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1.
Food Res Int ; 195: 114944, 2024 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-39277222

RESUMEN

The gelation of milk proteins can be achieved by various means, enabling the development of diverse products. In this study, heat-set milk protein gels (15 % protein) of diverse textures were made by pH modulation and two gels were selected for dynamic in vitro gastric digestion: a spoonable soft gel (SG, pH 6.55' G' of ∼100 Pa) and a sliceable firm gel (FG, pH 5.65; G' of ∼7000 Pa). The two gels displayed markedly different structural changes and digestion kinetics during gastric digestion. The SG underwent substantial structural compaction during the first 120 min of gastric digestion into a denser and firmer gastric chyme (26.3 % crude protein, G* of ∼8500 Pa) than the chyme of the FG (15.7 % crude protein, G* of ∼3000 Pa). These contrasting intragastric structural changes of the gels reversed their original textural differences, which led to slower digestion and gastric emptying of proteins from the SG compared with the FG. The different intragastric pH profiles during the digestion of the two gels likely played a key role by modulating the proteolytic activity and specificity (to κ-casein) of pepsin. Preferential early cleavage of κ-casein in SG stimulated coagulation and compaction of solid chyme, whereas rapid hydrolysis of αS- and ß-caseins in the FG weakened coagulation. This study provided new insights into controlling the structural development of dairy-based foods during gastric digestion and modulating digestion kinetics.


Asunto(s)
Digestión , Geles , Calor , Proteínas de la Leche , Geles/química , Digestión/fisiología , Concentración de Iones de Hidrógeno , Cinética , Proteínas de la Leche/química , Proteínas de la Leche/metabolismo , Vaciamiento Gástrico , Caseínas/química , Caseínas/metabolismo , Pepsina A/metabolismo , Animales , Manipulación de Alimentos/métodos , Proteolisis
2.
Food Funct ; 15(10): 5613-5626, 2024 May 20.
Artículo en Inglés | MEDLINE | ID: mdl-38722062

RESUMEN

Modification of dairy proteins during processing impacts structural assemblies, influencing textural and nutritional properties of dairy products, and release and availability of amino acids during digestion. By modifying only pH, acid heat-set bovine dairy gels with divergent textural properties were developed to alter protein digestion. In vitro assay confirmed faster digestion of protein from a firm gel (pH 5.65) versus a soft gel (pH 6.55). We hypothesised that firm gel (FIRM-G; pH 5.6) would result in greater indispensable amino acid (IAA) appearance in circulation over 5 h and corresponding differences in gastric myoelectrical activity relative to soft gel (SOFT-G; pH 6.2). In a randomised, single-blind cross-over trial, healthy females (n = 20) consumed 150 g of each gel; plasma amino acid appearance was assessed over 5 hours. Iso-nitrogenous, iso-caloric gels were prepared from identical mixtures of bovine milk and whey protein concentrates; providing 17.7 g (FIRM-G) and 18.9 g (SOFT-G) of protein per serving. Secondary outcomes included gastric myoelectrical activity measured by body surface gastric mapping, glycaemic, triglyceridaemic, and subjective appetite and digestive responses. Overall plasma IAA (area under the curve) did not differ between gels. However, plasma IAA concentrations were higher, and increased more rapidly over time after SOFT-G compared with FIRM-G (1455 ± 53 versus 1350 ± 62 µmol L-1 at 30 min, p = 0.024). Similarly, total, branched-chain and dispensable amino acids were higher at 30 min with SOFT-G than FIRM-G (total: 3939 ± 97 versus 3702 ± 127 µmol L-1, p = 0.014; branched-chain: 677 ± 30 versus 619 ± 34 µmol L-1, p = 0.047; dispensable: 2334 ± 53 versus 2210 ± 76 µmol L-1, p = 0.032). All other measured parameters were similar between gels. Peak postprandial aminoacidaemia was higher and faster following ingestion of SOFT-G. Customised plasma amino acid appearance from dairy is achievable by altering gel coagulum structure using pH during processing and may have minimal influence on related postprandial responses, with implications for targeting food design for optimal health. The Clinical Trial Registry number is ACTRN12622001418763 (https://www.anzctr.org.au) registered November 7, 2022.


Asunto(s)
Aminoácidos , Estudios Cruzados , Geles , Femenino , Humanos , Adulto , Concentración de Iones de Hidrógeno , Aminoácidos/sangre , Aminoácidos/química , Geles/química , Animales , Adulto Joven , Bovinos , Digestión , Calor , Proteínas de la Leche/química , Método Simple Ciego , Estómago/fisiología , Estómago/química , Leche/química
3.
Food Chem ; 423: 136350, 2023 Oct 15.
Artículo en Inglés | MEDLINE | ID: mdl-37196409

RESUMEN

The study was carried out to investigate cricket protein hydrolysates' (CPH) potential to enhance the storage stability of cheddar cheese. The cricket protein (CP) samples pre-processed with microwave (T1), ultrasonication (T2) or without pre-treatment (T0) were used for developing the CPH using alcalase enzyme (3%). Freeze-dried CPH were incorporated in the cheese samples (CPH-T1, CPH-T2 and CPH-T0) at the maximum level of 1.5% and were analysed for quality during 3 months of storage (4 ± 1 °C) compared to the control samples without CPH. The pre-treatments significantly improved the antimicrobial and antioxidant potential of the CPH. The CPH exhibited a significant positive effect on antioxidant potential, lipid stability, protein oxidation, microbial growth, and sensory quality of the cheddar cheese during storage. Digestion simulation showed a significant positive impact on the antioxidant activity of the cheddar cheese. Our results indicate the potential of CPH to enhance the quality of fat-rich foods during storage.


Asunto(s)
Queso , Gryllidae , Animales , Antioxidantes , Queso/análisis , Hidrolisados de Proteína , Microondas , Estrés Oxidativo , Lípidos
4.
J Proteomics ; 276: 104836, 2023 03 30.
Artículo en Inglés | MEDLINE | ID: mdl-36764652

RESUMEN

Sheep meat (encompassing lamb, hogget and mutton) is an important source of animal protein in many countries, with a unique flavour and sensory profile compared to other red meats. Flavour, colour and texture are the key quality attributes contributing to consumer liking of sheep meat. Over the last decades, various factors from 'farm to fork', including production system (e.g., age, breed, feeding regimes, sex, pre-slaughter stress, and carcass suspension), post-mortem manipulation and processing (e.g., electrical stimulation, ageing, packaging types, and chilled and frozen storage) have been identified as influencing different aspects of sheep meat quality. However conventional meat-quality assessment tools are not able to elucidate the underlying mechanisms and pathways for quality variations. Advances in broad-based analytical techniques have offered opportunities to obtain deeper insights into the molecular changes of sheep meat which may become biomarkers for specific variations in quality traits and meat authenticity. This review provides an overview on how omics techniques, especially proteomics (including peptidomics) and metabolomics (including lipidomics and volatilomics) are applied to elucidate the variations in sheep meat quality, mainly in loin muscles, focusing on colour, texture and flavour, and as tools for authentication. SIGNIFICANCE: From this review, we observed that attempts have been made to utilise proteomics and metabolomics techniques on sheep meat products for elucidating pathways of quality variations due to various factors. For instance, the improvement of colour stability and tenderness could be associated with the changes to glycolysis, energy metabolism and endogenous antioxidant capacity. Several studies identify proteolysis as being important, but potentially conflicting for quality as the enhanced proteolysis improves tenderness and flavour, while reducing colour stability. The use of multiple analytical methods e.g., lipidomics, metabolomics, and volatilomics, detects a wider range of flavour precursors (including both water and lipid soluble compounds) that underlie the possible pathways for sheep meat flavour evolution. The technological advancement in omics (e.g., direct analysis-mass spectrometry) could make analysis of the proteins, lipids and metabolites in sheep meat routine, as well as enhance the confidence in quality determination and molecular-based assurance of meat authenticity.


Asunto(s)
Proteómica , Carne Roja , Ovinos , Animales , Carne/análisis , Carne Roja/análisis , Metabolómica , Lipidómica
5.
Foods ; 9(1)2020 Jan 03.
Artículo en Inglés | MEDLINE | ID: mdl-31947758

RESUMEN

The present study investigated the effect of processing parameters comprising rigor temperature, ageing and display time on conjugated linoleic acid (CLA) concentrations, stability and the development of cholesterol oxidation products in hot boned beef semimembranosus muscles. Meat samples, having attained rigor mortis at 5 °C and 25 °C, were vacuum packed and aged for 7 and 14 days and then displayed under aerobic conditions for 7 days at 4 °C. Lipid was extracted at each time interval then 1H NMR and GC-FID were used for CLA quantification. The cholesterol oxidation products (COPs) were separated from lipids via column chromatography and derivatized for GC-FID. The CLA content was not affected by the rigor temperature, ageing and display time (p > 0.05). The cholesterol oxidative stability was not affected by rigor temperature (p > 0.05) but was affected by ageing and display time (p < 0.05). The COPs, 7α- and 7ß-hydroxycholesterol, and 7-ketocholesterol were positively identified and their quantities increased with ageing and display time (p < 0.05). These results demonstrate that the production of COPs in semimembranosus muscle was significantly altered by the ageing and display time parameters but not by the rigor temperature used in this study.

6.
Food Res Int ; 120: 793-799, 2019 06.
Artículo en Inglés | MEDLINE | ID: mdl-31000299

RESUMEN

The effect of pulsed electric field (PEF) on in-vitro simulated gastrointestinal protein digestion of cold-boned deer Longissimus dorsi was elucidated. PEF treated samples viz. T1 (2.5 kV, 50 Hz) and T2 (10 kV, 90 Hz) along with a control were subjected to in-vitro simulated gastrointestinal protein digestion. Samples were collected after 0, 30, and 60 min of gastric digestion and 120 and 180 min of intestinal digestion. A significant (P < 0.05) increase was observed in the protein digestibility and soluble protein (%) of PEF treated samples, highlighting a positive influence of PEF processing on the digestion process. Higher concentrations of almost all the free amino acids were observed for the PEF treated samples. No significant effect of PEF was observed on the release of various minerals. PEF may be utilized for the development of novel muscle foods with improved protein digestibility.


Asunto(s)
Ciervos/metabolismo , Digestión , Manipulación de Alimentos/métodos , Carne Roja/análisis , Animales , Tracto Gastrointestinal , Técnicas In Vitro , Músculos Paraespinales/metabolismo , Fenómenos Físicos
7.
Meat Sci ; 114: 146-153, 2016 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-26773972

RESUMEN

The effects of rigor temperature (5, 15, 20 and 25°C), ageing (3, 7, 14, and 21 days) and display time on meat quality and lipid oxidative stability of hot boned beef M. Semimembranosus (SM) muscle were investigated. Ultimate pH (pH(u)) was rapidly attained at higher rigor temperatures. Electrical conductivity increased with rigor temperature (p<0.001). Tenderness, purge and cooking losses were not affected by rigor temperature; however purge loss and tenderness increased with ageing (p<0.01). Lightness (L*) and redness (a*) of the SM increased as rigor temperature increased (p<0.01). Lipid oxidation was assessed using (1)H NMR where changes in aliphatic to olefinic (R(ao)) and diallylmethylene (R(ad)) proton ratios can be rapidly monitored. R(ad), R(ao), PUFA and TBARS were not affected by rigor temperature, however ageing and display increased lipid oxidation (p<0.05). This study shows that rigor temperature manipulation of hot boned beef SM muscle does not have adverse effects on lipid oxidation.


Asunto(s)
Culinaria , Calor , Peroxidación de Lípido , Carne/análisis , Músculo Esquelético/metabolismo , Animales , Huesos , Bovinos , Color , Humanos , Concentración de Iones de Hidrógeno , Espectroscopía de Protones por Resonancia Magnética/métodos , Rigor Mortis , Estrés Mecánico
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