scholarly journals In Vitro Antithrombotic and Hypocholesterolemic Activities of Milk Fermented with Specific Strains of Lactococcus lactis

Nutrients ◽  
2019 ◽  
Vol 11 (9) ◽  
pp. 2150 ◽  
Author(s):  
Miguel Ángel Rendon-Rosales ◽  
María J. Torres-Llanez ◽  
Aarón F. González-Córdova ◽  
Adrián Hernández-Mendoza ◽  
Miguel A. Mazorra-Manzano ◽  
...  
Keyword(s):  
Bile Acid ◽  
Lactococcus Lactis ◽  
Binding Capacity ◽  
Biological Activities ◽  
Fermented Milk ◽  
Water Soluble ◽  
Gastrointestinal Digestion ◽  
Simulated Gastrointestinal Digestion ◽  
Bile Acid Binding ◽  
Micellar Solubility

Milk fermented with specific lactic acid bacteria (LAB) was reported to be a rich source of metabolites, such as peptides with different biological activities that may have a positive effect on cardiovascular health. Thus, in this study, the antithrombotic and hypocholesterolemic activities of fermented milk with specific strains of Lactococcus lactis were investigated before and after exposure to a simulated gastrointestinal digestion (SGD) model. The inhibition of thrombin-induced fibrin polymerization (IC50 peptide concentration necessary to inhibit thrombin activity by 50%), anticoagulant activity, inhibition of micellar solubility of cholesterol and bile acid binding capacity of water soluble fractions (WSF) <3 kDa from fermented milk were evaluated. Results indicated that the WSF from fermented milk with Lc-572 showed antithrombotic (IC50 = 0.049 mg/mL) and hypocholesterolemic (55% inhibition of micellar solubility of cholesterol and 27% bile acid binding capacity) activities. Meanwhile, fermented milk with Lc-571 showed mainly antithrombotic activity (IC50 = 0.045 mg/mL). On the other hand, fermented milk with Lc-600 presented mainly hypocholesterolemic activity (31.4% inhibition of micellar solubility of and 70% bile acid binding capacity). Moreover, biological activities were not lost after simulated gastrointestinal digestion conditions. Thus, fermented milk with these specific L. lactis strains show potential for the development of functional foods.

Stability, antioxidant activity and in vitro bile acid-binding of green, black and dark tea polyphenols during simulated in vitro gastrointestinal digestion

RSC Advances ◽  
2015 ◽  
Vol 5 (112) ◽  
pp. 92089-92095 ◽  
Author(s):  
Zhengmei Wu ◽  
Jianwen Teng ◽  
Li Huang ◽  
Ning Xia ◽  
Baoyao Wei
Keyword(s):  
Antioxidant Activity ◽  
Bile Acid ◽  
Phenolic Compounds ◽  
Binding Activity ◽  
Tea Polyphenols ◽  
Gastrointestinal Digestion ◽  
In Vitro Gastrointestinal Digestion ◽  
Bile Acid Binding ◽  
The Stability

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.

Bile acid binding capacity of fish protein hydrolysates from discard species of the West Mediterranean Sea

2015 ◽  
Vol 6 (4) ◽  
pp. 1261-1267 ◽  
Author(s):  
Raúl Pérez-Gálvez ◽  
Pedro J. García-Moreno ◽  
Rocío Morales-Medina ◽  
Antonio Guadix ◽  
Emilia M. Guadix
Keyword(s):  
Bile Acid ◽  
Mediterranean Sea ◽  
Binding Capacity ◽  
Protein Hydrolysates ◽  
Fish Protein ◽  
The West ◽  
Bile Acid Binding ◽  
Fish Protein Hydrolysates

Fish protein hydrolysates from six fish discard species in the West Mediterranean Sea were tested for theirin vitrobile acid binding capacity.

Identification of Casein Phosphopeptides in β-casein and Commercial Hydrolysed Casein by Mass Spectrometry

2006 ◽  
Vol 12 (5) ◽  
pp. 379-384 ◽  
Author(s):  
E. Miquel ◽  
J. A. Gómez ◽  
A. Alegría ◽  
R. Barberá ◽  
R. Farré ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Binding Capacity ◽  
Amino Acid Sequences ◽  
Gastrointestinal Digestion ◽  
Simulated Gastrointestinal Digestion ◽  
Casein Phosphopeptides ◽  
Hydrolysed Casein ◽  
Cluster Sequence

Casein phosphopeptides (CPPs) in commercial hydrolysed casein (CE90CPP) and in β-CN (β-CN) after simulated gastrointestinal digestion (gastric stage pepsin, pH =2, 37°C 2h) and intestinal stage (pancreatic-bile extract, pH =5.2, 37°C 2h) were sequenced by on-line reversed-phase high performance liquid chromatography coupled to electrospray ionisation tandem mass spectrometry (RP-HPLC-ESIMS/MS). In β-CN digest five peptides that contained four to five phosphate groups and the cluster sequence SpSpSpEE (residues 17-21) were identified. All CPPs with one exception β-CN(1-24)4P, had the protein fragment β-CN(1-25)4P, which is one of the main CPPs produced in vivo digestion of casein and the results of in vitro studies showed that this fragment enhanced calcium, iron and zinc absorption. In commercial hydrolysed casein CE90CPP 13 peptides were identified, only one of them, αs2-CN (1-13)3P, contained the cluster sequence SpSpSpEE but all the peptides have one or two phosphoserine residues with mineral binding capacity. These CPPs were shorter (527-2061 Da vs 2966-6512 Da) and less phosphorylated (1-3 P vs 4-5 P) than those released after simulated gastrointestinal digestion of β-CN. In both samples, the potential mineral chelating properties of these peptides in relation to their amino acid sequences and the presence of the phosphorylated cluster are discussed.

A comparison study on polysaccharides extracted from Laminaria japonica using different methods: structural characterization and bile acid-binding capacity

2017 ◽  
Vol 8 (9) ◽  
pp. 3043-3052 ◽  
Author(s):  
Jie Gao ◽  
Lianzhu Lin ◽  
Baoguo Sun ◽  
Mouming Zhao
Keyword(s):  
Bile Acid ◽  
Rheological Properties ◽  
Structural Characterization ◽  
Binding Capacity ◽  
Laminaria Japonica ◽  
Extraction Methods ◽  
Comparison Study ◽  
Bile Acid Binding

The structural characterization, rheological properties and bile acid-binding capacity of LP obtained by seven different extraction methods were investigated.

scholarly journals Comparative Peptidomics Analysis of Fermented Milk by Lactobacillus delbrueckii ssp. Bulgaricus and Lactobacillus delbrueckii ssp. Lactis

Foods ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 3028
Author(s):  
Hongji Ye ◽  
Xinyi Zhang ◽  
Yang Jiang ◽  
Min Guo ◽  
Xiaoming Liu ◽  
...  
Keyword(s):  
Bioactive Peptides ◽  
Fermented Milk ◽  
Lactobacillus Delbrueckii ◽  
Gastrointestinal Digestion ◽  
Peptide Profile ◽  
Simulated Gastrointestinal Digestion

Few studies have investigated the peptidomics of fermented milk by Lactobacillus delbrueckii. The aim of the present study was to interpret the peptidomic pattern of the fermented milk by five strains of L. delbrueckii ssp. bulgaricus and ssp. lactis prior to and after the simulated gastrointestinal digestion in vitro. The results indicated variations in the peptidomics among the samples, particularly between the samples of different subspecies. The peptides originating from β-casein were abundant in the samples of ssp. bulgaricus, whereas the peptides derived from αs1-casein and αs2-casein were more likely to dominate in those of ssp. lactis. For β-casein, the strains of ssp. bulgaricus displayed extensive hydrolysis in the regions of (73–97), (100–120), and (130–209), whereas ssp. lactis mainly focused on (160–209). The digestion appears to reduce the variations of the peptidomics profile in general. Among the five strains, L. delbrueckii ssp. bulgaricus DQHXNS8L6 was the most efficient in the generation of bioactive peptides prior to and after digestion. This research provided an approach for evaluating the peptide profile of the strains during fermentation and digestion.

scholarly journals Protein Engineering of Mung Bean (Vigna radiata (L.) Wilczek) 8Sα Globulin with Lactostatin

2020 ◽  
Vol 10 (24) ◽  
pp. 8787
Author(s):  
Ma. Carla Gamis ◽  
Lawrence Yves Uy ◽  
Antonio Laurena ◽  
Wilma Hurtada ◽  
Mary Ann Torio
Keyword(s):  
Liquid Chromatography ◽  
Bile Acid ◽  
Protein Engineering ◽  
Mung Bean ◽  
Binding Capacity ◽  
Protein Structures ◽  
Bioactive Peptide ◽  
Wild Type ◽  
Cholesterol Lowering ◽  
Bile Acid Binding

Mung bean is a well-known good source of protein. To increase its bioactivity, economic value, and nutritional content as a functional food and food additive, lactostatin (IIAEK), a cholesterol-lowering bioactive peptide, was engineered into mung bean 8Sα globulin, a major storage protein. The results showed that the mutated 8Sα globulin has a significant bile acid binding capacity (cholesterol-lowering activity) up to 47.25%. Moreover, superimposed mutant (Mut2) and wild-type (Wt) 3D protein structures showed a 93–97% identity, indicating that the mutant proteins are stable. Ultra-performance liquid chromatography(UPLC)-based assay showed similar retention time for wild-type and mutant protein samples. Both IIAEK peptide standard and Mut2 digest had comparable baseline peaks corresponding to the same molecular size based on the liquid chromatography-mass spectrometry (LC-MS) data. A 573.36-Da mass spectrum was seen in Mut2, which indicates that Mut2 8Sα globulin has been successfully mutated and digested to release the bioactive peptide, IIAEK. In vitro bile acid binding capacity showed that the 6-h Wt and 12-h engineered protein (Mut2) digests had the highest activity. Lastly, potential allergenicity was checked in the Allergen Database for Food Safety (ADFS) and the AllerBase database, and the IIAEK peptide matched the Bos d 5 epitopes. This study provides a strong foundation and basis for mung bean nutrition improvement, development of cholesterol-lowering food supplements, and protein engineering of other food proteins.

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