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1.
Int J Biol Macromol ; 267(Pt 2): 131157, 2024 May.
Artículo en Inglés | MEDLINE | ID: mdl-38552684

RESUMEN

This study aimed to investigate the impact of different pre-heating temperatures (ranging from 40 °C to 80 °C) on the interactions between soy protein isolate (SPI) and catechin to effectively control catechin encapsulation efficiency and optimize the emulsifying properties of soy protein isolate. Results showed that optimal heat treatment at 70 °C improved catechin encapsulation efficiency up to 93.71 ±â€¯0.14 %, along with the highest solubility, enhanced emulsification activity index and improved thermal stability of the protein. Multiple spectroscopic techniques revealed that increasing pretreatment temperature (from 40 °C to 70 °C) altered the secondary structures of SPI, resulting in a more stable unfolded structure for the composite system with a significant increase in α-helical structures and a decrease in random coil and ß-sheet structures. Moreover, optimal heat treatment also leads to an augmentation of free sulfhydryl groups within complex as well as exposure of more internal chromophore amino acids on molecular surface. Size-exclusion high-performance liquid chromatography and SDS-PAGE analysis indicated that the band intensity of newly formed high-molecular-weight soluble macromolecules (>180 kDa) increased as the pre-heating temperature rose. Furthermore, fluorescence spectroscopy and molecular docking analysis suggest that hydrophobic and covalent interactions were involved in complex formation, which intensified with increasing temperature.


Asunto(s)
Catequina , Calor , Simulación del Acoplamiento Molecular , Solubilidad , Proteínas de Soja , Proteínas de Soja/química , Catequina/química , Emulsiones/química , Interacciones Hidrofóbicas e Hidrofílicas , Calefacción , Unión Proteica , Emulsionantes/química , Estructura Secundaria de Proteína
2.
J Agric Food Chem ; 63(19): 4853-61, 2015 May 20.
Artículo en Inglés | MEDLINE | ID: mdl-25940322

RESUMEN

Changes in the structural and gel textural properties were investigated in soy protein isolate (SPI) that was subjected to extreme acid pH-shifting and mild heating processes. The SPI was incubated up to 5 h in pH 1.5 solutions at room temperature or in a heated water bath (50 or 60 °C) to lead to protein structural unfolding, followed by refolding at pH 7.0 for 1 h. The combination of pH-shifting and heating treatments resulted in drastic increases in the SPI gel penetration force (p < 0.05). These treatments also significantly enforced the conversion of sulphydryl groups into disulfides, increased the particle size and hydrophobicity values, reduced the protein solubility (p < 0.05), and strengthened the disulfide-mediated aggregation of SPI. The intrinsic fluorescence spectroscopy results indicated structural unravelling when protein was subjected to acidic pH-shifting in combination with heating processes. The slight loss of secondary structure was observed by circular dichroism. These results suggested that pH-shifting combined with heating treatments provide great potential for the production of functionality-improved SPI, with the improved gelling property highly related to changes in the protein structure and hydrophobic aggregation.


Asunto(s)
Proteínas de Soja/química , Ácidos/química , Dicroismo Circular , Geles/química , Calor , Concentración de Iones de Hidrógeno , Interacciones Hidrofóbicas e Hidrofílicas , Conformación Proteica , Solubilidad
3.
J Agric Food Chem ; 62(27): 6390-9, 2014 Jul 09.
Artículo en Inglés | MEDLINE | ID: mdl-24950913

RESUMEN

This study was conducted to evaluate the contributions of fat addition levels and storage duration at -18 °C to the oxidation and physicochemical changes of frozen pork dumpling filler. With an increase in the fat addition, thiobarbituric acid-reactive substances and carbonyl production increased (P < 0.05), the transition temperatures (Tmax) shifted to lower temperatures, and the total enthalpy (ΔH) of protein denaturation reduced (P < 0.05). Dynamic rheological measurements revealed a compromised viscoelastic network in filler protein gels with increased fat levels and storage time. Increasing the fat level also increased cooking loss and decreased breaking strength (P < 0.05). The sensory results showed that the dumplings with a high fat level had significantly higher texture, juiciness, and overall acceptability scores (P < 0.05). The results suggest that the dumplings with a high fat level stored for long periods enhanced oxidation and cooking loss and decreased breaking strength; however, it is important to add proper fat considering the palatability.


Asunto(s)
Grasas de la Dieta/análisis , Grasas/química , Productos de la Carne/análisis , Gusto , Animales , Culinaria , Almacenamiento de Alimentos , Congelación , Humanos , Oxidación-Reducción , Porcinos
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