Evaluation of Saccharomyces cerevisiae as an anti-fumonisin B1 additive in a horse digestion model

2017 ◽  
Vol 10 (2) ◽  
pp. 121-130
Author(s):  
F.M.P. Taran ◽  
V.P. Silva ◽  
L. Abrunhosa ◽  
C.A.R. Rosa ◽  
A. Venâncio ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Crude Protein ◽  
Liquid Fraction ◽  
Fumonisin B1 ◽  
In Vitro Digestion ◽  
Enzymatic Digestion ◽  
In Vitro Assays ◽  
Yeast Strains ◽  
Maize Grain

In this study, the capacity of Saccharomyces cerevisiae to adsorb fumonisin B1 (FB1) was evaluated in in vitro assays. The digestion of nutrients from maize contaminated with FB1 was assessed as well as the influence of digestive enzymes and pH on the bioavailability of FB1 in solution. Adsorption assays in buffers containing 5 µg/ml of FB1 were conducted to determine the strain to be used in the in vitro digestion assays. Four different yeast strains (1, 2, 3 and 4) along with five different cell concentrations of each one were studied under pH 2 and 6.8 at 39 °C. Strain 4 showed higher adsorption values at 1×109 cfu/ml, adsorbing 39.4% of the mycotoxin at pH 2 and 37.5% at pH 6.8. After that, the in vitro enzymatic digestion was conducted in two separated experiments. First, maize artificially contaminated with FB1 (5 µg/g) was used in five different treatments. Then, assays with maize naturally contaminated with FB1 (Maize A: 3.2 µg/g and Maize B: 29.0 µg/g) were conducted. In all samples, FB1 was quantified by HPLC-FL in liquid fraction and in solid residue. Samples of maize in natura and solid residues were subjected to chemical analysis of dry matter, organic matter, crude protein, neutral detergent fibre and starch to estimate the digestion of nutrients. The presences of FB1 and S. cerevisiae (Strain 4) in these assays had no influence on the digestion of the maize nutrients. The adsorption capacity of yeast was observed more clearly in treatments with higher concentrations of FB1 in the maize grain. S. cerevisiae strain 4 removed between 8 to 18% of FB1 in solution, showing a limited capacity to adsorb FB1 under in vitro conditions of horse enzymatic digestion.

scholarly journals Assessment of In Vitro Bioaccessibility of Polyphenols from Annurca, Limoncella, Red Delicious, and Golden Delicious Apples Using a Sequential Enzymatic Digestion Model

Antioxidants ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 541
Author(s):  
Giulia Graziani ◽  
Anna Gaspari ◽  
Claudio Di Vaio ◽  
Aurora Cirillo ◽  
Carolina Liana Ronca ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Antioxidant Activities ◽  
In Vitro Digestion ◽  
Enzymatic Digestion ◽  
Beneficial Effects ◽  
Golden Delicious ◽  
In Vitro Bioaccessibility ◽  
Inflammatory Processes ◽  
Great Relevance

Four different varieties of apples have been considered (Limoncella, Annurca, Red Delicious, and Golden Delicious) to estimate the extent of colon polyphenolics release after in vitro sequential enzyme digestion. Since several studies report a positive effect of apple polyphenols in colonic damage, we found of interest to investigate the colon release of polyphenols in different varieties of apples in order to assess their prevention of colonic damage. UHPLC-HRMS analysis and antioxidant activity (ABTS, DPPH, and FRAP assays) were carried out on the apple extracts (peel, flesh, and whole fruit) obtained from not digested samples and on bioaccessible fractions (duodenal and colon bioaccessible fractions) after in vitro digestion. Polyphenolic content and antioxidant activities were found to vary significantly among the tested cultivars with Limoncella showing the highest polyphenol content accompanied by an excellent antioxidant activity in both flesh and whole fruit. The overall trend of soluble antioxidant capacity from the soluble duodenal phase (SDP) and soluble colonic phase (SCP) followed the concentrations of flavanols, procyandinis, and hydroxycinnamic acids under the same digestive steps. Our results highlighted that on average 64.2% of the total soluble antioxidant activity was released in the SCP with Limoncella exhibiting the highest values (82.31, 70.05, and 65.5%, respectively for whole fruit, flesh, and peel). This result suggested that enzymatic treatment with pronase E and viscozyme L, to reproduce biochemical conditions occurring in the colon, is effective for breaking the dietary fiber-polyphenols interactions and for the release of polyphenols which can exercise their beneficial effects in the colon. The beneficial effects related to the Limoncella consumption could thus be of potential great relevance to counteract the adverse effects of pro-oxidant and inflammatory processes on intestinal cells.

scholarly journals The immunosuppressant SR 31747 blocks cell proliferation by inhibiting a steroid isomerase in Saccharomyces cerevisiae.

1996 ◽  
Vol 16 (6) ◽  
pp. 2719-2727 ◽  
Author(s):  
S Silve ◽  
P Leplatois ◽  
A Josse ◽  
P H Dupuy ◽  
C Lanau ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Proliferation ◽  
Gene Product ◽  
In Vitro Assays ◽  
Gene Products ◽  
Yeast Saccharomyces Cerevisiae ◽  
Isomerase Activity ◽  
Encoding Gene ◽  
Resistant Mutants

SR 31747 is a novel immunosuppressant agent that arrests cell proliferation in the yeast Saccharomyces cerevisiae, SR 31747-treated cells accumulate the same aberrant sterols as those found in a mutant impaired in delta 8- delta 7-sterol isomerase. Sterol isomerase activity is also inhibited by SR 31747 in in vitro assays. Overexpression of the sterol isomerase-encoding gene, ERG2, confers enhanced SR resistance. Cells growing anaerobically on ergosterol-containing medium are not sensitive to SR. Disruption of the sterol isomerase-encoding gene is lethal in cells growing in the absence of exogenous ergosterol, except in SR-resistant mutants lacking either the SUR4 or the FEN1 gene product. The results suggest that sterol isomerase is the target of SR 31747 and that both the SUR4 and FEN1 gene products are required to mediate the proliferation arrest induced by ergosterol depletion.

scholarly journals Energy values and protein digestibility of soybean milk by-product in pigs based on in vitro assays

2020 ◽  
Vol 34 (1) ◽  
pp. 73-81
Author(s):  
Jung Yeol Sung ◽  
Bokyung Hong ◽  
Youngeun Song ◽  
Beob Gyun Kim
Keyword(s):  
Protein Content ◽  
Crude Protein ◽  
Protein Digestibility ◽  
Metabolizable Energy ◽  
In Vitro Assays ◽  
Feed Ingredient ◽  
Soybean Milk ◽  
Gross Energy ◽  
Swine Diets

Background: Soybean milk by-product (SMBP) is a potential alternative feed ingredient in swine diets due to its high protein content. However, information on energy and nutritional values of SMBP used as swine feed ingredient is limited. Objective: To estimate energy values and protein digestibility of SMBP in pigs based on in vitro assays. Methods: Four SMBP samples were obtained from 3 soybean milk-producing facilities. In vitro total tract disappearance (IVTTD) and in vitro ileal disappearance (IVID) of dry matter (DM) in the SMBP samples were determined. In vitro ileal disappearance of crude protein was determined by analyzing crude protein content in undigested residues after determining IVID of DM. Digestible and metabolizable energy of SMBP were estimated using gross energy, IVTTD of DM, and prediction equations. Results: Sample 4 had greater IVTTD of DM than that of sample 3 (97.7 vs. 94.4%, p<0.05), whereas IVID of DM in sample 4 was lower compared with sample 1 (53.5 vs. 65.0%, p<0.05). In vitro ileal disappearance of crude protein in sample 2 was greater than that in sample 1 and 3 (92.6 vs. 90.6 and 90.1%; p<0.05). The estimated metabolizable energy of SMBP ranged from 4,311 to 4,619 kcal/kg as-is basis and the value of sample 3 was the least (p<0.05) among SMBP samples. Conclusion: Energy values and protein digestibility should be determined before using SMBP in swine diets.

Chapter 8 In Vitro Assays for Studying Saccharomyces cerevisiae Kinetochore Activity

1998 ◽  
pp. 145-153 ◽  
Author(s):  
Fedor Severin ◽  
Ken Kaplan ◽  
Peter Sorger ◽  
Tony Hyman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
In Vitro Assays

scholarly journals Starch Digestion Enhances Bioaccessibility of Anti-Inflammatory Polyphenols from Borlotti Beans (Phaseolus vulgaris)

Nutrients ◽  
2020 ◽  
Vol 12 (2) ◽  
pp. 295
Author(s):  
Perez-Hernandez ◽  
Nugraheni ◽  
Benohoud ◽  
Sun ◽  
Hernández-Álvarez ◽  
...  
Keyword(s):  
Phaseolus Vulgaris ◽  
Cell Model ◽  
In Vitro Digestion ◽  
Enzymatic Digestion ◽  
Mrna Levels ◽  
Starch Digestion ◽  
Granule Structure ◽  
Domestic Processing ◽  
Anti Inflammatory

The consumption of beans has been associated with chronic disease prevention which may be attributed to the polyphenols present in the seed coat and endosperm. However, their bioaccessibility is likely to be limited by interactions with bean matrix components, including starch, protein and fibre. The aim of this project was to evaluate the effect of domestic processing and enzymatic digestion on the bioaccessibility of polyphenols from Borlotti beans (Phaseolus vulgaris) and to test their anti-inflammatory properties in a macrophage cell model. In vitro digestion of cooked beans released twenty times more polyphenols (40.4 ± 2.5 mg gallic acid equivalents (GAE)/g) than domestic processing (2.22 ± 0.1 mg GAE/g), with starch digestion contributing to the highest release (30.9 ± 0.75 mg GAE/g). Fluorescence microscopy visualization of isolated bean starch suggests that polyphenols are embedded within the granule structure. LC-MS analysis showed that cooked Borlotti bean contain flavonoids, flavones and hydroxycinnamic acids, and cooked bean extracts exerted moderate anti-inflammatory effects by decreasing mRNA levels of IL1β and iNOS by 25% and 40%, respectively. In conclusion, the bioaccessibility of bean polyphenols is strongly enhanced by starch digestion. These polyphenols may contribute to the health benefits associated with bean consumption.

scholarly journals Mutational and in vitro protein-binding studies on centromere DNA from Saccharomyces cerevisiae.

1987 ◽  
Vol 7 (12) ◽  
pp. 4522-4534 ◽  
Author(s):  
R Ng ◽  
J Carbon
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Binding ◽  
In Vitro Assays ◽  
Binding Studies ◽  
Mobility Shift ◽  
Sequence Element ◽  
Sequence Elements ◽  
Mobility Shift Assay

Centromeres on chromosomes in the yeast Saccharomyces cerevisiae contain approximately 140 base pairs (bp) of DNA. The functional centromere (CEN) region contains three important sequence elements (I, PuTCACPuTG; II, 78 to 86 bp of high-AT DNA; and III, a conserved 25-bp sequence with internal bilateral symmetry). Various point mutations or deletions in the element III region have a profound effect on CEN function in vivo, indicating that this DNA region is a key protein-binding site. This has been confirmed by the use of two in vitro assays to detect binding of yeast proteins to DNA fragments containing wild-type or mutationally altered CEN3 sequences. An exonuclease III protection assay was used to demonstrate specific binding of proteins to the element III region of CEN3. In addition, a gel DNA fragment mobility shift assay was used to characterize the binding reaction parameters. Sequence element III mutations that inactivate CEN function in vivo also prevent binding of proteins in the in vitro assays. The mobility shift assay indicates that double-stranded DNAs containing sequence element III efficiently bind proteins in the absence of sequence elements I and II, although the latter sequences are essential for optimal CEN function in vivo.

Mutational and in vitro protein-binding studies on centromere DNA from Saccharomyces cerevisiae

1987 ◽  
Vol 7 (12) ◽  
pp. 4522-4534
Author(s):  
R Ng ◽  
J Carbon
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Binding ◽  
In Vitro Assays ◽  
Binding Studies ◽  
Mobility Shift ◽  
Sequence Element ◽  
Sequence Elements ◽  
Mobility Shift Assay

Centromeres on chromosomes in the yeast Saccharomyces cerevisiae contain approximately 140 base pairs (bp) of DNA. The functional centromere (CEN) region contains three important sequence elements (I, PuTCACPuTG; II, 78 to 86 bp of high-AT DNA; and III, a conserved 25-bp sequence with internal bilateral symmetry). Various point mutations or deletions in the element III region have a profound effect on CEN function in vivo, indicating that this DNA region is a key protein-binding site. This has been confirmed by the use of two in vitro assays to detect binding of yeast proteins to DNA fragments containing wild-type or mutationally altered CEN3 sequences. An exonuclease III protection assay was used to demonstrate specific binding of proteins to the element III region of CEN3. In addition, a gel DNA fragment mobility shift assay was used to characterize the binding reaction parameters. Sequence element III mutations that inactivate CEN function in vivo also prevent binding of proteins in the in vitro assays. The mobility shift assay indicates that double-stranded DNAs containing sequence element III efficiently bind proteins in the absence of sequence elements I and II, although the latter sequences are essential for optimal CEN function in vivo.

scholarly journals Determination of the amount of bioaccessible fumonisin B1 in different matrices after in vitro digestion

2015 ◽  
Vol 8 (3) ◽  
pp. 261-267 ◽  
Author(s):  
J. Szabó-Fodor ◽  
C. Dall'Asta ◽  
C. Falavigna ◽  
M. Kachlek ◽  
Á. Szécsi ◽  
...  
Keyword(s):  
Analytical Methods ◽  
Fusarium Verticillioides ◽  
Animal Experiments ◽  
Extraction Procedure ◽  
Fumonisin B1 ◽  
In Vitro Digestion ◽  
The Matrix ◽  
Pre Treatment

Conventional analytical methods used for the analysis of fumonisin content in animal feeds fail to take into account the fumonisin content bound to the matrix, which is otherwise bioaccessible and can be absorbed from the gastrointestinal tract. Moreover, underestimation of fumonisin content using routine analytical methods can affect animal experiments using cereals contaminated by fungi. In the present study, hidden fumonisin B1 was analysed in two cereal substrates (maize and wheat) which were inoculated with Fusarium verticillioides (MRC 826). The study compared a routine extraction procedure with an in vitro digestion sample pre-treatment. We found that all samples showed a higher content of fumonisin B1 after digestion, compared to the free fumonisin obtained only by extraction. The percentage of the hidden form was 38.6% (±18.5) in maize and 28.3% (±17.8) in wheat, expressed as the proportion of total fumonisin B1. These results indicate that the toxin exposure of the animals determined by the routine fumonisin analysis was underestimated, generally by 40%, as bioaccessibility was not taken into consideration. This is crucial in interpretation (and maybe in re-evaluation) of the results obtained from (other) animal experiments.

Sign in / Sign up

Export Citation Format

Share Document