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1.
Materials (Basel) ; 17(1)2023 Dec 29.
Artículo en Inglés | MEDLINE | ID: mdl-38204043

RESUMEN

Atomistic simulations on the creep of a nickel-based single-crystal superalloy are performed for examining whether the so-called rhenium effect can be tuned by changing the spatial distribution of rhenium in the nickel matrix phase. Results show that Rhenium dopants at {100} phase interfaces facilitate mobile partial dislocations, which intensify the creep, leading to a larger creep strain than that of a pure Ni/Ni3Al system containing no alloying dopants. If all the Re dopants in the matrix phase are far away from phase interfaces, a conventional retarding effect of Re can be observed. The current study implies a tunable Re effect on creep via dislocation triggering at the phase interfaces.

2.
Foods ; 12(11)2023 Jun 02.
Artículo en Inglés | MEDLINE | ID: mdl-37297491

RESUMEN

The stability and digestive properties of a dual-protein emulsion consisting of soy protein isolate (SPI) and whey protein isolate (WPI) have been systematically studied. The results showed that the particle size and viscosity of the dual-protein emulsion system decreased continuously with the increase in WPI, and this might be related to the large amount of electric charge on the surface of the emulsion droplets. Dual-protein emulsions with ratios of 3:7 and 5:5 showed the highest emulsion activity, while emulsion stability increased with the increase in WPI. The thicker adsorption layer formed at the interface might have contributed to this phenomenon. After in-vitro-simulated digestion, the emulsion droplet particle size increased substantially due to the weakened electrostatic repulsion on the droplet surface, especially for the intestinal digestion phase. Meanwhile, WPI accelerated the release of free fatty acids in the digestion process, which played a positive role in the nutritional value of the dual-protein emulsion. In accelerated oxidation experiments, WPI also improved the antioxidant properties of the dual-protein emulsion system. This study will provide a new insight and necessary theoretical basis for the preparation of dual-protein emulsions.

3.
Materials (Basel) ; 14(4)2021 Feb 04.
Artículo en Inglés | MEDLINE | ID: mdl-33557391
4.
Ultrason Sonochem ; 38: 225-233, 2017 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-28633822

RESUMEN

The effects of pulsed ultrasound (PUS) (power: 240w) with varying time (0, 3, 6, 9, 12 and 15min) on rheological and structural properties of chicken myofibrillar protein (CMP) were examined. PUS treatment significantly caused a decrease in the viscosity coefficients (k) but an increase in the flow index (n) value of CMP solutions within short time (0-6min), while had no significant effect for longer time (9-15min). Besides, at 6min, the solubility and microstructure of CMP samples were optimum. The primary structure of CMP was not altered by PUS treatment. However, Raman spectroscopy revealed a decrease in the α-helix and ß-sheets proportion and an increase in the ß-turn of CMP following PUS treatment. Random coil reached a maximum at 6min. The changes in tertiary and quaternary structure of CMP by PUS treatment also occurred. As PUS time extended, S0-ANS for CMP increased measured by ANS fluorescence probe method. However, the normalized intensity of 760cm-1 increased from 0min to 6min, and then decreased to 15min by Raman test. Moreover, the reactive sulphur (SH) contents and disulfide bonds (S-S) of samples increased while the total SH contents decreased within 0-6min. At 9min and above, the contents of reactive SH groups were almost equal to the contents of total SH groups. Differential scanning calorimetry (DSC) of CMP showed that peak temperature (Td2) for myosin and peak temperature (Td3) for actin were both reduced in the first 6min, while Td3 was not observed from 9min following PUS treatment. Therefore, 6min was the optimum PUS time to obtain better CMP rheological and structural properties.


Asunto(s)
Proteínas Musculares/química , Miofibrillas/química , Reología , Ondas Ultrasónicas , Animales , Pollos , Manipulación de Alimentos , Interacciones Hidrofóbicas e Hidrofílicas , Conformación Proteica en Hélice alfa , Conformación Proteica en Lámina beta , Solubilidad
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