Journal
FOOD CHEMISTRY
Volume 386, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2022.132811
Keywords
Mulberry anthocyanin extract; Soy protein hydrolysate; Pepsin; Papain; Color stability
Funding
- Six Talent Peaks Project in Jiangsu Province [NY-095]
- National Natural Science Founda-tion of China [31771978, 32001746]
- National First-class Discipline Program of Food Science and Technology [JUFSTR20180201]
- Innovation and Exploration Fund of State Key Laboratory of Food Science and Technology, Jiangnan University [SKLF-ZZB-202102]
- Fundamental Research Funds for the Central Universities [JUSRP21802]
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Soy protein papain hydrolysate (SPAH) and soy protein pepsin hydrolysate (SPEH) can protect mulberry anthocyanin extracts (MAEs) and enhance their stability at pH 6.3. SPEH has a higher binding affinity for C3G and can alter the secondary structures of SPAH and SPEH.
Soy protein papain hydrolysate (SPAH) and soy protein pepsin hydrolysate (SPEH) were used as protective agents for mulberry anthocyanin extracts (MAEs) to inhibit its color fading and enhance the anthocyanin stability at pH 6.3. Both SPAH and SPEH showed a significant protective effect on total anthocyanins in MAEs solutions. 1.0 mg/mL of SPEH presented the best protective effect on MAEs by increasing its half-life from 1.8 to 5.7 days. SPAH/SPEH-cyaniding-3-O-glucoside (C3G) interactions were investigated at pH 6.3 by fluorescence, Fourier-transform infrared spectroscopy (FT-IR), and Circular Dichroism (CD). Their association was mainly driven by hydrophobic interactions, and SPEH showed a higher binding affinity for C3G than SPAH, with a KA value of 2.62 x 10(5) M-1 at 300 K. The second structures of SPAH and SPEH were altered by C3G, with a decrease in the beta-sheets and an increase in the turns and random coils.
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