Browsing by Author "Ye A"
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- ItemCharacterizations of emulsion gel formed with the mixture of whey and soy protein and its protein digestion under in vitro gastric conditions(Elsevier B V, 2024-01-06) Cheng Y; Ye A; Singh H; Marangoni AGPartially replacing animal proteins with plant proteins to develop new products has much attention. To get knowledge of their application in emulsion gels, heat-induced composite protein emulsion gels were fabricated using the mixtures of whey protein isolate (WPI) and soy protein isolate (SPI) with the final total protein concentration of 10% (w/w). The water holding capacity (WHC), mechanical and rheological properties and microstructure of mixed protein emulsion gels prepared at different WPI to SPI ratios (100:0, 90:10, 70:30, 50:50, 30:70, 10:90, 0:100, w/w) were investigated. The ratios of WPI to SPI showed little effect on the WHC of the mixed protein emulsion gels (p > 0.05). Increasing the ratio of SPI decreased the hardness and storage modulus (G') of mixed protein emulsion gels, whereas the porosity of mixed protein emulsion gels in the microstructure increased, as shown by CLSM. Both β-lactoglobulin and α-lactalbumin from WPI and 7 S and 11 S from SPI participated in forming the gel matrix of mixed protein emulsion gels. More protein aggregates existed as the gel matrix filler at the high soy protein levels. Interestingly, the G' of mixed protein emulsion gels at the WPI to SPI ratio of 50:50 was higher than the sum of G' of individual WPI and SPI emulsion gels. The whey protein network predominated the gel matrix, while soy protein predominated in the active filling effect. When subjected to an in vitro dynamic gastric digestion model, soy protein in the gels (WPI:SPI = 50:50) degraded faster than whey protein during gastric digestion. This study provided new information on the characteristics of composite protein emulsion gel fabricated with the WPI and SPI mixture.
- ItemComparative lipidomics analysis of different-sized fat globules in sheep and cow milks(Elsevier B V, 2024) Pan Z; Ye A; Fraser K; Li S; Dave A; Singh HThe effect of milk fat globule (MFG) size and species (sheep versus cow) on the lipid and protein compositions of sheep and cow milks was studied. The MFGs in raw cow and sheep milks were separated into six significantly different-sized (1.5-5.5 μm) groups by a gravity-based separation method, and their fatty acids, their lipidomes and the protein compositions of their MFG membranes were determined. The proportions of polar lipids increased but glycoproteins decreased with decreasing MFG size in both sheep milk and cow milk; the fatty acid composition showed few differences among the MFG groups. The average size of each MFG group was comparable between sheep milk and cow milk. Sheep milk contained higher proportions of short-chain fatty acids, medium-chain fatty acids and sphingomyelin than cow milk in all MFG groups. The proportion of glycoproteins was higher in cow MFG membrane than in sheep MFG membrane. The results suggested that the lipid and protein compositions were markedly species and size dependent.
- ItemComparative lipidomics analysis of in vitro lipid digestion of sheep milk: Influence of homogenization and heat treatment(Elsevier Inc on behalf of the American Dairy Science Association, 2024-02) Pan Z; Ye A; Fraser K; Li S; Dave A; Singh HThis study investigated the changes in sheep milk lipids during in vitro gastrointestinal digestion in response to heat treatment (75°C/15 s and 95°C/5 min) and homogenization (200/50 bar) using lipidomics. Homogenized and pasteurized sheep milk had higher levels of polar lipids in gastric digesta emptied at 20 min than raw sheep milk. Intense heat treatment of homogenized sheep milk resulted in a reduced level of polar lipids compared with homogenized-pasteurized sheep milk. The release rate of free fatty acids during small intestinal digestion for gastric digesta emptied at 20 min followed the order: raw ≤ pasteurized < homogenized-pasteurized ≤ homogenized-heated sheep milk; the rate for gastric digesta emptied at 180 min showed a reverse order. No differences in the lipolysis degree were observed among differently processed sheep milks. These results indicated that processing treatments affect the lipid composition of digesta and the lipolysis rate but not the lipolysis degree during small intestinal digestion.
- ItemCorrigendum to "Kinetics of pepsin-induced hydrolysis and the coagulation of milk proteins" (J. Dairy Sci. 105:990-1003)(Elsevier Inc on behalf of the American Dairy Science Association, 2023-11) Yang M; Ye A; Yang Z; Everett DW; Gilbert EP; Singh HIn equation [3] (page 994), “1−” was placed incorrectly. The corrected equation reads as follows: [Formula Presented] The authors regret the error.
- ItemDifferences in small intestinal apparent amino acid digestibility of raw bovine, caprine, and ovine milk are explained by gastric amino acid retention in piglets as an infant model(Frontiers Media S.A., 2023-09-04) Ahlborn NG; Montoya CA; Roy D; Roy NC; Stroebinger N; Ye A; Samuelsson LM; Moughan PJ; McNabb WC; Gallier SBACKGROUND: The rate of stomach emptying of milk from different ruminant species differs, suggesting that the small intestinal digestibility of nutrients could also differ across these milk types. OBJECTIVE: To determine the small intestinal amino acid (AA) digestibility of raw bovine, caprine, and ovine milk in the piglet as an animal model for the infant. METHODS: Seven-day-old piglets (n = 12) consumed either bovine, caprine, or ovine milk diets for 15 days (n = 4 piglets/milk). On day 15, fasted piglets received a single meal of fresh raw milk normalized for protein content and containing the indigestible marker titanium dioxide. Entire gastrointestinal tract contents were collected at 210 min postprandially. Apparent AA digestibility (disappearance) in different regions of the small intestine was determined. RESULTS: On average, 35% of the dietary AAs were apparently taken up in the small intestine during the first 210 min post-feeding, with 67% of the AA digestibility occurring in the first quarter (p ≤ 0.05) and 33% in the subsequent two quarters. Overall, except for isoleucine, valine, phenylalanine, and tyrosine, the small intestinal apparent digestibility of all AAs at 210 min postprandially in piglets fed ovine milk was, on average, 29% higher (p ≤ 0.05) than for those fed bovine milk. Except for lysine, there was no difference in the apparent digestibility (p > 0.05) of any AAs between piglets fed caprine milk or ovine milk. The apparent digestibility of alanine was higher (p ≤ 0.05) in piglets fed caprine milk than those fed bovine milk. When apparent digestibility was corrected for gastric AA retention, only small differences in the small intestinal apparent digestibility of AAs were observed across milk types. CONCLUSION: Bovine, caprine and ovine milk had different apparent small intestinal AA digestibility at 210 min postprandially. When corrected for gastric AA retention, the differences in apparent digestibility across species largely disappeared. The apparent AA digestibility differed across small intestinal locations.
- ItemDigestion behaviour of capsaicinoid-loaded emulsion gels and bioaccessibility of capsaicinoids: Effect of emulsifier type(Elsevier B V, 2023-03-06) Luo N; Ye A; Wolber FM; Singh H; Sun QIn this study, the effect of emulsifier type, i.e. whey protein versus Tween 80, on the digestion behaviour of emulsion gels containing capsaicinoids (CAPs) was examined. The results indicate that the CAP-loaded Tween 80 emulsion gel was emptied out significantly faster during gastric digestion than the CAP-loaded whey protein emulsion gel. The Tween-80-coated oil droplets appeared to be in a flocculated state in the emulsion gel, had no interactions with the protein matrix and were easily released from the protein matrix during gastric digestion. The whey-protein-coated oil droplets showed strong interactions with the protein matrix, and the presence of thick protein layer around the oil droplets protected their liberation during gastric digestion. During intestinal digestion, the CAP-loaded Tween 80 emulsion gel had a lower extent of lipolysis than the CAP-loaded whey protein emulsion gel, probably because the interfacial layer formed by Tween 80 was resistance to displacement by bile salts, and/or because Tween 80 formed interfacial complexes with bile salts/lipolytic enzymes. Because of the softer structure of the CAP-loaded Tween 80 emulsion gel, the gel particles were broken down much faster and the oil droplets were liberated from the protein matrix more readily than for the CAP-loaded whey protein emulsion gel during intestinal digestion; this promoted the release of CAP molecules from the gel. In addition, the Tween 80 molecules displaced from the interface would participate in the formation of mixed micelles and would help to solubilize the released CAP molecules, leading to improved bioaccessibility of CAP. Information obtained from this study could be useful in designing functional foods for the delivery of lipophilic bioactive compounds.
- ItemDigestive diversity and kinetic intrigue among heated and unheated β-lactoglobulin species.(ROYAL SOC CHEMISTRY, 2014-11) Loveday SM; Peram MR; Singh H; Ye A; Jameson GBFood processing often alters the structure of proteins, and proteins are deliberately denatured and aggregated to improve technological functionality in many cases. However, the digestive consequences of processing-induced alterations to protein structure have only recently been studied. Here we explored the process-structure-digestibility relationship in the context of heat-processing effects on the structure and gastric digestibility of the bovine whey protein β-lactoglobulin (β-lg). Heating β-lg produces an array of non-native monomers, dimers and aggregates, and we have characterised these with reverse-phase high performance liquid chromatography (RP-HPLC) as a complement to our earlier work using polyacrylamide gel electrophoresis (PAGE) techniques. Using a combination of SDS-PAGE and RP-HPLC we have identified pepsin-resistant dimers and peptides that appear early in digestion. In an unexpected finding, native β-lg underwent complete hydrolysis during prolonged incubation (48 h) with pepsin. Two phases of hydrolysis were identified, and the transition between phases appears to result from alterations to the secondary structure of β-lg at 3-4 h, as measured with circular dichroism spectroscopy, and/or the binding and release of a pepsin inhibitor peptide. This work has unpacked some of the complexities of the processing-structure-digestibility relationship in a highly simplified system; further work is needed to explore the implications of these findings for food processors, regulatory authorities and consumers.
- ItemDynamic in vitro gastric digestion behavior of goat milk: Effects of homogenization and heat treatments.(Elsevier Inc on behalf of the American Dairy Science Association, 2022-02) Li S; Ye A; Pan Z; Cui J; Dave A; Singh HThe gastric digestion behavior of differently processed goat milks was investigated using a dynamic in vitro gastric digestion model, the human gastric simulator. Homogenization and heat treatment of goat milk resulted in gastric clots with highly fragmented structures. They also delayed the pH reduction during digestion, altered the chemical composition of the clots and the emptied digesta, promoted the release of calcium from the clots, and accelerated the hydrolysis and the emptying of milk proteins. The apparent density of the protein particles and the location of the homogenized fat globules changed during the digestion process, as shown in the emptied digesta of the homogenized goat milks. The effects of processing on the digestion behavior of goat milk were broadly similar to those previously reported for cow milk. However, the overall gastric digestion process of goat milk was more affected by homogenization than by heat treatments.
- ItemDynamic in vitro gastric digestion behaviour of camel milk(Elsevier Ltd, 2023-08) Li S; Ayyash M; Ye A; Singh HThis study investigated the dynamic in vitro gastric digestion behaviour of camel milk. Coagulum that was retainable in the stomach was not formed during the digestion of camel milk, whereas bovine milk reconstituted to the same protein concentration (2.9%, w/w) underwent pronounced gastric coagulation into structured clots. During early digestion, the camel milk formed small particles, resulting from its weak coagulation, that were preferentially emptied from the stomach. These particles became more compact and spherical in the first hour of digestion and then gradually decreased in size. Protein analysis indicated that the main camel milk proteins were digested in the order αS1-casein > β-casein > α-lactalbumin, which may have been modulated by the decreasing pH during the dynamic gastric digestion. This unique coagulation behaviour of camel milk resulted in its rapid gastric digestion and emptying, which may have nutritional implications.
- ItemDynamic In Vitro Gastric Digestion of Sheep Milk: Influence of Homogenization and Heat Treatment(MDPI (Basel, Switzerland), 2021-08-20) Pan Z; Ye A; Li S; Dave A; Fraser K; Singh H; Velickovic TCMilk is commonly exposed to processing including homogenization and thermal treatment before consumption, and this processing could have an impact on its digestion behavior in the stomach. In this study, we investigated the in vitro gastric digestion behavior of differently processed sheep milks. The samples were raw, pasteurized (75 °C/15 s), homogenized (200/20 bar at 65 °C)-pasteurized, and homogenized-heated (95 °C/5 min) milks. The digestion was performed using a dynamic in vitro gastric digestion system, the human gastric simulator with simulated gastric fluid without gastric lipase. The pH, structure, and composition of the milks in the stomach and the emptied digesta, and the rate of protein hydrolysis were examined. Curds formed from homogenized and heated milk had much looser and more fragmented structures than those formed from unhomogenized milk; this accelerated the curd breakdown, protein digestion and promoted the release of protein, fat, and calcium from the curds into the digesta. Coalescence and flocculation of fat globules were observed during gastric digestion, and most of the fat globules were incorporated into the emptied protein/peptide particles in the homogenized milks. The study provides a better understanding of the gastric emptying and digestion of processed sheep milk under in vitro gastric conditions.
- ItemEffect of Gel Structure on the In Vitro Gastrointestinal Digestion Behaviour of Whey Protein Emulsion Gels and the Bioaccessibility of Capsaicinoids(MDPI (Basel, Switzerland), 2021-03-04) Luo N; Ye A; Wolber FM; Singh H; Kontominas MGThis study investigated the effect of gel structure on the digestion of heat-set whey protein emulsion gels containing capsaicinoids (CAP), including the bioaccessibility of CAP. Upon heat treatment at 90 °C, whey protein emulsion gels containing CAP (10 wt% whey protein isolate, 20 wt% soybean oil, 0.02 wt% CAP) with different structures and gel mechanical strengths were formed by varying ionic strength. The hard gel (i.e., oil droplet size d4,3 ~ 0.5 μm, 200 mM NaCl), with compact particulate gel structure, led to slower disintegration of the gel particles and slower hydrolysis of the whey proteins during gastric digestion compared with the soft gel (i.e., d4,3 ~ 0.5 μm, 10 mM NaCl). The oil droplets started to coalesce after 60 min of gastric digestion in the soft gel, whereas minor oil droplet coalescence was observed for the hard gel at the end of the gastric digestion. In general, during intestinal digestion, the gastric digesta from the hard gel was disintegrated more slowly than that from the soft gel. A power-law fit between the bioaccessibility of CAP (Y) and the extent of lipid digestion (X) was established: Y = 49.2 × (X - 305.3)0.104, with R2 = 0.84. A greater extent of lipid digestion would lead to greater release of CAP from the food matrix; also, more lipolytic products would be produced and would participate in micelle formation, which would help to solubilize the released CAP and therefore result in their higher bioaccessibility.
- ItemEffect of ingestion temperature on the pepsin-induced coagulation and the in vitro gastric digestion behavior of milk(Elsevier Ltd, 2023-05) Yang M; Ye A; Yang Z; Everett DW; Gilbert EP; Singh HPepsin-induced protein coagulation occurs in the gastric environment when the milk pH is above the isoelectric point of casein proteins. In this study, the effect of milk temperature (4–48 °C) on the hydrolysis of κ-casein by pepsin and the consequent protein coagulation was studied at pH 6.0 for 120 min. Quantitative determination of the released para-κ-casein showed that both the κ-casein hydrolysis reaction rate constant and the pepsin denaturation rate constant increased with an increase in temperature. The temperature coefficient (Q10) of the specific hydrolysis of κ-casein was calculated to be ∼1.95. The coagulation process was investigated by the evolution of the storage modulus (Gʹ). At higher temperature, the milk coagulated faster but had a lower firming rate and Gʹmax with larger aggregates and voids were observed. The digestion behavior of the milk ingested at 4 °C, 37 °C, or 50 °C was investigated for 240 min in a human gastric simulator, in which the milk temperature increased or decreased to 37 °C (body temperature) over ∼ 60 min. The coagulation of the 4 °C milk was slower than for the 37 °C and 50 °C milk. The curd obtained from the 4 °C milk had a looser and softer structure with a significantly higher moisture content at the initial stage of digestion (20 min) which, in turn, facilitated the breakdown and hydrolysis of the caseins by pepsin. During the digestion, the curd structure became more cohesive, along with a decrease in moisture content. The knowledge gained from this study provides insight into the effect of temperature on the kinetics of pepsin-induced milk coagulation and the consequent digestion behavior.
- ItemHeat stability of sheep's skim milk: Aggregation and interaction of proteins(Elsevier Ltd, 2023-09) Pan Z; Ye A; Fraser K; Dave A; Singh HSheep's milk proteins are susceptible to heat-induced coagulation, but the protein interactions under high heat treatment have not been determined. Heat stability and protein interactions of sheep's skim milk (SSM) at pH 6.2–7.2 were examined at 140 °C. SSM had the longest heat coagulation time at pH 6.9, but became very unstable at higher or lower pH. Protein aggregates formed consisted mainly of whey proteins and κ-casein (κ-CN)-depleted casein micelles. Modification of SSM pH alters ionic calcium concentration, dissociation of caseins and electrostatic interactions, resulting in different extents of protein interactions. The extent of dissociation of κ-CN from casein micelles increased with increasing pH (from ∼6.6 to 7.0) before and after heat treatment, contributing to κ-CN-depleted casein micelle aggregation. High ionic calcium concentrations, low levels of κ-CN on casein micelles and ready dissociation of κ-CN from casein micelles may be responsible for the low heat stability of sheep's milk.
- ItemHeat-induced colloidal interactions of whey proteins, sodium caseinate and gum arabic in binary and ternary mixtures(Elsevier Ltd, 2013-11) Loveday SM; Ye A; Anema SG; Singh HMany food-grade proteins and polysaccharides will aggregate together when acidified or heated, due to electrostatic and hydrophobic interactions. At low concentrations, aggregates are soluble and colloidally stable, and they have potential applications as Pickering emulsifiers and nutrient carriers. Sodium caseinate (SC) and gum arabic (GA) at pH. 7 will form colloidal aggregates when heated, but aggregation is largely reversed on cooling. Whey proteins (in the form of whey protein isolate, WPI) will aggregate irreversibly with GA when they are heated together, but aggregation is often so rapid and extensive that aggregates precipitate. Here we sought to overcome those limitations, and to develop an in situ method for quantifying heat-induced aggregation. Aggregation was measured using temperature-controlled dynamic light scattering equipment and transmission electron microscopy. Combinations of SC, WPI and GA were heated at either pH. 7 or 3.5, and the weight ratio of protein to polysaccharide was held at 1:5 for simplicity. Heat-induced colloidally stable aggregates of SC. +. WPI. +. GA did not dissociate on cooling. Aggregation was measured in situ, both in temperature ramps and with isothermal experiments. In situ measurement allowed us to avoid potential artefacts stemming from the temperature changes and measurement delays associated with ex situ measurements. This work demonstrated how the size and heat-stability of colloidal protein-polysaccharide aggregates can be tailored by judicious selection of proteins, pH and heat treatment.
- ItemHigh-pressure processing of bovine milk: Effects on the coagulation of protein and fat globules during dynamic in vitro gastric digestion(Elsevier B V, 2022-09-15) He X; Yang M; Yuan F; Singh H; Ye A; Sun QThe effect of high-pressure processing (HPP) on the digestion behavior of skim and whole bovine milks was investigated using a human gastric simulator. Both milks formed clots during gastric digestion. HPP treatment led to the formation of a coagulum with a fragmented and crumbled structure, compared with the coagulum formed from untreated milk. At pressures over 400 MPa, more intense pressure resulted in looser and more fragmented gastric clot structures. The weight of the dried clots and the moisture content in the clots of the skim milk treated at 600 MPa were significantly lower and higher than that of untreated skim milk, respectively. The looser and more fragmented gastric clot structures consequently led to faster hydrolysis of the proteins by pepsin during gastric digestion. The denaturation of the whey proteins induced by HPP may have also altered the resistance of α-lactalbumin and β-lactoglobulin in the HPP-treated milk samples to pepsin hydrolysis. This study provides insights into the differences among untreated skim milk, untreated whole milk and HPP-treated milk under in vitro gastric digestion conditions. The structure of the clots formed in the gastric environment affects their breakdown and consequently their emptying rate into the intestine.
- ItemImpact of Recombined Milk Systems on Gastrointestinal Fate of Curcumin Nanoemulsion(Frontiers Media S.A., 2022-06-23) Qazi HJ; Ye A; Acevedo-Fani A; Singh H; Santini AMilk powder is an important ingredient in various foods and pediatric formulations. The textural and digestion properties of the formulations depend on the preheat treatment of the milk powder during manufacture. Thus, it is interesting to know how these modifications can influence on the release of fortified bioactive compounds during digestion with a milk matrix. In this study, a curcumin nanoemulsion was incorporated into milks reconstituted from low-heat, medium-heat and high-heat skim milk powders (SMPs) and the milks were subjected to semi dynamic in vitro digestion. All the recombined milk systems formed a curd under gastric conditions, which reduced the gastric emptying of protein and curcumin-loaded oil droplets. Because of the formation of heat-induced casein/whey protein complexes, the open fragmented curd formed by the high-heat-treated reconstituted powder resulted in higher protein and oil droplets emptying to the intestine and higher curcumin bioaccessibility. This study provides useful information for how protein ingredients can govern the fate of added health-promoting compounds during digestion.
- ItemKinetics of heat-induced interactions among whey proteins and casein micelles in sheep skim milk and aggregation of the casein micelles(Elsevier Inc on behalf of the American Dairy Science Association, 2022-05) Pan Z; Ye A; Dave A; Fraser K; Singh HThe interactions among the proteins in sheep skim milk (SSM) during heat treatments (67.5-90°C for 0.5-30 min) were characterized by the kinetics of the denaturation of the whey proteins and of the association of the denatured whey proteins with casein micelles, and changes in the size and structure of casein micelles. The relationship between the size of the casein micelles and the association of whey proteins with the casein micelles is discussed. The level of denaturation and association with the casein micelles for β-lactoglobulin (β-LG) and α-lactalbumin (α-LA) increased with increasing heating temperature and time; the rates of denaturation and association with the casein micelles were markedly higher for β-LG than for α-LA in the temperature range 80 to 90°C; the Arrhenius critical temperature was 80°C for the denaturation of both β-LG and α-LA. The casein micelle size increased by 7 to 120 nm, depending on the heating temperature and the holding time. For instance, the micelle size (about 293 nm) of SSM heated at 90°C for 30 min increased by about 70% compared with that (about 174.6 nm) of unheated SSM. The casein micelle size increased slowly by a maximum of about 65 nm until the level of association of the denatured whey proteins with casein micelles reached 95%, and then increased markedly by a maximum of about 120 nm when the association level was greater than about 95%. The marked increases in casein micelle size in heated SSM were due to aggregation of the casein micelles. Aggregation of the casein micelles and association of whey protein with the micelles occurred simultaneously in SSM during heating.
- ItemKinetics of pepsin-induced hydrolysis and the coagulation of milk proteins(Elsevier Inc and the Federation of Animal Science Societies on behalf of the American Dairy Science Association, 2022-02) Yang M; Ye A; Yang Z; Everett DW; Gilbert EP; Singh HHydrolysis-induced coagulation of casein micelles by pepsin occurs during the digestion of milk. In this study, the effect of pH (6.7–5.3) and pepsin concentration (0.110–2.75 U/mL) on the hydrolysis of κ-casein and the coagulation of the casein micelles in bovine skim milk was investigated at 37°C using reverse-phase HPLC, oscillatory rheology, and confocal laser scanning microscopy. The hydrolysis of κ-casein followed a combined kinetic model of first-order hydrolysis and putative pepsin denaturation. The hydrolysis rate increased with increasing pepsin concentration at a given pH, was pH dependent, and reached a maximum at pH ~6.0. Both the increase in pepsin concentration and decrease in pH resulted in a shorter coagulation time. The extent of κ-casein hydrolysis required for coagulation was independent of the pepsin concentration at a given pH and, because of the lower electrostatic repulsion between para-casein micelles at lower pH, decreased markedly from ~73% to ~33% when pH decreased from 6.3 to 5.3. In addition, the rheological properties and the microstructures of the coagulum were markedly affected by the pH and the pepsin concentration. The knowledge obtained from this study provides further understanding on the mechanism of milk coagulation, occurring at the initial stage of transiting into gastric conditions with high pH and low pepsin concentration.
- ItemModifying quinoa protein for enhanced functional properties and digestibility: A review(Elsevier B V, 2023-10-05) Cui H; Li S; Roy D; Guo Q; Ye AQuinoa (Chenopodium quinoa Willd.) is a pseudocereal plant that originally came from South America. The trend of consuming quinoa is propelled by its well‒balanced amino acid profile compared to that of other plants. In addition, its gluten‒free nature makes quinoa a promising diet option for celiac disease patients. Protein accounts for approximately 17% of the quinoa seed composition and quinoa protein possesses excellent quality. Quinoa protein is mainly composed of 11S globulins (37%) and 2S albumins (35%), both of which are stabilized by disulfide bonds. To date, the alkaline extraction method is the most commonly used method to extract quinoa protein. The functional properties and digestibility of quinoa protein can be improved with the help of various modification methods, and as a result, the application of quinoa protein will be extended. In this review, the extraction method, modification of functional properties and digestibility of quinoa protein are thoroughly discussed, providing insights into the application of quinoa protein in plant‒based foods.
- ItemMovements of moisture and acid in gastric milk clots during gastric digestion: Spatiotemporal mapping using hyperspectral imaging(Elsevier Ltd, 2024-01-15) Li S; Dixit Y; Reis MM; Singh H; Ye ARuminant milk is known to coagulate into structured clots during gastric digestion. This study investigated the movements of moisture and acid in skim milk clots formed during dynamic gastric digestion and the effects of milk type (regular or calcium-rich) and the presence/absence of pepsin. We conducted hyperspectral imaging analysis and successfully modelled the moisture contents based on the spectral information using partial least squares regression. We generated prediction maps of the spatiotemporal distribution of moisture within the samples at different stages of gastric digestion. Simultaneously to acid uptake, the moisture in the milk clots tended to decrease over the digestion time; this was significantly promoted by pepsin. Moisture mapping by hyperspectral imaging demonstrated that the high and low moisture zones were centralized within the clot and at the surface respectively. A structural compaction process promoted by pepsinolysis and acidification probably contributed to the water expulsion from the clots during digestion.