03 nm).SDS-PAGE analysis indicated that the microwave treatment did not disrupt the primary structure of PP.A complex formation between modified potato protein(MPP)and pectin(PC)at the optimum mass ratio of MPP to PC of 4:1 and pH 5 was characterized by fluorescence spectroscopy,fourier transform infrared spectroscopy,scanning electron microscopy and transmission electron microscopy,which showed that MPP and PC had electrostatic interaction.Moreover,the effect of mass ratios of MPP to PC from 5:1 to 1:2 on the phase behavior of MPP-PC soluble complexes was evaluated by the phase diagram andζ-potential measurement.These results showed that the dispersibility,emulsification and thermal stability of the protein were improved by forming MPP-PC complexes.This study provides a valuable reference for the improvement of physicochemical and functional properties of PP which is conducive to broaden the application of the protein in food industry.展开更多
Emulsion gel is widely used in the delivery of functional components because of its network structure and mechanical properties.In this study,to improve the structural and functional properties of emulsion gels and ac...Emulsion gel is widely used in the delivery of functional components because of its network structure and mechanical properties.In this study,to improve the structural and functional properties of emulsion gels and achieve efficient encapsulation and release of functional components,transglutaminase(TGase)and genipin were employed to crosslink pH-shifting/ultrasonication-modified soybean lipophilic protein(SLP),enabling the simultaneous encapsulation of vitamin E(VE,oil phase)and quercetin(QU,aqueous phase),thereby developing a co-encapsulated emulsion gel system.The impacts of combined modification(pH-ultrasonication)and enzymatic/chemical crosslinking on gel properties were systematically investigated through gel strength analysis,rheological characterization,intermolecular interaction profiling,microstructural observation,and in vitro digestion evaluation.Results demonstrated that pH-shifting combined with ultrasonication exposed more hydrophobic groups in SLP,thereby enhancing intermolecular hydrophobic interactions.Microstructural analysis revealed that TGase and genipin synergistically strengthened network crosslinking density,forming a more compact gel network structure under modified conditions.Furthermore,TGase/genipin crosslinking significantly improved structural characteristics and rheological performance(e.g.,water-holding capacity increased by 14.97%,hardness and viscosity improved),while concurrently enhancing encapsulation efficiencies of both VE and QU.In vitro digestion test confirmed that the maximum release rate reached 97.43±1.50%(VE)and 90.39±2.43%(QU)(p<0.05).These findings elucidated the potential for constructing emulsion gels via combined modification and crosslinking strategies,providing theoretical guidance for co-encapsulation systems in functional factors delivery applications.展开更多
Legume protein-based yogurts formulated without added fat or stabilizers typically exhibit poor gelation ca-pacity and are prone to phase separation.To overcome this limitation and extend the applicability of pH-shift...Legume protein-based yogurts formulated without added fat or stabilizers typically exhibit poor gelation ca-pacity and are prone to phase separation.To overcome this limitation and extend the applicability of pH-shifting in yogurt systems,a synergistic modification strategy for mung bean protein isolate(MBPI)was developed by integrating heat-alkali treatment(pH 10.5,50℃)with limited proteolysis using papain or bromelain.SDS-PAGE analysis showed that papain induced controlled hydrolysis while largely preserving the medium-molecular-weight protein fractions.Compared with native MBPI(solubility:23.7%),MBPI subjected to pH-shifting com-bined with papain treatment exhibited a pronounced increase in solubility(75.5%)and formed gels with enhanced water-holding capacity(WHC,78.6%)and improved viscoelastic properties(G′/G″).The combined treatment slightly reduced gel hardness due to particle size reduction,resulting in a finer gel structure suitable for yogurt products.LF-NMR analysis further confirmed a more restricted water distribution within the modified gels,indicating the formation of a stable and cohesive gel network.Overall,these findings demonstrate an effective approach for alleviating textural limitations in plant-based yogurts and support the development of high-quality,clean-label fermented products.展开更多
Curcumin has garnered significant attention due to its multifaceted health benefits,yet the poor physicochemical properties limit broader applications.The pH-shift method was employed to induce the formation of soy na...Curcumin has garnered significant attention due to its multifaceted health benefits,yet the poor physicochemical properties limit broader applications.The pH-shift method was employed to induce the formation of soy nanoparticles and achieve efficient encapsulation of curcumin,with a specific focus on elucidating the distinct roles of the major subunits,β-conglycinin(7 S)and glycinin(11 S).Systematic comparison revealed that the dissociation and reassembly behaviors of soy protein isolate(SPI),7 S,and 11 S were governed by their subunitspecific properties,particularly hydrophilicity/hydrophobicity,glycosylation and surface charge distribution.Specifically,the more hydrophilic glycosylated subunits of 7 S(α,α′)were able to inhibit excessive aggregation during dissociation,ultimately reassembling into more compact 7 S nanoparticles with highly charged and moderate surface hydrophobicity(30.62 nm,-32.2 mV),driven by hydrophobic interactions,electrostatic forces,and hydrogen bonding.The improved structural properties and extensive exposure of hydrophobic regions enabled a high curcumin loading capacity(~93%)and significantly enhanced thermal,digestive and storage stability.This study elucidates the application potential and molecular mechanisms of complex soy protein structures as active ingredient delivery carriers,aiming to provide new insights for designing efficient,plant-based nano-delivery systems for bio-actives.展开更多
In this study,the pH-shifting method was used for the encapsulation of microbial canthaxanthin with soy protein hydrolysates to increase its antioxidant activity.Enzymatic hydrolysis improved the functional and struct...In this study,the pH-shifting method was used for the encapsulation of microbial canthaxanthin with soy protein hydrolysates to increase its antioxidant activity.Enzymatic hydrolysis improved the functional and structural properties of soy protein hydrolysates in comparison to native ones.Reducing power and radical quenching activity of hydrolysates were raised respectively from 14.6 and 0.05 to 92.9 and 0.19 and their bioactive loading properties were significantly increased more than five times.Encapsulation parameters,structural attributes,and antioxidant activity were also studied after complexation.Fourier transform infrared spectroscopy findings indicated the formation of hydrogen bonds between canthaxanthin and hydrolysates.The crystalline nature of canthaxanthin was changed to amorphous,according to the X-ray diffraction assay.Reducing power and radical quenching activity increased(respectively 2.3-fold and 1.5-fold).The results showed the positive effects of enzymatic hydrolysis of soy protein and the pH-driven method of encapsulation on improvement in the antioxidant activity of canthaxanthin.展开更多
基金supported by the USDA National Institute of Food and Agriculture,Hatch project 7009323.
文摘Oat milk has gained widespread consumer acceptance for its creamy texture,β-glucan content,and environmental sustainability.However,its relatively low protein content(typically 2-3 g/serving)presents a nutritional limitation,largely due to poor protein solubility.This study investigated how processing conditions influence protein content and functional stability in oat-based systems by applying two treatments:(1)α-amylase enzymatic hydrolysis,and(2)pH-shifting(from pH 7 to 12 and back)with mild heating(50℃for 10 or 30 min).Oat protein solutions were formulated from two sources:oat flour(OF)and oat protein isolate(OPI).Results suggests that α-amylase pretreatment effectively reduced starch-driven viscosity in OF,facilitating better sample handling and centrifugation.Following pH-shifting and heat treatment,both OF and OPI solutions showed significantly improved protein solubility,with protein content increased from 2.0 to~6.5 g/serving.These changes were accompanied by reduced precipitation,smaller particle sizes,and more negative zeta potential values,indicating enhanced colloidal stability.SDS-PAGE analysis revealed the presence of low-molecular-weight protein fractions,supporting increased solubilization.Fluorescence microscopy confirmed the formation of smaller,more uniformly dispersed particles in treated samples compared to controls.However,noticeable darkening or browning occurred under high-pH heating,indicating potential challenges in color control.The findings provide useful information for future industrial applications and product innovation in the plant-based beverage sector.
基金the National Natural Science Foundation of China(No.22078143)Jiangxi Provincial Finance Science and Technology Special"Contract System"Demonstration Project(No.ZBG20230418035)the Research Project of State Key Laboratory of Food Science and Resources,Nanchang University(No.SKLF-ZZB-202331)for financial support.
文摘The application of potato protein(PP)in food industry has been limited due to its low water solubility,poor emulsification and stability.Herein,it was found that the pH-shifting combined with microwave heating significantly increased the solubility of PP(from 24.0%to 89.0%)and surface hydrophobicity(from 125 to 207).The particle size of PP was significantly reduced(from 249.95±1.15 mm to 90.37±1.03 nm).SDS-PAGE analysis indicated that the microwave treatment did not disrupt the primary structure of PP.A complex formation between modified potato protein(MPP)and pectin(PC)at the optimum mass ratio of MPP to PC of 4:1 and pH 5 was characterized by fluorescence spectroscopy,fourier transform infrared spectroscopy,scanning electron microscopy and transmission electron microscopy,which showed that MPP and PC had electrostatic interaction.Moreover,the effect of mass ratios of MPP to PC from 5:1 to 1:2 on the phase behavior of MPP-PC soluble complexes was evaluated by the phase diagram andζ-potential measurement.These results showed that the dispersibility,emulsification and thermal stability of the protein were improved by forming MPP-PC complexes.This study provides a valuable reference for the improvement of physicochemical and functional properties of PP which is conducive to broaden the application of the protein in food industry.
基金funding bodies of the National Keypoint Research and Invention Program of the“14th Five Year”Period(2021YFD2100302-02).
文摘Emulsion gel is widely used in the delivery of functional components because of its network structure and mechanical properties.In this study,to improve the structural and functional properties of emulsion gels and achieve efficient encapsulation and release of functional components,transglutaminase(TGase)and genipin were employed to crosslink pH-shifting/ultrasonication-modified soybean lipophilic protein(SLP),enabling the simultaneous encapsulation of vitamin E(VE,oil phase)and quercetin(QU,aqueous phase),thereby developing a co-encapsulated emulsion gel system.The impacts of combined modification(pH-ultrasonication)and enzymatic/chemical crosslinking on gel properties were systematically investigated through gel strength analysis,rheological characterization,intermolecular interaction profiling,microstructural observation,and in vitro digestion evaluation.Results demonstrated that pH-shifting combined with ultrasonication exposed more hydrophobic groups in SLP,thereby enhancing intermolecular hydrophobic interactions.Microstructural analysis revealed that TGase and genipin synergistically strengthened network crosslinking density,forming a more compact gel network structure under modified conditions.Furthermore,TGase/genipin crosslinking significantly improved structural characteristics and rheological performance(e.g.,water-holding capacity increased by 14.97%,hardness and viscosity improved),while concurrently enhancing encapsulation efficiencies of both VE and QU.In vitro digestion test confirmed that the maximum release rate reached 97.43±1.50%(VE)and 90.39±2.43%(QU)(p<0.05).These findings elucidated the potential for constructing emulsion gels via combined modification and crosslinking strategies,providing theoretical guidance for co-encapsulation systems in functional factors delivery applications.
基金supported by the National Key Research and Development Plan Project(2021YFD2100404)the China Agricul-ture Research System project(CARS-08-G19)the Major Science and Technology Projects of Xinjiang Uygur Autonomous Region(2022A02009-4).
文摘Legume protein-based yogurts formulated without added fat or stabilizers typically exhibit poor gelation ca-pacity and are prone to phase separation.To overcome this limitation and extend the applicability of pH-shifting in yogurt systems,a synergistic modification strategy for mung bean protein isolate(MBPI)was developed by integrating heat-alkali treatment(pH 10.5,50℃)with limited proteolysis using papain or bromelain.SDS-PAGE analysis showed that papain induced controlled hydrolysis while largely preserving the medium-molecular-weight protein fractions.Compared with native MBPI(solubility:23.7%),MBPI subjected to pH-shifting com-bined with papain treatment exhibited a pronounced increase in solubility(75.5%)and formed gels with enhanced water-holding capacity(WHC,78.6%)and improved viscoelastic properties(G′/G″).The combined treatment slightly reduced gel hardness due to particle size reduction,resulting in a finer gel structure suitable for yogurt products.LF-NMR analysis further confirmed a more restricted water distribution within the modified gels,indicating the formation of a stable and cohesive gel network.Overall,these findings demonstrate an effective approach for alleviating textural limitations in plant-based yogurts and support the development of high-quality,clean-label fermented products.
基金supported by the National Natural Science Foundation of China(serial numbers:3217160131).
文摘Curcumin has garnered significant attention due to its multifaceted health benefits,yet the poor physicochemical properties limit broader applications.The pH-shift method was employed to induce the formation of soy nanoparticles and achieve efficient encapsulation of curcumin,with a specific focus on elucidating the distinct roles of the major subunits,β-conglycinin(7 S)and glycinin(11 S).Systematic comparison revealed that the dissociation and reassembly behaviors of soy protein isolate(SPI),7 S,and 11 S were governed by their subunitspecific properties,particularly hydrophilicity/hydrophobicity,glycosylation and surface charge distribution.Specifically,the more hydrophilic glycosylated subunits of 7 S(α,α′)were able to inhibit excessive aggregation during dissociation,ultimately reassembling into more compact 7 S nanoparticles with highly charged and moderate surface hydrophobicity(30.62 nm,-32.2 mV),driven by hydrophobic interactions,electrostatic forces,and hydrogen bonding.The improved structural properties and extensive exposure of hydrophobic regions enabled a high curcumin loading capacity(~93%)and significantly enhanced thermal,digestive and storage stability.This study elucidates the application potential and molecular mechanisms of complex soy protein structures as active ingredient delivery carriers,aiming to provide new insights for designing efficient,plant-based nano-delivery systems for bio-actives.
文摘In this study,the pH-shifting method was used for the encapsulation of microbial canthaxanthin with soy protein hydrolysates to increase its antioxidant activity.Enzymatic hydrolysis improved the functional and structural properties of soy protein hydrolysates in comparison to native ones.Reducing power and radical quenching activity of hydrolysates were raised respectively from 14.6 and 0.05 to 92.9 and 0.19 and their bioactive loading properties were significantly increased more than five times.Encapsulation parameters,structural attributes,and antioxidant activity were also studied after complexation.Fourier transform infrared spectroscopy findings indicated the formation of hydrogen bonds between canthaxanthin and hydrolysates.The crystalline nature of canthaxanthin was changed to amorphous,according to the X-ray diffraction assay.Reducing power and radical quenching activity increased(respectively 2.3-fold and 1.5-fold).The results showed the positive effects of enzymatic hydrolysis of soy protein and the pH-driven method of encapsulation on improvement in the antioxidant activity of canthaxanthin.
