The regulation of sodium alginate on the stability of ovalbumin-pectin complexes for VD3 encapsulation and in vitro simulated gastrointestinal digestion study

2021 ◽  
Vol 140 ◽  
pp. 110011
Author(s):  
Jian Gao ◽  
Chengzhi Liu ◽  
Jieyu Shi ◽  
Fangfang Ni ◽  
Qing Shen ◽  
...  
Antioxidants ◽  
2019 ◽  
Vol 8 (11) ◽  
pp. 563 ◽  
Author(s):  
Raquel Rodríguez-Solana ◽  
Natacha Coelho ◽  
Antonio Santos-Rufo ◽  
Sandra Gonçalves ◽  
Efrén Pérez-Santín ◽  
...  

Carob liqueur is a traditional Mediterranean alcoholic beverage obtained via a wide range of production techniques contributing to the different organoleptic attributes of the final product. The aim of this research was to evaluate the stability of the chemical composition and biological capacities (antioxidant and enzyme inhibition) under in vitro simulated gastrointestinal digestion of liqueurs prepared by flavouring the fig spirit with carob pulp by maceration, distillation, percolation, or aqueous and hydro-alcoholic infusions. For this purpose, the phenolic and furanic compositions, the total phenolic (TPC) and flavonoid (TFC) contents, antioxidant capacity (AC), and enzyme inhibitory potential against acethylcholinesterase, tyrosinase, α-glucosidase and α-amylase enzymes were evaluated. The content of gallic acid decreased after gastrointestinal digestion, while TPC, TFC, and AC significantly increased after each digestion phase. Overall, no significantly different enzyme inhibitions (p < 0.05) were observed among digested liqueurs, with moderate inhibition against acethylcholinesterase and tyrosinase (enzymes related with neurodegenerative diseases), and potent and low inhibitory capacities for α-glucosidase and α-amylase, respectively (ideal conditions employed in antidiabetic therapy). The study indicates that hydro-alcoholic infusion and maceration were the most appropriate methods to obtain liqueurs with higher values of the aforementioned parameters and safe levels of toxic furanics.


RSC Advances ◽  
2015 ◽  
Vol 5 (112) ◽  
pp. 92089-92095 ◽  
Author(s):  
Zhengmei Wu ◽  
Jianwen Teng ◽  
Li Huang ◽  
Ning Xia ◽  
Baoyao Wei

The stability and antioxidant activity of phenolic compounds, as well as the bile acid-binding activity of green, black, raw liubao and aged liubao tea duringin vitrogastrointestinal digestion were evaluated.


2021 ◽  
Vol 343 ◽  
pp. 128394
Author(s):  
Eslim Sugey Sandoval-Sicairos ◽  
Ada Keila Milán-Noris ◽  
Diego Armando Luna-Vital ◽  
Jorge Milán-Carrillo ◽  
Alvaro Montoya-Rodríguez

2020 ◽  
Vol 21 (3) ◽  
pp. 1059 ◽  
Author(s):  
Ruidan Wang ◽  
Xin Lu ◽  
Qiang Sun ◽  
Jinhong Gao ◽  
Lin Ma ◽  
...  

The aim of this study was to isolate and identify angiotensin I-converting enzyme (ACE) inhibitory peptides from sesame protein through simulated gastrointestinal digestion in vitro, and to explore the underlying mechanisms by molecular docking. The sesame protein was enzymatically hydrolyzed by pepsin, trypsin, and α-chymotrypsin. The degree of hydrolysis (DH) and peptide yield increased with the increase of digest time. Moreover, ACE inhibitory activity was enhanced after digestion. The sesame protein digestive solution (SPDS) was purified by ultrafiltration through different molecular weight cut-off (MWCO) membranes and SPDS-VII (< 3 kDa) had the strongest ACE inhibition. SPDS-VII was further purified by NGC Quest™ 10 Plus Chromatography System and finally 11 peptides were identified by Nano UHPLC-ESI-MS/MS (nano ultra-high performance liquid chromatography-electrospray ionization mass spectrometry/mass spectrometry) from peak 4. The peptide GHIITVAR from 11S globulin displayed the strongest ACE inhibitory activity (IC50 = 3.60 ± 0.10 μM). Furthermore, the docking analysis revealed that the ACE inhibition of GHIITVAR was mainly attributed to forming very strong hydrogen bonds with the active sites of ACE. These results identify sesame protein as a rich source of ACE inhibitory peptides and further indicate that GHIITVAR has the potential for development of new functional foods.


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