Isolation and identification of anti-colorectal cancer peptides from walnut proteins and associated in silico analysis

Xie, Jing; Hong, ZiShan; Dai, JingJing; Li, Tingting; Bai, Yuying; Zhang, Li; Hu, Xia; Chen, Jinlian; Sheng, Jun; Tian, Yang

doi:10.1016/j.jff.2023.105952

Cited by 7 publications

(2 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The regression equation was fitted using Design Expert 12, wherein the three independent variables of pH, enzymatic hydrolysis temperature, and enzymatic hydrolysis time were represented by A, B, and C, respectively. The quadratic multinomial regression model was obtained through multiple fitting regression of the ACE inhibition rate: Y = 63.67 + 0.915A − 0.7175B + 1.64C + 0.865AB + 0.61AC + 0.295BC − 2.23A 2 − 1.81B 2 − 1.66C 2 .…”

Section: Response Surface Regression Equationmentioning

confidence: 99%

“…To enhance the depth of processing efficiency and overall utilization rate of walnut meal, further processing of peptides derived from readily accessible walnut meal was undertaken. Current research on the active ingredients in walnuts mainly focuses on the extraction of polyphenols, flavonoids, proteins, and walnut oil, as well as their antioxidant, antibacterial, anti-inflammatory, anti-cancer, and memory improvement effects [2]. Current research efforts center on identifying natural bioactive compounds that can effectively reduce blood pressure, with ACE inhibitory peptides gaining significant attention.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Optimization of Extraction Process and Activity of Angiotensin-Converting Enzyme (ACE) Inhibitory Peptide from Walnut Meal

Meng,

She,

Feng

et al. 2024

Foods

View full text Add to dashboard Cite

In order to further realize the resource reuse of walnut meal after oil extraction, walnut meal was used as raw material to prepare polypeptide, and its angiotensin-converting enzyme (ACE) inhibitory activity was investigated. The ACE inhibitory peptides were prepared from walnut meal protein by alkaline solution and acid precipitation. The hydrolysis degree and ACE inhibition rate were used as indexes to optimize the preparation process by single-factor experiment and response surface method. The components with the highest ACE activity were screened by ultrafiltration, and their antioxidant activities were evaluated in vitro. The effect of gastrointestinal digestion on the stability of walnut peptide was analyzed by measuring molecular weight and ACE inhibition rate. The results showed that the optimal extraction conditions were pH 9.10, hydrolysis temperature 54.50 °C, and hydrolysis time 136 min. The ACE inhibition rate of walnut meal hydrolysate (WMH) prepared under these conditions was 63.93% ± 0.43%. Under the above conditions, the fraction less than 3 kDa showed the highest ACE inhibitory activity among the ACE inhibitory peptides separated by ultrafiltration. The IC50 value of scavenging ·OH free radical was 1.156 mg/mL, the IC50 value of scavenging DPPH free radical was 0.25 mg/mL, and the IC50 value of scavenging O2− was 3.026 mg/mL, showing a strong total reducing ability. After simulated gastrointestinal digestion in vitro, the ACE inhibitory rate of walnut peptide decreased significantly, but it still maintained over 90% ACE inhibitory activity. This study provides a reference for the application of low-molecular-weight walnut peptide as a potential antioxidant and ACE inhibitor.

show abstract

Section: Response Surface Regression Equationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%