Fabrication of soy protein-polyphenol covalent complex nanoparticles with improved wettability to stabilize high-oil-phase curcumin emulsions.

BACKGROUND: Recent studies have shown that the wettability of protein-based emulsifiers is critical for emulsion stability. However, few studies have been conducted to investigate the effects of varying epigallocatechin gallate (EGCG) concentrations on the wettability of protein-based emulsifiers. Additionally, limited studies have examined the effectiveness of soy protein-EGCG covalent complex nanoparticles with improved wettability as emulsifiers for stabilizing high-oil-phase (≥ 30%) curcumin emulsions. RESULTS: Soy protein isolate (SPI)-EGCG complex nanoparticles (SPIEn) with improved wettability were fabricated to stabilize high-oil-phase curcumin emulsions. The results showed that EGCG forms covalent bonds with SPI, which changes its secondary structure, enhances its surface charge, and improves its wettability. Moreover, SPIEn with 2.0 g L -1 EGCG (SPIEn-2.0) exhibited a better three-phase contact angle (56.8 ± 0.3o) and zeta potential (-27 mV) than SPI. SPIEn-2.0 also facilitated the development of curcumin emulsion gels at an oil volume fraction of 0.5. Specifically, the enhanced network between droplets as a result of the packing effects and SPIEn-2.0 with inherent antioxidant function was more effective at inhibiting curcumin degradation during long-term storage and ultraviolet light exposure. CONCLUSION: The results of the present study indicate that SPIEn with 2.0 g L -1 EGCG (SPIEn-2.0) comprises the optimum conditions for fabricating emulsifiers with improved wettability. Additionally, SPIEn-0.2 can improve the physicochemical stability of high-oil-phase curcumin emulsions, suggesting a novel strategy to design and fabricate high-oil-phase emulsion for encapsulating bioactive compounds. © 2024 Society of Chemical Industry.

Dynamic In Vitro Gastric Digestion Behaviour of Commercial Infant Formulae Made with Cow, Goat and Sheep Milk.

There are a wide range of commercial infant formulae available on the market. These are made using milk from different species, such as goat, sheep, and cow. The different protein compositions of these milks and the process used during infant-formulae manufacture, such as heat treatment, may impact the digestion of nutrients. This study compared the effect of protein composition and heat treatment on the in vitro gastric digestion behaviour of commercial infant formulae made with cow, goat, and sheep milk using a dynamic infant human gastric simulator (IHGS). During the simulated dynamic gastric digestion, the goat milk infant formula (GIF) showed earlier signs of aggregate formation compared to cow milk infant formula (CIF) and sheep milk infant formula (SIF). In addition, the microstructures of GIF chyme showed fragmented and porous structures. On the contrary, CIF formed dense protein networks that trapped oil droplets, whereas SIF exhibited a microstructure of smooth oil droplets surrounded by fewer protein networks. The different aggregation behaviours and aggregate structures of the three infant-formulae chyme were related to their different protein compositions, especially the different casein compositions. Furthermore, the open fragile structure of GIF aggregates provided easier access to pepsin, allowing it to hydrolyse protein. The results from the present study provided some information to assist in understanding the coagulation and digestion behaviours of commercial infant formulae made from different species of milk.

Dynamic Gastrointestinal Digestion of Bovine, Caprine and Ovine Milk Reconstituted from Commercial Whole Milk Powders.

The global dairy market has been increasingly diversified with more dairy product offerings of milk products from different animal species. Meanwhile, milk powders remain the main exported dairy product format due to their ease of transportation. In this work, we studied the structural changes, protein hydrolysis and nutrient delivery during dynamic gastric digestion and small intestinal digestion of cow, goat and sheep milk reconstituted from commercial whole milk powders. The results show that the reconstituted milks digest similarly to processed fresh milk. The digestion behaviors of the three reconstituted ruminant milks are broadly similar (gastric coagulation, kinetics of gastric emptying of protein and fat and the high digestibility in the small intestine) with some differences, which are likely contributed by the processing history of the milk powders. The delivery of individual amino acids to the small intestine differed between the early and late stages of gastric digestion, which were primarily affected by the abundance of amino acids in caseins and whey proteins but also by the difference between milk types associated with their gastric coagulation behaviors. This work showed that powdered milk is similar to fresh processed milk in digestion behavior, and the inherent differences between ruminant milks can be modified by processing treatments.

Delivery of encapsulated bioactive compounds within food matrices to the digestive tract: recent trends and future perspectives.

Encapsulation technologies have achieved encouraging results improving the stability, bioaccessibility and absorption of bioactive compounds post-consumption. There is a bulk of published research on the gastrointestinal behavior of encapsulated bioactive food materials alone using in vitro and in vivo digestion models, but an aspect often overlooked is the impact of the food structure, which is much more complex to unravel and still not well understood. This review focuses on discussing the recent findings in the application of encapsulated bioactive components in fabricated food matrices. Studies have suggested that the integration of encapsulated bioactive compounds has been proven to have an impact on the physicochemical characteristics of the finished product in addition to the protective effect of encapsulation on the fortified bioactive compound. These products containing bioactive compounds undergo further structural reorganization during digestion, impacting the release and emptying rates of fortified bioactive compounds. Thus, by manipulation of various food structures and matrices, the release and delivery of these bioactive compounds can be altered. This knowledge provides new opportunities for designing specialized foods for specific populations.

Food structure confers specific functionalities to supplemented encapsulated bioactive compounds during processing and digestion.Encapsulation of bioactive compounds prevents changes in physicochemical attributes of foods during processing.The unique disintegration patterns of foods in the gut impacts how bioactive substances are released and absorbed.

Heat Treatment and Homogenization Influence the Gastric Digestion of Bovine Milk Protein in Growing Pigs as an Adult Human Model.

BACKGROUND: Bovine milk processing influences the structure of the curd formed during gastric digestion, which may alter gastric protein hydrolysis and impact amino acid (AA) release into the small intestine. OBJECTIVES: This study aimed to determine the influence of heat treatment and homogenization on the gastric protein digestion and AA emptying of bovine milk. METHODS: Nine-wk-old pigs (n = 144) consumed either raw, pasteurized nonhomogenized (PNH), pasteurized homogenized (PH), or ultra-high-temperature homogenized (UHT) bovine milk for 10 d. On day 11, fasted pigs received the milk treatment (500 mL) before gastric contents were collected at 0, 20, 60, 120, 180, and 300 min postprandially. The apparent degree of gastric protein hydrolysis (based on the release of free amino groups), apparent gastric disappearance of individual proteins [based on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) gel band intensity], and the gastric emptying of digested protein and AA were determined. RESULTS: During the first 60 min, the rate of apparent gastric protein hydrolysis was fastest in pigs fed UHT milk (0.29%/min compared with on average 0.07%/min in pigs fed raw, PNH, and PH milk). Differences in the apparent degree of gastric protein hydrolysis and emptying were reflected in the rate of digested protein entering the small intestine. The AA gastric emptying half-time was generally shorter in pigs fed PH and UHT milk than in pigs fed raw and PNH milk. For example, the gastric release of total essential AA was >2-fold faster (P < 0.01) in pigs fed PH or UHT milk than that in pigs fed raw or PNH milk (i.e., homogenized compared with nonhomogenized milk). CONCLUSIONS: Heat treatment and homogenization increased the apparent gastric degree of protein hydrolysis and the release of digested protein into the small intestine. However, the rate of AA entering the small intestine was mainly increased by homogenization.

The novel lactoferrin and DHA-codelivered liposomes with different membrane structures: Fabrication, in vitro infant digestion, and suckling pig intestinal organoid absorption.

Inspired by membrane structure of breast milk and infant formula fat globules, four liposomes with different particle size (large and small) and compositions (Single phospholipids contained phosphatidylcholine, complex phospholipids contained phosphatidylcholine, phosphatidylethanolamine and sphingomyelin) were fabricated to deliver lactoferrin and DHA. In vitro infant semi-dynamic digestive behavior and absorption in intestinal organoids of liposomes were investigated. Liposomal structures were negligible changed during semi-dynamic gastric digestion while damaged in intestine. Liposomal degradation rate was primarily influenced by particle size, and complex phospholipids accelerated DHA hydrolysis. The release rate of DHA (91.7 ± 1.3 %) in small-sized liposomes (0.181 ± 0.001 µm) was higher than free DHA (unencapsulated, 64.6 ± 3.4 %). Complex phospholipids liposomal digesta exhibited higher transport efficiency (3.4-fold for fatty acids and 2.0-fold for amino acids) and better organoid growth than digesta of bare nutrients. This study provided new insights into membrane structure-functionality relationship of liposomes and may aid in the development of novel infant nutrient carriers.

Comparative lipidomics analysis of different-sized fat globules in sheep and cow milks.

The 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.

Characterizations of emulsion gel formed with the mixture of whey and soy protein and its protein digestion under in vitro gastric conditions.

Partially 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 ß-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.

Comparative lipidomics analysis of in vitro lipid digestion of sheep milk: Influence of homogenization and heat treatment.

This 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.

Protein digestibility of textured wheat protein (TWP)-based meat analogs: (II) Effects of sodium tripolyphosphate.

In this study, the effects of adding sodium tripolyphosphate during the extrusion of textured wheat protein (TWP)-based meat analogs were investigated. Five TWPs (TWP-C0, TWP-C0.10, TWP-C0.25, TWP-C0.50, and TWP-C0.75) were prepared with sodium tripolyphosphate concentrations of 0%, 0.10%, 0.25%, 0.50%, and 0.75%, respectively. The fibrous structure of TWPs was analyzed by determining their textural properties, degree of texturization, microstructure, and protein bonds. When the concentration of sodium tripolyphosphate increased from 0% to 0.75%, the fibers in TWPs became more regular and finer with smaller pores, the degree of texturization increased from 2.10 ± 0.09 to 2.73 ± 0.07, and the proportions of solubilized protein from the breaking of hydrophobic bonds and disulfide bonds increased from 2.06 ± 0.14% and 1.38 ± 0.11% to 3.42 ± 0.12% and 1.74 ± 0.05%, respectively. The results of particle size, soluble nitrogen content, and free amino acids of samples during digestion indicated that the disintegration rate and protein digestibility of TWPs increased with the increase in the concentration of sodium tripolyphosphate. After gastrointestinal digestion, the total free amino acids released in TWP-C0, TWP-C0.10, TWP-C0.25, TWP-C0.50, and TWP-C0.75 were 391.5 ± 2.2, 403.9 ± 1.5, 430.0 ± 3.6, 473.8 ± 2.9 and 485.3 ± 5.73 mg/10 g digesta, respectively. Sodium tripolyphosphate may improve the protein digestibility of TWPs by forming a finer fibrous structure with a more unfolded protein structure and more hydrophobic groups being exposed to enzymes.

Modifying quinoa protein for enhanced functional properties and digestibility: A review.

Quinoa (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.

Differences 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.

Background: 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.

The impact of differently structured starch gels on the gastrointestinal fate of a curcumin-containing nanoemulsion.

In this study, we focused on the in vitro gastrointestinal digestion of curcumin-nanoemulsion-loaded corn starch gels formed using starches with different amylose contents, i.e. waxy (WCS), normal (NCS) and high amylose (HACS) corn starches and their impact on the release and bioaccessibility of curcumin. Curcumin nanoemulsion (CNE) loading significantly increased the storage modulus of the WCS and NCS gels by interspersing in the gelatinized continuous phase, whereas it decreased in the HACS gel due to the formation of a weak network structure as a result of the incomplete gelatinized amylose granules. During the gastric digestion, the disintegration and emptying of the WCS + CNE gel from the stomach was the slowest compared to the other two gels. The changes in the stomach, influenced the emptying of total solids (HACS + CNE > NCS + CNE > WCS + CNE) into the gastric digesta, which further affected the rate of starch and lipid digestion during the intestinal phase. The HACS + CNE and NCS + CNE gels showed a higher and faster release of curcumin compared to the WCS + CNE gel that showed a slower and sustained release during the intestinal digestion. This study demonstrated that the oral-gastric digestion of these starch gels was more dependent on the gel structures rather than on the molecular properties of the starches. The dynamic gastric environment resulted in the formation of distinct gel structures, which significantly influenced the composition and microstructure of the emptied digesta, further affecting starch hydrolysis and curcumin bioaccessibility in the small intestine.

Role of Ca2+ in the pepsin-induced coagulation and in the dynamic in vitro gastric digestion behavior of casein micelles.

The effect of Ca2+ on pepsin-induced hydrolysis of κ-casein and subsequent coagulation of casein micelles was studied in a micellar casein (MC) solution at pH ≈ 6.0 at 37 °C without stirring. An NaCl-supplemented MC solution was used as a positive control to assess the effect of increased ionic strength after CaCl2 addition. Quantitative determination of the released para-κ-casein during the reaction using reverse-phase high-performance liquid chromatography showed that specific hydrolysis of κ-casein by pepsin was little affected by the addition of either CaCl2 or NaCl. However, rheological properties and microstructures of curds induced by pepsin hydrolysis depended markedly on the addition of salts. Addition of CaCl2 up to 17.5 mM facilitated coagulation, with decreases in coagulation time and critical hydrolysis degree, and increases in firming rate and maximum storage modulus (G'max); further addition of CaCl2 (22.5 mM) resulted in a lower G'max. Increased ionic strength to 52.5 mM by adding NaCl retarded the coagulation and resulted in a looser curd structure. In a human gastric simulator, MC, without the addition of CaCl2, did not coagulate until the pH decreased to ≈5.0 after ≈50 min of digestion. Addition of CaCl2 facilitated coagulation of casein micelles and resulted in more cohesive curds with dense structures during digestion, which slowed the emptying rate of caseins. At the same CaCl2 concentration, a sample with higher ionic strength coagulated more slowly. This study provides further understanding on the effect of divalent (Ca2+) ions and ionic strength on the coagulation of casein micelles and the digestion behavior of milk.

Structural Properties of Quinoa Protein Isolate: Impact of Neutral to High Alkaline Extraction pH.

In this work, we extracted proteins from white quinoa cultivated in the northeast of Qinghai-Tibet plateau using the method of alkaline solubilization and acid precipitation, aiming to decipher how extraction pH (7-11) influenced extractability, purity and recovery rate, composition, multi-length scale structure, and gelling properties of quinoa protein isolate (QPI). The results showed that protein extractability increased from 39 to 58% with the increment of pH from 7 to 11 whereas protein purity decreased from 89 to 82%. At pH 7-11, extraction suspensions and QPI showed the similar major bands in SDS-PAGE with more minor ones (e.g., protein fractions at > 55 or 25-37 kDa) in suspensions. Extraction pH had limited effect on the secondary structure of QPI. In contrast, the higher-order structures of QPI were significantly affected, e.g., (1) emission maximum wavelength of intrinsic fluorescence increased with extraction pH; (2) surface hydrophobicity and the absolute value of zeta-potential increased with increasing extraction pH from 7 to 9, and then markedly decreased; (3) the particle size decreased to the lowest value at pH 9 and then increased to the highest value at pH 11; and (4) denaturation temperature of QPI had a large decrease with increasing extraction pH from 7/8 to 9/10. Besides, heat-set QPI gels were formed by loosely-connected protein aggregates, which were strengthened with increasing extraction pH. This study would provide fundamental data for industrial production of quinoa protein with desired quality.

The use of confocal Raman microscopy and microfluidic channels to monitor the location and mobility of ß-carotene incorporated in droplet-stabilized oil-in-water emulsions.

This study sought to explore the combined use of confocal Raman microscopy and microfluidic channels to probe the location and mobility of hydrophobic antioxidant (ß-carotene) incorporated at the interface of food-grade droplet-stabilized emulsions (DSEs). Microfluidic channels were used to isolate emulsion droplets for efficient investigation of antioxidant mobility. This approach proved more conclusive than fixing the sample in agarose, because a single layer of droplets could be obtained. Results also indicated that the migration of ß-carotene incorporated in shell droplets of olive oil and trimyristin DSEs to core droplets was minimal and beta-carotene remained mostly localised at the interface even after 3 days of production. This work demonstrates that microfluidic isolation of emulsion droplets combined with confocal Raman microscopy can give new insights into the spatial variation of chemical composition within emulsions. This study revealed that the migration of ß-carotene between shell and core was minimal and hence it may be possible to concurrently deliver two incompatible compounds by spatially segregating them between shell and core compartments of DSEs.

Characteristics of Red Deer (Cervus elaphus) Milk: Lactational Changes in Composition and Processing Impacts on Structural and Gelation Properties.

In an increasingly diversified global market, milk of minor dairy species has gained interest as a novel and premium source of nutrition. Relative to the major dairy species, much is lacking in our understanding of red deer (Cervus elaphus) milk. In this study, we characterized the compositions (macronutrients, minerals, fatty acids, and proteins) of red deer milk and their variations throughout lactation. We also investigated the structures, physical properties, and gelation (acid- and rennet-induced) properties of deer milk and how they are impacted by typical processing treatments (e.g., homogenization and pasteurization). We identified unique features in the composition of deer milk, including being richer in protein, fat, calcium, zinc, iodine, branched-chain fatty acids, and α-linolenic acid than other ruminant milks. Different deer milk components displayed diverse variation patterns over the lactation cycle, many of which were different from those demonstrated in other ruminant species. Other physicochemical features of deer milk were identified, such as its markedly larger fat globules. Processing treatments were demonstrated to alter the structural and gelation properties of deer milk. Most of the gelation properties of deer milk resembled that of bovine milk more than ovine and caprine milks. This study furthers our understanding of red deer milk and will aid in its processing and applications in novel products.

Digestion behaviour of capsaicinoid-loaded emulsion gels and bioaccessibility of capsaicinoids: Effect of emulsifier type.

In 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.

Acid and rennet gelation properties of sheep, goat, and cow milks: Effects of processing and seasonal variation.

Gelation is an important functional property of milk that enables the manufacture of various dairy products. This study investigated the acid (with glucono-δ-lactone) and rennet gelation properties of differently processed sheep, goat, and cow milks using small-amplitude oscillatory rheological tests. The impacts of ruminant species, milk processing (homogenization and heat treatments), seasonality, and their interactions were studied. Acid gelation properties were improved (higher gelation pH, shorter gelation time, and higher storage modulus (G') by intense heat treatment (95°C for 5 min) to comparable extents for sheep and cow milks, both better than those for goat milk. Goat milk produced weak acid gels with low G' (<100 Pa) despite improvements induced by heat treatments. Seasonality had a marked impact on the acid gelation properties of sheep milk. The acid gels of late-season sheep milk had a lower gelation pH, no maximum in tan δ following gel formation, and 70% lower G' values than those from other seasons. We propose the potential key role of a critical acid gelation pH that induces structural rearrangements in determining the viscoelastic properties of the final gels. For rennet-induced gelation, compared with cow milk, the processing treatments of the goat and sheep milks had much smaller impacts on their gelation properties. Intense heat treatment (95°C for 5 min) prolonged the rennet gelation time of homogenized cow milk by 8.6 min (74% increase) and reduced the G' of the rennet gels by 81 Pa (85% decrease). For sheep and goat milks, the same treatment altered the rennet gelation time by only less than 3 min and the G' of the rennet gels by less than 14 Pa. This difference may have been caused by the different physicochemical properties of the milks, such as differences in their colloidal stability, proportion of serum-phase caseins, and ionic calcium concentration. The seasonal variations in the gelation properties (both acid and rennet induced) of goat milk could be explained by the minor variation in its protein and fat contents. This study provides new perspectives and understandings of milk gelation by demonstrating the interactive effects among ruminant species, processing, and seasonality.