With the growth of global protein demand and the development of plant-based foods,pea protein,as a low-allergenic,nutritionally balanced and environmentally friendly plant protein,has shown great potential in replacin...With the growth of global protein demand and the development of plant-based foods,pea protein,as a low-allergenic,nutritionally balanced and environmentally friendly plant protein,has shown great potential in replacing animal protein.Pea protein is mainly composed of globulin and albumin,with a protein content of 20%to 30%,and has a balanced amino acid composition,as well as being rich in minerals and dietary fiber.It also possesses good foaming,gelling,emulsifying and antioxidant functional properties.However,pea protein also has inherent defects that limit its application in the food industry.This article systematically reviews the extraction techniques,functional properties,modification methods and application fields of pea protein,and focuses on evaluating the effects of different extraction and modification strategies on protein yield and functional properties.Research shows that ultrasonic-assisted alkaline extraction can reduce solvent usage by 55%,shorten extraction time by 50%,and increase extraction rate by 12.51%;under optimized conditions,ultrafiltration membrane technology can achieve a protein purity of 91%.In terms of modification,ultrasonic treatment increases foaming capacity by 37.4%,and phenolic cross-linking increases gel strength from 3.0 kPa to 48 kPa.This article provides data support and theoretical reference for the efficient extraction and functional optimization of pea protein,and has promoting significance for its wide application in plant-based foods.展开更多
This study investigated the effect of pH 11 adjustment and heat treatment on the foaming properties of soy protein.Untreated soy protein isolate(SPI)exhibited the lowest foaming capacity(~70%)and stability(~40%),which...This study investigated the effect of pH 11 adjustment and heat treatment on the foaming properties of soy protein.Untreated soy protein isolate(SPI)exhibited the lowest foaming capacity(~70%)and stability(~40%),which was attributed to intact protein aggregates with limited surface activity.pH-shifting improved foaming capacity(~130%)and stability(~60%)by partially unfolding proteins,alkaline hydrolysis,and exposing hydrophobic groups.Heat treatment further enhanced these properties,with moderate heating at 55℃and 65℃under pH shifting conditions yielding a balanced foaming capacity(~140-150%)and stability(~70-75%),primarily due to enhanced alkaline hydrolysis.At higher temperatures(75℃and 85℃),pH 11 adjustment combined with heating produced smaller peptides with superior interfacial activity,leading to the highest foaming capacity(~180%)and stability(~85%).These findings highlight the potential of pH shifting and controlled heat treatment to tailor the functionality of soy protein for aerated food applications,particularly whipped toppings and bakery foams products.展开更多
Vitamin C(VC)can greatly enhance the quality properties of dough and steamed bread in the food field.However,there are few studies on the interaction between VC and gluten,and the mechanism of VC influencing the foami...Vitamin C(VC)can greatly enhance the quality properties of dough and steamed bread in the food field.However,there are few studies on the interaction between VC and gluten,and the mechanism of VC influencing the foaming capacity,emulsifiablity,and dynamic viscosity of gluten is not clear.In this study,different content of VC(0,1%,2%,3%,4%and 5%)was added to gluten to obtain VC-gluten dough samples(CK,GV1,GV2,GV3,GV4 and GV5),and the properties of the VC-gluten dough were determined.Results showed that the increasing VC content lead to increase in the content of high-,medium-and low-molecular weight gluten,suggesting that VC improved the protein solubility of gluten.The G'and G"values of dough containing VC were higher than those of the control with the increase of scanning frequency.The foaming ability of gluten increased with the increase of VC content.Emulsibility of the dough of GV1 to GV 5 were significantly lower than that of the CK.Furthermore,VC could reduce the number of bubbles in gluten protein,when the VC content was less than 3%.In conclusion,VC might reduce the emulsifying characteristic and emulsifying stability of gluten,increase the solubility of gluten,and improve the dynamic viscosity of gluten dough by changing the content of disulfide bond in gluten.This study hopes to not only improve the functional characteristics of gluten protein,but also provide the basis for future development and improvement of VC-enriched health foods.展开更多
Grass pea is a legume crop with a protein content ranging from 20% to 30%,primarily composed of approximately 66% globulin,along with glutelin(15%),albumin(14%),and prolamin(5%).Grass pea protein(GPP)ingredients are c...Grass pea is a legume crop with a protein content ranging from 20% to 30%,primarily composed of approximately 66% globulin,along with glutelin(15%),albumin(14%),and prolamin(5%).Grass pea protein(GPP)ingredients are commonly isolated using alkaline extraction and acid precipitation methods.The water solubility of GPP ingredients is approximately 60%at neutral pH.However,the resulting functional attributes of these ingredients are relatively poor,which limits their application in numerous food and beverage products.This review describes the grass pea protein as an emerging source of plant proteins including structure,modification,functionality,as well as its applications in food systems.The functional attributes of GPP can be enhanced using various physical,chemical,and biological modification methods that alter the conformation,aggregation,or molecular weight of the proteins.Physical methods like ultrasonication,cold plasma,heat treatment,and high-pressure treatment,as well as chemical methods like protein-polysaccharide conjugation and enzymatic modification,have been used for this purpose.Modification techniques such as ultrasonication has the potential to enhance protein solubility by over 90% and also significantly improve emulsifying,foaming,and gelation properties of GPPs by more than two-fold.The properties of GPPs can be characterized using a variety of analytical methods including UV-visible spectroscopy,surface hydrophobicity,free sulfhydryl groups,Fourier transform infrared spectroscopy,circular dichroism,and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.In conclusion,GPP holds great potential for application in the formulation of plant-based foods and beverages in the food industry due to its good functional and nutritional properties.展开更多
This work evaluated the functional properties of sesame protein fractions in order to determine their potential in food applications.Sesame seed protein fractions were prepared according to their solubility:water-solu...This work evaluated the functional properties of sesame protein fractions in order to determine their potential in food applications.Sesame seed protein fractions were prepared according to their solubility:water-soluble(albumin),salt-soluble(globulin),alkaline-soluble(glutelin)and ethanol-soluble(prolamin).Globulin was the most abundant fraction,consisting of 91%protein,followed by glutelin,albumin and prolamin in decreasing order.Non-reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE)showed polypeptides of sizes≥20 kDa for albumin while glutelin and globulin had similar polypeptide sizes at 19,85 and 100 kDa.Prolamin had polypeptide sizes 20,40 and 100 kDa.The albumin and globulin fractions had higher intrinsic fluorescence intensity(FI)values than the glutelin.Albumin had a higher solubility(ranging from 80 to 100%)over a wide pH range when compared with the other fractions.Water holding capacity(g/g)reduced from 2.76(glutelin)to 1.35(prolamin)followed by 0.42(globulin)and 0.08(albumin).Oil holding capacity(g/g)reduced from:4.13(glutelin)to 2.57(globulin)and 1.56,1.50 for albumin and prolamin respectively.Gelling ability was stronger for prolamin and glutelin than albumin and globulin,while higher emulsion(p<0.05)quality was obtained for prolamin and albumin than for glutelin and globulin.展开更多
文摘With the growth of global protein demand and the development of plant-based foods,pea protein,as a low-allergenic,nutritionally balanced and environmentally friendly plant protein,has shown great potential in replacing animal protein.Pea protein is mainly composed of globulin and albumin,with a protein content of 20%to 30%,and has a balanced amino acid composition,as well as being rich in minerals and dietary fiber.It also possesses good foaming,gelling,emulsifying and antioxidant functional properties.However,pea protein also has inherent defects that limit its application in the food industry.This article systematically reviews the extraction techniques,functional properties,modification methods and application fields of pea protein,and focuses on evaluating the effects of different extraction and modification strategies on protein yield and functional properties.Research shows that ultrasonic-assisted alkaline extraction can reduce solvent usage by 55%,shorten extraction time by 50%,and increase extraction rate by 12.51%;under optimized conditions,ultrafiltration membrane technology can achieve a protein purity of 91%.In terms of modification,ultrasonic treatment increases foaming capacity by 37.4%,and phenolic cross-linking increases gel strength from 3.0 kPa to 48 kPa.This article provides data support and theoretical reference for the efficient extraction and functional optimization of pea protein,and has promoting significance for its wide application in plant-based foods.
基金supported by the National Key R&D Program of China(2024YFF1106500).
文摘This study investigated the effect of pH 11 adjustment and heat treatment on the foaming properties of soy protein.Untreated soy protein isolate(SPI)exhibited the lowest foaming capacity(~70%)and stability(~40%),which was attributed to intact protein aggregates with limited surface activity.pH-shifting improved foaming capacity(~130%)and stability(~60%)by partially unfolding proteins,alkaline hydrolysis,and exposing hydrophobic groups.Heat treatment further enhanced these properties,with moderate heating at 55℃and 65℃under pH shifting conditions yielding a balanced foaming capacity(~140-150%)and stability(~70-75%),primarily due to enhanced alkaline hydrolysis.At higher temperatures(75℃and 85℃),pH 11 adjustment combined with heating produced smaller peptides with superior interfacial activity,leading to the highest foaming capacity(~180%)and stability(~85%).These findings highlight the potential of pH shifting and controlled heat treatment to tailor the functionality of soy protein for aerated food applications,particularly whipped toppings and bakery foams products.
基金the National Natural Science Foundation of China(Project No.31771897,31871852,and 31772023).
文摘Vitamin C(VC)can greatly enhance the quality properties of dough and steamed bread in the food field.However,there are few studies on the interaction between VC and gluten,and the mechanism of VC influencing the foaming capacity,emulsifiablity,and dynamic viscosity of gluten is not clear.In this study,different content of VC(0,1%,2%,3%,4%and 5%)was added to gluten to obtain VC-gluten dough samples(CK,GV1,GV2,GV3,GV4 and GV5),and the properties of the VC-gluten dough were determined.Results showed that the increasing VC content lead to increase in the content of high-,medium-and low-molecular weight gluten,suggesting that VC improved the protein solubility of gluten.The G'and G"values of dough containing VC were higher than those of the control with the increase of scanning frequency.The foaming ability of gluten increased with the increase of VC content.Emulsibility of the dough of GV1 to GV 5 were significantly lower than that of the CK.Furthermore,VC could reduce the number of bubbles in gluten protein,when the VC content was less than 3%.In conclusion,VC might reduce the emulsifying characteristic and emulsifying stability of gluten,increase the solubility of gluten,and improve the dynamic viscosity of gluten dough by changing the content of disulfide bond in gluten.This study hopes to not only improve the functional characteristics of gluten protein,but also provide the basis for future development and improvement of VC-enriched health foods.
文摘Grass pea is a legume crop with a protein content ranging from 20% to 30%,primarily composed of approximately 66% globulin,along with glutelin(15%),albumin(14%),and prolamin(5%).Grass pea protein(GPP)ingredients are commonly isolated using alkaline extraction and acid precipitation methods.The water solubility of GPP ingredients is approximately 60%at neutral pH.However,the resulting functional attributes of these ingredients are relatively poor,which limits their application in numerous food and beverage products.This review describes the grass pea protein as an emerging source of plant proteins including structure,modification,functionality,as well as its applications in food systems.The functional attributes of GPP can be enhanced using various physical,chemical,and biological modification methods that alter the conformation,aggregation,or molecular weight of the proteins.Physical methods like ultrasonication,cold plasma,heat treatment,and high-pressure treatment,as well as chemical methods like protein-polysaccharide conjugation and enzymatic modification,have been used for this purpose.Modification techniques such as ultrasonication has the potential to enhance protein solubility by over 90% and also significantly improve emulsifying,foaming,and gelation properties of GPPs by more than two-fold.The properties of GPPs can be characterized using a variety of analytical methods including UV-visible spectroscopy,surface hydrophobicity,free sulfhydryl groups,Fourier transform infrared spectroscopy,circular dichroism,and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.In conclusion,GPP holds great potential for application in the formulation of plant-based foods and beverages in the food industry due to its good functional and nutritional properties.
基金Natural Sciences and Engineering Research Council of Canada(NSERC),funding reference number RGPIN 2018–06019Cette recherche aétéfinancée par le Conseil de recherches en sciences naturelles et en génie du Canada(CRSNG),numéro de référence RGPIN 2018–06019.
文摘This work evaluated the functional properties of sesame protein fractions in order to determine their potential in food applications.Sesame seed protein fractions were prepared according to their solubility:water-soluble(albumin),salt-soluble(globulin),alkaline-soluble(glutelin)and ethanol-soluble(prolamin).Globulin was the most abundant fraction,consisting of 91%protein,followed by glutelin,albumin and prolamin in decreasing order.Non-reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE)showed polypeptides of sizes≥20 kDa for albumin while glutelin and globulin had similar polypeptide sizes at 19,85 and 100 kDa.Prolamin had polypeptide sizes 20,40 and 100 kDa.The albumin and globulin fractions had higher intrinsic fluorescence intensity(FI)values than the glutelin.Albumin had a higher solubility(ranging from 80 to 100%)over a wide pH range when compared with the other fractions.Water holding capacity(g/g)reduced from 2.76(glutelin)to 1.35(prolamin)followed by 0.42(globulin)and 0.08(albumin).Oil holding capacity(g/g)reduced from:4.13(glutelin)to 2.57(globulin)and 1.56,1.50 for albumin and prolamin respectively.Gelling ability was stronger for prolamin and glutelin than albumin and globulin,while higher emulsion(p<0.05)quality was obtained for prolamin and albumin than for glutelin and globulin.
