Nanocomplexation between Curcumin and Soy Protein Isolate: Influence on Curcumin Stability/Bioaccessibility and in Vitro Protein Digestibility

2015 ◽  
Vol 63 (13) ◽  
pp. 3559-3569 ◽  
Author(s):  
Fei-Ping Chen ◽  
Bian-Sheng Li ◽  
Chuan-He Tang
Keyword(s):  
Soy Protein ◽  
Soy Protein Isolate ◽  
Protein Digestibility ◽  
Protein Isolate ◽  
In Vitro Protein Digestibility ◽  
Vitro Protein

Partial substitution of soy protein isolates with cricket flour during extrusion affects firmness and in vitro protein digestibility

2020 ◽  
Vol 6 (2) ◽  
pp. 169-177 ◽  
Author(s):  
S.M. Kiiru ◽  
J.N. Kinyuru ◽  
B.N. Kiage ◽  
A.K. Marel
Keyword(s):  
Soy Protein ◽  
Protein Digestibility ◽  
Partial Substitution ◽  
Meat Production ◽  
In Vitro Protein Digestibility ◽  
Low Fat ◽  
Alternative Source ◽  
The Impact ◽  
Vitro Protein

The rapid increase in global population and the unsustainable conventional meat production have created demand for alternative animal-derived protein. Traditionally, soy has been utilised in structuring meat analogues. Currently, edible insects are researched as a potential alternative source of proteins and a valuable ingredient in development of meat analogues. High moisture extrusion was applied to a mixture of soy protein isolate (SPI) and full or low-fat cricket flour (CF) and the impact of cricket inclusion levels as well as extruder barrel temperature on the firmness and in vitro protein digestibility was evaluated. The SPI flour was substituted at 0 (control), 15, 30 and 45% and extruded on a laboratory co-rotating twin-screw extruder with a throughput of 1 kg/h at 150 rpm screw speed. Cooking temperature was varied at 120, 140 and 160 °C and water flowrate set to 10 ml/min. Texture as evaluated on all the treatments by texture profile analysis while the in vitro crude protein digestibility (CPD) was done on raw flours and extrudates with 15 and 45% CF inclusion and at 120 and 160 °C. The extrusion temperature had a negative correlation (r=-0.49) with the CPD but the CF inclusion had a correlation; r=0.71 (120 °C) and -0.28 (160 °C). The highest CPD (50%) was recorded from 45% full-fat CF extruded blend at 120 °C. Firmness was positively influenced (r=0.56) by temperature but negatively influenced (r≈-0.57) by CF inclusions at selected temperatures. Overall the low-fat CF blends had lower firmness values compared to their full-fat counterparts and control samples. The findings from this research demonstrated to be relevant for processing of high-protein and insect-based meat alternatives for food dependencies.

Physical-chemical properties and in vitro digestibility of phosphorylated and glycosylated soy protein isolate

LWT ◽  
2021 ◽  
Vol 152 ◽  
pp. 112380
Author(s):  
Jingyuan Liu ◽  
Yangling Wan ◽  
Liuyang Ren ◽  
Mengdi Li ◽  
Ying Lv ◽  
...  
Keyword(s):  
Soy Protein ◽  
Soy Protein Isolate ◽  
Chemical Properties ◽  
Protein Isolate ◽  
In Vitro Digestibility ◽  
Physical Chemical

scholarly journals Interaction of Soy Protein Isolate Hydrolysates with Cyanidin-3-O-Glucoside and Its Effect on the In Vitro Antioxidant Capacity of the Complexes under Neutral Condition

Molecules ◽  
2021 ◽  
Vol 26 (6) ◽  
pp. 1721
Author(s):  
Yaru Wu ◽  
Zhucheng Yin ◽  
Xuejiao Qie ◽  
Yao Chen ◽  
Maomao Zeng ◽  
...  
Keyword(s):  
Antioxidant Capacity ◽  
Soy Protein ◽  
Average Particle Size ◽  
Soy Protein Isolate ◽  
Surface Hydrophobicity ◽  
Protein Isolate ◽  
Antagonistic Effect ◽  
Masking Effect ◽  
Average Particle

The interaction of soy protein isolate (SPI) and its hydrolysates (SPIHs) with cyanidin-3-O-glucoside (C3G) at pH 7.0 were investigated to clarify the changes in the antioxidant capacity of their complexes. The results of intrinsic fluorescence revealed that C3G binds to SPI/SPIHs mainly through hydrophobic interaction, and the binding affinity of SPI was stronger than that of SPIHs. Circular dichroism and Fourier-transform infrared spectroscopy analyses revealed that the interaction with C3G did not significantly change the secondary structures of SPI/SPIHs, while the surface hydrophobicity and average particle size of proteins decreased. Furthermore, the SPI/SPIHs-C3G interaction induced an antagonistic effect on the antioxidant capacity (ABTS and DPPH) of the complex system, with the masking effect on the ABTS scavenging capacity of the SPIHs-C3G complexes being lower than that of the SPI-C3G complexes. This study contributes to the design and development of functional beverages that are rich in hydrolysates and anthocyanins.

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