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1.
Food Chem ; 457: 140214, 2024 Jun 24.
Artículo en Inglés | MEDLINE | ID: mdl-38959683

RESUMEN

This study investigated the gelling properties, rheological behaviour, and microstructure of heat-induced, low-salt myofibrillar protein (MP) gels containing different levels (2%, 4%, 6%, and 8%, w/w) of cross-linked (CTS) or acetylated (ATS) tapioca starch. The results indicated that either CTS or ATS significantly enhanced the gel strength and water-holding capacity of low-salt MP gels (P < 0.05), an outcome verified by the rheological behaviour test results under different modes. Furthermore, iodine-staining images indicated that the MP-dominated continuous phase gradually transited to a starch-dominated phase with increasing CTS or ATS levels, and 4% was the critical point for this phase transition. In addition, hydrophobic interactions and disulphide bonds constituted the major intermolecular forces of low-salt MP gels, effectively promoting phase transition. In brief, modified tapioca starches possess considerable potential application value in low-salt meat products.

2.
Meat Sci ; 217: 109595, 2024 Jul 10.
Artículo en Inglés | MEDLINE | ID: mdl-39004037

RESUMEN

The purpose of the present study was to investigate the mechanism of gel deterioration of myofibrillar proteins (MP) gels induced by high-temperature treatments based on the protein aggregation and conformation. The results showed that the gel strength and water holding capacity of MP obviously increased and then decreased as the temperature increased, reaching the maximum value at 80 °C (P < 0.05). The microstructure analysis revealed that appropriate temperature (80 °C) contributed to the formation of a more homogeneous, denser, and smoother three-dimensional mesh structure when compared other treatment temperatures, whereas excessive temperature (95 °C) resulted in the formation of heterogeneous and large protein aggregates of MP, decreasing the continuity of gel networks. This was verified by the rheological properties of MP gels. The particle size (D4,3 and D3,2) of MP obviously increased with larger clusters at excessive temperature, and the surface hydrophobicity of MP decreased (P < 0.05), which has been linked to the formation of soluble or insoluble protein aggregates. Tertiary structure and secondary structure results revealed that the proteins had a tendency to be more stretched under higher temperature treatments, which resulted in a decrease in covalent interactions and non-covalent interactions, fostering the over-aggregation of MP. Therefore, our present study indicated that the degradation of MP gels treated at high temperatures was explained by protein aggregation and conformational changes in MP.

3.
Meat Sci ; 216: 109555, 2024 Jun 04.
Artículo en Inglés | MEDLINE | ID: mdl-38850886

RESUMEN

In present study, the quality profiles, microstructures and in vitro digestibility of pork chip snacks (PCS) prepared by microwave vacuum drying (MVD) under different drying times (20, 21, 22, 23, and 24 min) were investigated. The results revealed significant decreases in the moisture content and L*-value of PCS, while the protein/ash contents, a*-value, and b*-value of PCS markedly increased with prolonged MVD time (P < 0.05). Additionally, as MVD time extended from 20 to 24 min, the textural characteristics of PCS, particularly brittleness and crunchiness, initially increased and then gradually decreased (P < 0.05). Scanning electron microscopy (SEM) images showed that a moderate MVD time (22 min) resulted in the formation of larger pores in PCS, enhancing brittleness and crunchiness. However, excessive MVD time (24 min) led to the melting of these pores, subsequently reducing the brittleness and crunchiness of PCS. Furthermore, in vitro protein digestibility of PCS gradually decreased with increasing MVD time, primarily attributed to increased protein aggregation, as indicated by changes in sulfhydryl contents. In summary, our findings highlight that PCS subjected to 22 min of MVD exhibited the highest overall acceptability. This study provides a novel strategy for the application of MVD in the processing of meat snacks.

4.
Meat Sci ; 215: 109554, 2024 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-38838569

RESUMEN

This study investigated the effect of ultrasound (US) combined with pre- and post-addition of κ-carrageenan (KC) on the gelling properties, structural characteristics and rheological behavior of myofibrillar proteins (MP) under low-salt conditions. The results showed that US combined with either pre- or post-addition of KC rendered higher gel strength and water holding capacity (WHC) of MP gels than those treated with US alone and added with KC alone (P < 0.05). US combined with pre-addition of KC facilitated the binding between MP and KC, which enhanced the gel strength and WHC of the mixed MP gels and significantly improved the rheological behavior of MP. This was also confirmed by the highest surface hydrophobicity, disulfide bonds and ß-sheet content of the MP gels with US combined with pre-addition of KC. Moreover, microstructural results reflected a denser structure for the pre-addition of KC in combination with US. However, US combined with post-addition of KC resulted in limited MP unfolding and relatively weak hydrophobic interactions in the composite gels, which were less effective in improving the gel properties of the MP gels. This study provides potential strategies for enhancing the gelling properties of low-salt meat products via application of US and KC.


Asunto(s)
Carragenina , Manipulación de Alimentos , Geles , Interacciones Hidrofóbicas e Hidrofílicas , Productos de la Carne , Reología , Carragenina/química , Animales , Geles/química , Productos de la Carne/análisis , Manipulación de Alimentos/métodos , Proteínas Musculares/química , Porcinos , Miofibrillas/química
5.
Meat Sci ; 213: 109511, 2024 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-38598966

RESUMEN

This study primarily aimed to investigate the influence of seaweed dietary fibre (SDF), as a potential alternative to phosphates, on the quality profiles and flavour attributes of frankfurters. The results revealed that SDF addition can significantly improve the cooking yield and texture characteristics of phosphate-free frankfurters (P < 0.05), and 1.00% SDF proved to be the optimal concentration for replacing phosphates in frankfurters. Moreover, electronic nose and electronic tongue analyses demonstrated that SDF incorporation potentially influences the aroma and taste of phosphate-free frankfurters. Furthermore, volatile compound analysis revealed that SDF addition potentially compensates for the decrease in volatile flavour compound content caused by phosphate deficiency. Generally, our results indicate that SDF can be successfully applied as a potential alternative to phosphates and subsequently improve the quality profiles and flavour attributes of phosphate-free frankfurters. Moreover, they provide valuable theoretical guidance for the processing of phosphate-free emulsified meat products.


Asunto(s)
Fibras de la Dieta , Productos de la Carne , Fosfatos , Algas Marinas , Gusto , Algas Marinas/química , Productos de la Carne/análisis , Fibras de la Dieta/análisis , Fosfatos/análisis , Animales , Humanos , Culinaria , Aromatizantes , Compuestos Orgánicos Volátiles/análisis , Odorantes , Porcinos , Masculino
6.
Food Res Int ; 182: 114177, 2024 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-38519164

RESUMEN

This work investigated the effect of ultrasound (US) treatment synergized with κ-carrageenan (KC) on the gel properties, structural characteristics and microstructures of myofibrillar protein (MP) gel. The results demonstrated that simply adding KC enhanced the gel strength and water holding capacity (WHC) of MP gels. Moreover, the gel strength and WHC of MP gels were increased by 56.67 % and 76.19 % via 20 min US treatment synergized with KC, which was mainly attributed to the changes in sulfhydryl content, surface hydrophobicity, and fluorescence intensity of MP gels. Based on the results of molecular docking and secondary structure, it can be hypothesized that the synergistic effect resulted in the rearrangement of the proteins, which altered the interaction site between MP gels and KC, accompanied by stronger binding. Furthermore, the microstructural results indicated that moderate US treatment (20 min) facilitated the production of a more compact and denser MP gels matrix with uniformly sized and distributed pores. However, excessive US treatment (40 and 50 min) caused the MP gels to form looser and disordered gel structure, which reduced the gel strength and WHC. This study suggested that combining of US and KC was a potential tactic to enhance the gelling properties of heat-induced MP gels.


Asunto(s)
Calor , Proteínas Musculares , Carragenina , Proteínas Musculares/química , Simulación del Acoplamiento Molecular , Reología , Geles/química , Agua/química
7.
Food Res Int ; 181: 114115, 2024 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-38448099

RESUMEN

The purpose of the present study was to investigate the gelling properties and in vitro digestibility of myofibrillar protein (MP) gels under low-salt condition as mediated by different concentrations of thermo-reversible curdlan gels (TRC) or thermo-irreversible curdlan gels (TIRC). The results showed that the incorporation of TRC or TIRC obviously improved the gel strength and water holding capacity of MP gels (P < 0.05). Those properties were most improved by adding 0.3 % TRC or TIRC with gel strength of 0.18 N or 0.17 N and WHC of 54.85 % or 49.05 %. Meanwhile, both TRC and TIRC promoted the transformation of α-helix into ß-sheet, as well as hydrophobic interactions and disulfide bonds, which are the main forces for the maintenance of the MP gels. The microstructure revealed that the formation of dense and uniform protein network structures can be promoted by the addition of TRC or TIRC. The different modes of interaction between TRC or TIRC and MP resulted in different microstructures of the MP gels. Furthermore, incorporation of TRC or TIRC significantly reduced in vitro protein digestibility, especially for the 0.3 % (w/w) form (P < 0.05). Meanwhile, MP gels had the lowest in vitro protein digestibility after the addition of TRC (66.67 %) compared to the form of TIRC (70.93 %). Therefore, our present study indicated that incorporation form of TRC or TIRC have distinct implications on regulating the gelling properties and in vitro digestibility of MP gels under low-salt condition.


Asunto(s)
Cloruro de Sodio , beta-Glucanos , Cloruro de Sodio Dietético , Geles
8.
Food Res Int ; 176: 113846, 2024 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-38163692

RESUMEN

The aim of this study was to investigate the effect of replacing different amounts (5 %, 10 %, 15 %, 20 % and 25 %) of lean meat with Tenebrio molitor larvae protein (TMLP) on the quality profiles of hybrid frankfurters. The results showed that there were no obvious differences in moisture, protein or fat content of all the hybrid frankfurters (P > 0.05), only a higher substitution rate (from 10 % to 25 %) resulted in a higher ash content than the control group (P < 0.05). With the increasing replacement rate (5 %, 10 % and 15 %), the cooking loss of the hybrid frankfurters showed the similar effects as the control group (P > 0.05), whereas the higher replacement rates of 20 % and 25 % obviously decreased the emulsion stability of the hybrid frankfurters. Moreover, with lower substitution rate (5 %, 10 % and 15 %) there were no significant differences in cooking loss between the hybrid frankfurters and the control group (P > 0.05), whereas the higher substitution rates (20 % and 25 %) obviously increased the cooking loss of the hybrid frankfurters (P < 0.05). Meanwhile, as the level of substitution increased, the hybrid frankfurters had higher digestibility, poorer texture than the standard frankfurters, as well as the rheological behaviour of hybrid meat batters (P < 0.05). The results showed that a moderate level (15 %) of TMLP was used to replace lean pork could be potentially and successfully be used to produce hybrid frankfurters.


Asunto(s)
Productos de la Carne , Tenebrio , Animales , Estudios de Factibilidad , Color , Culinaria , Productos de la Carne/análisis
9.
Int J Biol Macromol ; 257(Pt 1): 128569, 2024 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-38065443

RESUMEN

This work aimed to investigate the combined effect of ultrasound (US) treatment and κ-carrageenan (KC) addition on the gelling properties and rheological behaviors of myofibrillar protein (MP). Without US treatment, the KC incorporation promoted the gel strength and water-holding capacity (WHC) of MP gels. These properties were further improved by 20 min US treatment with gel strength of 98.61 g and WHC of 79.87 %, which was mainly attributed to changes associated with hydrophobic interactions and disulfide bonds and the transformation from α-helix to ß-sheet in MP gels. In addition, US treatment for 20 min effectively resulted in a more homogeneous polymer distribution of the MP-KC mixed system, leading to lower particle size and the largest G' and G″ values of the MP-KC mixed gels. However, longer US treatment times (30, 40 and 50 min) rendered lower gel strength, WHC, storage modulus and loss modulus of MP-KC mixed gels, which was mainly due to the formation of loose and disordered gel structures. Our present results indicated that the application of US to MP for an intermediate treatment time (20 min) combined with KC provides a potential and novel strategy to promote the gel qualities of heat-induced MP gels.


Asunto(s)
Proteínas Musculares , Carragenina , Geles/química , Proteínas Musculares/química , Interacciones Hidrofóbicas e Hidrofílicas , Tamaño de la Partícula , Reología
10.
Int J Biol Macromol ; 257(Pt 2): 128659, 2024 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-38101671

RESUMEN

The present work was aimed to investigate the effects of incorporating κ-carrageenan into myofibrillar protein (MP) as a dry powder (CP) or water suspension (CW) and the ionic strength (0.3 or 0.6 M sodium chloride (NaCl)) on MP physicochemical and gelling properties. The results indicated that incorporation of either CP or CW significantly increased turbidity, surface hydrophobicity, particle size and rheological behaviour of MP. In contrast, the protein solubility and fluorescence intensity of MP decreased when added with each form of κ-carrageenan (P < 0.05). These observed effects improved MP's gelling properties and produced a more compact and homogenous gel network after heating treatment. Moreover, the addition of CW rendered higher gel strength, water holding capacity and intermolecular interactions, such as ionic, hydrogen and disulphide bonds and hydrophobic interactions in MP gel compared with those added with CP, especially for 0.3 M NaCl (P < 0.05). Furthermore, addition of CW significantly decreased the α-helix content of MP gels (P < 0.05), which mainly contributing to the transformation from a random structure to an organised configuration. In addition, a higher NaCl concentration (0.6 M) enhanced the gelling properties of MP gels compared with 0.3 M NaCl concentration in the presence of each form of κ-carrageenan. Therefore, our present study indicated that incorporation form of κ-carrageenan and ionic strength have distinctive effects on regulating physicochemical characteristics and improves gelling properties of MP.


Asunto(s)
Cloruro de Sodio , Agua , Carragenina/química , Geles/química , Concentración Osmolar , Agua/química
11.
Int J Biol Macromol ; 248: 125903, 2023 Sep 01.
Artículo en Inglés | MEDLINE | ID: mdl-37479206

RESUMEN

The present study was aimed to investigate the intermolecular interaction between myofibrillar proteins (MP) and κ-carrageenan (KC) as mediated by KC concentration (0.1, 0.2, 0.3, and 0.4 %, w/w) and NaCl levels (0.3 and 0.6 M) based on the multiple spectroscopy and molecular docking. The results showed that the incorporation of KC increased the turbidity, zeta-potential, and surface hydrophobicity of MP-KC mixed sols with a dose-dependent manner, as well as significantly decreasing the protein solubility (P < 0.05), which indicated that the interaction between KC and MP promoted the expansion of protein structure and exposed more hydrophobic groups. Fluorescence spectra result revealed that the interaction between MP and KC was a static quenching in the fluorescence quenching process, which affected the aromatic amino acids residue microenvironment of MP. Moreover, the existence of KC decreased the α-helix contents of MP (P < 0.05), contributing to the transformation from random structure to organized configuration of MP. In addition, molecular forces, the molecular docking and thermodynamic parameters indicated that hydrophobic interactions, van der Waals force, and hydrogen bonding were considered as the main interaction forces between MP and KC. Furthermore, 0.6 M NaCl level rendered higher solubility and particle size, as well as lower turbidity and the surface hydrophobicity of MP-KC mixed sols than those with 0.3 M NaCl level (P < 0.05), which promoted the unfolding of MP molecule and subsequently increased the numbers of binding sites between MP and KC, facilitating the intermolecular interactions between MP and KC in mixed sols.


Asunto(s)
Cloruro de Sodio , Simulación del Acoplamiento Molecular , Carragenina/química , Sitios de Unión , Termodinámica , Espectrometría de Fluorescencia , Unión Proteica
12.
Meat Sci ; 204: 109265, 2023 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-37379703

RESUMEN

The effects and mechanism of incorporation of cross-linked tapioca starch (CTS) or acetylated tapioca starch (ATS) on the gel properties and in vitro digestibility of kung-wan (a Chinese-style meatball) were evaluated. The results indicated that incorporation of either CTS or ATS significantly enhanced the gel properties of kung-wan in a dose-dependent manner (P < 0.05), as well as the rheological properties of meat batter. Moreover, hydrogen bonds and electrostatic interaction were the major intermolecular forces in kung-wan when incorporated with CTS or ATS. Meanwhile, CTS and ATS acted as fillers in the meat protein gel matrix, which was further verified by the microstructure of kung-wan. However, CTS produced a more uniform and dense meat protein gel network than ATS, which was mainly due to its limited swelling characteristics. In addition, the incorporation of CTS or ATS significantly increased the in vitro digestibility of protein in kung-wan with increasing level of addition (P < 0.05). However, no significant differences in protein digestibility were detected between the CTS and ATS groups at the same addition level (P > 0.05). Our results provided some critical points for the actual application of modified tapioca starch to promote the quality profiles of kung-wan.


Asunto(s)
Manihot , Almidón , Almidón/química , Manihot/química , Manihot/metabolismo , Proteínas de la Carne
13.
Foods ; 12(7)2023 Apr 03.
Artículo en Inglés | MEDLINE | ID: mdl-37048328

RESUMEN

This study aimed to investigate the effects of different concentrations (0.1, 0.2, 0.3, 0.4, and 0.5% w/w) of Abelmoschus manihot gum (AMG) on the gel properties and in vitro digestibility of frankfurters. The results indicated that AMG incorporation significantly enhanced the emulsion stability and texture of frankfurters, as well as the dynamic rheological characteristics of raw meat batter, with the optimal concentration being 0.3% (p < 0.05). Furthermore, hydrogen bonds and disulphide bonds were the main molecular forces of the frankfurters in the presence of AMG. Microstructural images showed that more uniform and dense microstructures of frankfurters were formed due to AMG supplementation. In addition, AMG incorporation significantly increased the in vitro protein digestibility of frankfurters as the level of addition increased (p < 0.05). In conclusion, our results provided critical information for the practical application of AMG in the production of emulsified meat products.

14.
Ultrason Sonochem ; 95: 106379, 2023 May.
Artículo en Inglés | MEDLINE | ID: mdl-36965311

RESUMEN

Currently, as a promising alternative protein source, the interest of edible insect protein has been continuously increased. However, the extraction processing had distinct effects on the physicochemical properties and functionalities of this novel and sustainable protein. In this study, Tenebrio molitor larvae protein (TMLP) was extracted via ultrasound (US)-assisted alkaline extraction. The changes of extraction kinetics, physicochemical characteristics, and functional properties of TMLP as a function of US time (10, 20, 30, 40, 50 min) were investigated. The results showed that 30 min US treatment rendered the maximum protein yield (60.04 %) (P < 0.05). Meanwhile, Peleg's model was considered a suitable model to represent the extraction kinetics of TMLP, with a correlation coefficient of 0.9942. Moreover, the protein secondary structure, particle size, and amino acid profiles of TMLP were changed under the US-assisted alkaline extraction process. Additionally, a significant improvement of the functional properties of TMLP extracted with this method was observed compared to traditional alkaline extraction. In conclusion, the present work suggests that US-assisted alkaline extraction could be considered as a potential method to improve the protein yield, quality profiles, and functional properties of TMLP.


Asunto(s)
Tenebrio , Animales , Larva/química , Tenebrio/química , Tenebrio/metabolismo , Ultrasonografía , Aminoácidos/metabolismo , Tamaño de la Partícula
15.
Ultrason Sonochem ; 94: 106335, 2023 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-36821935

RESUMEN

Edible insects have been considered as a sustainable and novel protein source to replace animal-derived proteins. The present study aimed to extract Tenebrio molitor larvae proteins (TMP) using ultrasound-assisted alkaline extraction (UAE). Effects of different UAE times (10, 20, 30, 40, and 50 min) on the structural properties and in vitro digestibility of TMP were comparatively investigated with the traditional alkaline extraction method. The results revealed that ultrasonication could effectively alter the secondary/tertiary structures and thermal stability of TMP during UAE. The molecular unfolding and subsequent aggregation of TMP during UAE were mainly attributed to the formation of disulfide bonds and hydrophobic interactions. Moreover, TMP extracted by UAE had higher in vitro digestibility and digestion kinetics than those extracted without ultrasound, and the intermediate UAE time (30 min) was the optimal ultrasound parameter. However, longer UAE times (40 and 50 min) lowered the digestibility of TMP due to severe protein aggregation. The present work provides a potential strategy for the extraction of TMP with higher nutritional values.


Asunto(s)
Tenebrio , Animales , Larva/química , Tenebrio/química , Tenebrio/metabolismo , Interacciones Hidrofóbicas e Hidrofílicas
16.
Meat Sci ; 196: 109044, 2023 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-36410055

RESUMEN

This study was designed to investigate the utilization of seaweed dietary fiber (SDF) as a potential alternative to phosphates on the quality profiles of phosphate-free frankfurters. The results showed that the incorporation of SDF obviously promote the textural parameters of phosphate-free frankfurters, which was effectively verified by scanning electron microscopy. Meanwhile, SDF effectively retarded lipid oxidation of phosphate-free frankfurters during storage (P < 0.05). Moreover, 1.00% SDF was proven to show the best optimal phosphates replacing effect, as well as overcome the quality defects of phosphate-free frankfurters to the maximum extent. In addition, hydrogen bonding and hydrophobic interactions were the primary molecular force in SDF-added phosphate-free frankfurters. Therefore, our results implied that SDF can be considered as a feasible alternative for the processing of phosphate-free frankfurters with improved quality profile and superior health benefits which consistent with the demand of healthier meat products.


Asunto(s)
Productos de la Carne , Algas Marinas , Fosfatos , Fibras de la Dieta , Verduras
17.
Foods ; 11(22)2022 Nov 10.
Artículo en Inglés | MEDLINE | ID: mdl-36429173

RESUMEN

The present study investigated the additive effects of L-Arginine (L-Arg) with potassium carbonate (PC) on the quality characteristics of phosphate-free frankfurters. The results showed that L-Arg combined with PC could act as a viable phosphate replacer by decreasing cooking loss and improving the textural properties of phosphate-free frankfurters (p < 0.05), mainly because of its pH-raising ability. Moreover, L-Arg could assist PC in effectively retarding lipid oxidation in phosphate-free frankfurters during storage (p < 0.05). Furthermore, 0.1% L-Arg combined with 0.15% PC was found to exhibit the best optimal phosphate-replacing effect. This combination could also overcome quality defects and promote the sensory attributes of phosphate-free frankfurters to the maximum extent. Therefore, our results suggest that L-Arg combined with PC can be considered a feasible alternative for the processing of phosphate-free frankfurters with an improved quality profile and superior health benefits.

18.
Meat Sci ; 189: 108823, 2022 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-35429824

RESUMEN

Present study aimed to investigate the concentration effect of micronized cold-pressed hemp seed cake (MCPHSC) on the quality profiles and sensorial attributes of 50% phosphates reduced frankfurters. The results showed that MCPHSC could be used as an ideal phosphates replacer for obviously decreasing the cooking loss and promoting textural and gel properties of reduced-phosphates frankfurters (P < 0.05), which was verified by scanning electron microscopy. Moreover, the incorporation of MCPHSC could significantly inhibit the occurrence of lipid oxidation of reduced-phosphates frankfurters during storage in a dose-dependent manner (P < 0.05). Additionally, replacing 50% phosphates with 2% (w/w) MCPHSC was found to possess the best optimal replacement effect to enhance the quality profiles of reduced-phosphates frankfurters (P < 0.05). However, a higher amount of MCPHSC had a negative effect on the sensorial evaluations of the reduced-phosphates frankfurters. Our results suggested that the addition of MCPHSC could be applied as a practical way for improving the quality defects of reduced-phosphates frankfurters.


Asunto(s)
Cannabis , Productos de la Carne , Fosfatos , Culinaria , Manipulación de Alimentos/métodos , Semillas , Productos de la Carne/análisis
19.
Food Chem ; 385: 132733, 2022 Aug 15.
Artículo en Inglés | MEDLINE | ID: mdl-35318178

RESUMEN

The changes of physical stability and protein-lipid co-oxidation of oil-in-water (O/W) emulsions which stabilized by whey protein isolates (WPI) and ethanol pre-treated WPI (EWPI) under different homogenization methods were investigated. Compared with WPI, EWPI could obviously enhance the O/W emulsion's stability due to smaller particle size and higher level of adsorbed proteins. Moreover, protein-lipid co-oxidation was observed in both WPI and EWPI stabilized O/W emulsions and controlled by the characteristics of the adsorbed proteins. EWPI protect themselves from attacked of lipid oxidation products more effectively than WPI, showing lower N'-formyl-l-kynurenine or carbonyl contents and degree of aggregation, as well as higher fluorescence intensity. Furthermore, high-pressure homogenization induced higher levels of adsorbed proteins in O/W emulsions than ultrasound homogenization, resulting in a higher degree of protein oxidation and lower degree of lipid oxidation. Therefore, EWPI can be applied as an efficient emulsifier in emulsion foods with higher physical and oxidative stabilities.


Asunto(s)
Etanol , Agua , Emulsiones , Lípidos , Proteína de Suero de Leche
20.
Food Chem ; 385: 132700, 2022 Aug 15.
Artículo en Inglés | MEDLINE | ID: mdl-35305436

RESUMEN

Protein-lipid co-oxidation of whey protein isolate (WPI)-stabilized oil-in-water (O/W) emulsions with different ionic strengths (0, 100, 200, 300 and 400 mM) during storage were investigated. The results proved that changes in levels of adsorbed proteins induced by different ionic strengths could obviously affect the occurrence of protein-lipid co-oxidation. The level of oxidative stress was higher in adsorbed proteins extracted from control sample than in those extracted from emulsions with 300 or 400 mM ionic strengths. This was indicated by higher levels of N'-formyl-l-kynurenine (NFK) and carbonyl, lower fluorescence intensity and more serious unfolding of protein structure. Moreover, control sample showed the highest oxidative stability, which was indicated by lower levels of primary and secondary lipid oxidation products. These findings clearly illustrated that altered levels of adsorbed proteins induced by different ionic strengths play a crucial role in affecting protein-lipid co-oxidation in O/W emulsions.


Asunto(s)
Lípidos , Agua , Emulsiones/química , Concentración Osmolar , Oxidación-Reducción , Agua/química , Proteína de Suero de Leche/química
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