scholarly journals Probiotics role of Saccharomyces cerevisiae and Bacillus subtilis in improving the health status of rabbits’ gastrointestinal tract

2021 ◽  
Vol 45 (1) ◽  
Author(s):  
Farouk Helal ◽  
Alaa El-Badawi ◽  
Soad El-Naggar ◽  
Mohamed Shourrap ◽  
Osama Aboelazab ◽  
...  

Abstract Background Probiotics are direct-fed microbial feed supplements which can modulate the gut microflora by competing intestinal pathogens through a competitive process. The present study was conducted to investigate the effect of feeding Saccharomyces cerevisiae, Bacillus subtilis or their mixture on blood biochemical constituents, intestinal pathogenic load and intestinal histological changes of growing New Zealand White (NZW) rabbits. Results Serum total protein, albumin, and globulin were (P ≤ 0.05) increased for rabbits fed supplemented diets. Microbial pathogenic load of small intestinal and caecal contents (E. coli and C. perfringens) showed reduction (P ≤ 0.05) for rabbits fed supplemented diets, while, lactobacillus spp. recorded higher counts (P ≤ 0.05) in intestinal and caecal contents of rabbits fed probiotics supplemented diets than control group. Small intestine length, villus height and crypt depth were higher (P ≤ 0.05) with probiotic diets than control. Musculosa depth was depressed (P ≤ 0.05) with probiotic diets. Conclusions It could be concluded that the addition of Bacillus subtilis or Saccharomyces cerevisiae to diets of growing NZW rabbits by 0.1% is recommended to minimize the pathogenic intestinal load and increasing of beneficial lactobacillus strains as well as improving the intestinal barriers integrity.

Author(s):  
Hassan Ghorbani-Choboghlo ◽  
Donya Nikaein ◽  
Ali-Reza Khosravi ◽  
Reza Rahmani ◽  
Zohreh Farahnejad

ABSTRACT     Background and Objectives: Probiotics are live microorganisms that, when administered in an adequate amount, confer a health benefit on the host through the gut. Saccharomyces cerevisiae is a widespread yeast found in nature. This microor- ganism has been used as a probiotic agent in recent years. In this study, the effect of microencapsulation on survival rate of S. cerevisiae var. boulardii in the simulated gastrointestinal tract medium and the impact of microencapsulated S. cerevisiae var. boulardii on some serum biochemical factors in a rat model was evaluated. Materials and Methods: 30 male wistar rats were divided into three groups (control, rats receiving microencapsulated S. cerevisiae var. boulardii, and rats receiving S. cerevisiae var. boulardii alone). The probiotic was gavaged at a dosage of 2 gr/ kg BW for 8 weeks. Blood was collected from rats at the end of the treatment period and biochemical factors were measured using Mancompany kits. Results: The results showed a significant increase in viability of microencapsulated S. cerevisiae var. boulardii in compar- ison with free S. cerevisiae var. boulardii (p<0.05). Weight of rats in probiotic treated groups was significantly higher in comparison with the control group (p<0.05). Moreover, probiotic treatment reduced mean levels of triglycerides, cholesterol, free blood sugar and liver enzymes in rats. Conclusion: Microencapsulation could increase the survival rate of yeast probiotics in the gastrointestinal tract; however, more studies are needed for better understanding of the exact effect of microencapsulation on probiotics’ function.


2021 ◽  
Vol 77 (3) ◽  
pp. 76-82
Author(s):  
Galyna Fadieienko ◽  
Oleksiy Gridnyev ◽  
Inna Kushnir

Objective — to study the features of endotoxinemia and its relationship with changes in the intestinal microbial spectrum in obese patients with non-alcoholic fatty liver disease (NAFLD). Materials and methods. 84 patients with obesity and NAFLD were examined. The control group consisted of 20 apparently healthy individuals. The concentration of endotoxin (ET) in the blood serum was determined using the LAL Chromogenic Endpoint Assay kit manufactured by Hycult Biotech (Netherlands), relative quantitative composition of the microbiota at the level of basic phylotypes — by real-time polymerase chain reaction (CFX96Touch (Bio-Rad, USA)) using universal primers for the 16SpPHK gene and taxon-specific primers), quantitative composition of microbiota — using test of the «Colonoflor-16» system (Alfalab, RF) by real-time polymerase chain reaction.Results. Among patients with comorbidity of obesity and NAFLD, there were 40.48 % of males and 59.52 % of females, whose mean age was 53.72 ± 4.61 years. The ET level in the examined patients with comorbidity of obesity and NAFLC was significantly (p < 0.001) higher (1.01 ET/ml) than in the control group (0.60 ET/ml), was significantly (p < 0,05) is higher in women than in men (1.06 and 0.92 UE/ml, respectively) and increased with increasing age of patients (r = 0.30, p < 0.05). The ET level correlated with the relative content of Firmicutes (r = 0.39, p < 0.05) and their ratio in Bacteroidetes (r = 0.29, p < 0.05) and the level of Bifidobacterium spp. (r = 0 .37, p < 0 .05) a nd h ad a n i nverse r elationship w ith t he r elative c ontent o f B acteroidetes ( r = – 0.42, p < 0.01), including Bacteroides fragilis group (r = – 0.43, p < 0.01), Escherichia coli (r = – 0.41, p < 0.01) and total bacterial mass (r = – 0.39, p < 0.05). In the intestinal microbiota of the examined patients, a decrease in the representatives of the Lactobacillus spp. and Bifidobacterium spp. in 84.5 % and 30.9 % of patients, respectively, as well as Bacteroides thetaiotaomicron (88.0 %), Akkermansia muciniphila (79.8 %) and Faecalibacteriumprausnitzii (33.3 %). Whereas the number of gram-negative bacteria increased primarily due to Enterobacter spp, Citrobacter spp (45.2 %), Escherichia coli (19 %), Bacteroides fragilis group (29.8 %). It should be noted that the decrease in the level of A. muciniphila was often accompanied by an increase in the content of enterobacteria, while the excess content of B. fragilis group was accompanied by an increase above the upper limit of E. coli and the presence of anaerobic imbalance in the microbiota. In turn, increasing the number of Enterobacter spp. / Citrobacter spp. It was often accompanied by an increase in the content of E. coli and representatives of the B. fragilis group, against the background of a reduced number of A. muciniphila. Conclusions. The above indicates the presence of metabolic endotoxinemia in patients with comorbidity of obesity and NAFLD against the background of a decrease in the number of gram-positive anaerobic Lactobacillus spp. i Bifidobacterium spp. and bacteria involved in providing the intestinal barrier function (Bacteroides Thetaiotaomicron, Akkermansia muciniphila, Faecalibacterium prausnitzii), which creates conditions for an increased amount of ET into the blood and is especially important against the background of an increase in the content of gram-negative bacteria (representatives of gammaproteobacteria and bacteria of the Bacteroides fragilis), which are the source of ET.


1992 ◽  
Vol 55 (9) ◽  
pp. 739-740 ◽  
Author(s):  
HUSSEIN YOUSSEF ◽  
ABDEL KHALIK EL-TIMAWY ◽  
SHABAN AHMED

A total of 101 fresh water fish Tilapia nilotica were bacteriologically investigated for pathogenic and potentially pathogenic organisms. True intestinal pathogens were obtained in 11.8% of the examined specimens including 7.9% with enteropathogenic Escherichia coli and 3.9% with Salmonella species. Serological typing of Salmonella (4 strains) revealed the detection of Salmonella typhimurium (1 strain), S. wangata (2 strains), and S. newport (1 strain). Other potentially pathogenic organisms were isolated in considerable frequencies, Proteus spp. (43.5%) atypable E. coli (13.8%), Micrococcus spp. (11.8%) and Providencia (9.9%). Vibrio parahaemolyticus and Staphylococci were not detected in the examined samples.


1999 ◽  
Vol 338 (3) ◽  
pp. 701-708 ◽  
Author(s):  
Evelyne RAUX ◽  
Treasa McVEIGH ◽  
Sarah E. PETERS ◽  
Thomas LEUSTEK ◽  
Martin J. WARREN

MET1 and MET8 mutants of Saccharomyces cerevisiae can be complemented by Salmonella typhimurium cysG, indicating that the genes are involved in the transformation of uroporphyrinogen III into sirohaem. In the present study, we have demonstrated complementation of defined cysG mutants of Sal. typhimurium and Escherichia coli, with either MET1 or MET8 cloned in tandem with Pseudomonas denitrificans cobA. The conclusion drawn from these experiments is that MET1 encodes the S-adenosyl-l-methionine uroporphyrinogen III transmethylase activity, and MET8 encodes the dehydrogenase and chelatase activities (all three functions are encoded by Sal. typhimurium and E. coli cysG). MET8 was further cloned into pET14b to allow expression of the protein with an N-terminal His-tag. After purification, the functions of the His-tagged Met8p were studied in vitro by assay with precorrin-2 in the presence of NAD+ and Co2+. The results demonstrated that Met8p acts as a dehydrogenase and chelatase in the biosynthesis of sirohaem. Moreover, despite the fact that S. cerevisiae does not make cobalamins de novo, we have shown also that MET8 is able to complement cobalamin cobaltochelatase mutants and have revealed a subtle difference in the early stages of the anaerobic cobalamin biosynthetic pathways between Sal. typhimurium and Bacillus megaterium.


2000 ◽  
Vol 348 (2) ◽  
pp. 367-373 ◽  
Author(s):  
Jörg P. MÜLLER ◽  
Jörg OZEGOWSKI ◽  
Stefan VETTERMANN ◽  
Jelto SWAVING ◽  
Karel H. M. VAN WELY ◽  
...  

CsaA from the Gram-positive bacterium Bacillus subtilis has been identified previously as a suppressor of the growth and protein-export defect of Escherichia coli secA(Ts) mutants. CsaA has chaperone-like activities in vivo and in vitro. To examine the role of CsaA in protein export in B. subtilis, expression of the csaA gene was repressed. While export of most proteins remained unaffected, export of at least two proteins was significantly reduced upon CsaA depletion. CsaA co-immunoprecipitates and co-purifies with the SecA proteins of E. coli and B. subtilis, and binds the B. subtilis preprotein prePhoB. Purified CsaA stimulates the translocation of prePhoB into E. coli membrane vesicles bearing the B. subtilis translocase, whereas it interferes with the SecB-mediated translocation of proOmpA into membrane vesicles of E. coli. The specific interaction with the SecA translocation ATPase and preproteins suggests that CsaA acts as a chaperone that promotes the export of a subset of preproteins in B. subtilis.


2020 ◽  
Vol 33 (3) ◽  
pp. 456-464
Author(s):  
Qi Zhang ◽  
Yuchen Jie ◽  
Chuli Zhou ◽  
Leyun Wang ◽  
Liang Huang ◽  
...  

Objective: The aim of this study is to investigate the effect of oral spray with probiotics on the intestinal development and microflora colonization of hatched ducklings.Methods: In Exp. 1, an one-way factorial design was used to study the antibacterial activity of the probiotics and metabolites on Escherichia coli (E. coli) without antimicrobial resistance. There were four experimental groups including saline as control and Lactobacillus, Bacillus subtilis, combined Lactobacillus and Bacillus subtilis groups. In Exp. 2, 64-day-old ducklings were allotted to 2 treatments with 4 replicated pens. Birds in the control group were fed a basal diet supplemented with Lactobacillus fermentation in the feed whereas birds in the oral spray group were fed the basal diet and administrated Lactobacillus fermentation by oral spray way during the first week.Results: In Exp. 1, the antibacterial activities of probiotics and metabolites on E. coli were determined by the diameter of inhibition zone in order: Lactobacillus>combined Lactobacillusand Bacillus subtilis>Bacillus subtilis. Additionally, compared to E. coli without resistance, E. coli with resistance showed a smaller diameter of inhibition zones. In Exp. 2, compared to control feeding group, oral spray group increased (p<0.05) the final body weight at d 21 and average daily gain for d 1-21 and the absolute weight of the jejunum, ileum and total intestine tract as well as cecum Lactobacillus amount at d 21.Conclusion: Lactobacillus exhibited a lower antibacterial activity on E. coli with resistance than E. coli without resistance. Oral spray with Lactobacillus fermentation during the first week of could improve the intestinal development, morphological structure, and microbial balance to promote growth performance of ducklings from hatch to 21 d of age.


2020 ◽  
Vol 44 ((E0)) ◽  
pp. 14-20
Author(s):  
Aamir M. Al-ghareebaw

This study aimed to investigate the protective influence of olive leave extract zinc oxidenanoparticles (OLEZnONPs) complex against gentamicin–induced kidney dysfunctions ingoats. Twenty five adult female goats were randomly divided into five equal groups andtreated as follows: control group (C) administered sterile distilled water (IM) for 10 days,group G administered 25 mg/kg BW gentamicin (IM) for 7 days, group Z administered 10μg/kg BW of OLEZnONPs (IP) for 3 days, group GTZ administered 25 mg/kg BW gentamicin(IM) for 7 days and then 10 μg/kg BW of OLEZnONPs (IP) for 3 days, group GWZadministered 25 mg/kg BW gentamicin (IM) and 10 μg/kg BW of OLEZnONPs (IP) togetherfor first 3 days and then followed by gentamicin only for 4 days. After seven days of theexperiment, the gene expression of kidney injury molcule-1(KIM-1) and neutrophilgelatinase-association lipocalin (NGAL) gene expression of kidney tissue were measured. Inaddition, samples of kidney were obtained for histopathological examination. Gentamicinmedication induced a marked elevation in kidney tissue KIM-1 and NGAL gene expressionin G and GTZ groups compared to control and other groups. Intraperitoneal treatment ofgoats with OLEZnONPs did not significantly affect NGAL and KIM-1 gene expression in Z,GWZ, and control groups. Histologically, in contrast to control, gentamicin induced moreextensive kidney damages such as necrotized glomeruli, atrophic glomeruli, and renaltubular epithelial necrosis, while it was found that these alterations in kidney tissues wereimproved in goats given OLEZnONPs with gentamicin compared to group G. In conclusion,our results demonstrate that OLEZnONPs reduce the deleterious effects of gentamicin withsignificantly decreasing of KIM-1 and NGAL gene expression and remodeling the histologicalchanges of kidney in goats


1986 ◽  
Vol 6 (12) ◽  
pp. 4509-4515
Author(s):  
M Rosenkrantz ◽  
T Alam ◽  
K S Kim ◽  
B J Clark ◽  
P A Srere ◽  
...  

Saccharomyces cerevisiae contains two genes, CIT1 and CIT2, encoding functional citrate synthase (K.-S. Kim, M. S. Rosenkrantz, and L. Guarente, Mol. Cell. Biol. 6:1936-1942, 1986). We show here that CIT2 encodes a nonmitochondrial form of citrate synthase. The DNA sequence of CIT2 presented provides a possible explanation for why the CIT2 product, unlike the CIT1 product, fails to be imported into mitochondria. While the products of these two genes are highly homologous, they diverge strikingly at their amino termini. The amino terminus of the CIT1 primary translation product extends 39 residues beyond the amino termini of Escherichia coli and porcine citrate synthases. This extension consists of a typical mitochondrial targeting motif. The amino terminus of the CIT2 primary translation product extends 20 residues beyond the amino termini of the E. coli and porcine enzymes. The CIT2-encoded extension is not homologous to that of CIT1, resulting in a nonmitochondrial localization of the product. The CIT2-encoded extension, however, does bear certain similarities to mitochondrial targeting sequences. The possible role of this sequence in targeting this CIT2 product to a nonmitochondrial organelle is discussed.


2001 ◽  
Vol 276 (15) ◽  
pp. 11499-11506 ◽  
Author(s):  
Simone Heimpel ◽  
Gabriele Basset ◽  
Sabine Odoy ◽  
Martin Klingenberg

Previously, the role of residues in the ADP/ATP carrier (AAC) fromSaccharomyces cerevisiaehas been studied by mutagenesis, but the dependence of mitochondrial biogenesis on functional AAC impedes segregation of the mutational effects on transport and biogenesis. Unlike other mitochondrial carriers, expression of the AAC from yeast or mammalians inEscherichia coliencountered difficulties because of disparate codon usage. Here we introduce the AAC fromNeurospora crassainE. coli, where it is accumulated in inclusion bodies and establish the reconstitution conditions. AAC expressed with heat shock vector gave higher activity than with pET-3a. Transport activity was absolutely dependent on cardiolipin. The 10 single mutations of intrahelical positive residues and of the matrix repeat (+X+) motif resulted in lower activity, except of R245A. R143A had decreased sensitivity toward carboxyatractylate. The ATP-linked exchange is generally more affected than ADP exchange. This reflects a charge network that propagates positive charge defects to ATP4−more strongly than to ADP3−transport. Comparison to the homologous mutants of yeast AAC2 permits attribution of the roles of these residues more to ADP/ATP transport or to AAC import into mitochondria.


1986 ◽  
Vol 6 (12) ◽  
pp. 4509-4515 ◽  
Author(s):  
M Rosenkrantz ◽  
T Alam ◽  
K S Kim ◽  
B J Clark ◽  
P A Srere ◽  
...  

Saccharomyces cerevisiae contains two genes, CIT1 and CIT2, encoding functional citrate synthase (K.-S. Kim, M. S. Rosenkrantz, and L. Guarente, Mol. Cell. Biol. 6:1936-1942, 1986). We show here that CIT2 encodes a nonmitochondrial form of citrate synthase. The DNA sequence of CIT2 presented provides a possible explanation for why the CIT2 product, unlike the CIT1 product, fails to be imported into mitochondria. While the products of these two genes are highly homologous, they diverge strikingly at their amino termini. The amino terminus of the CIT1 primary translation product extends 39 residues beyond the amino termini of Escherichia coli and porcine citrate synthases. This extension consists of a typical mitochondrial targeting motif. The amino terminus of the CIT2 primary translation product extends 20 residues beyond the amino termini of the E. coli and porcine enzymes. The CIT2-encoded extension is not homologous to that of CIT1, resulting in a nonmitochondrial localization of the product. The CIT2-encoded extension, however, does bear certain similarities to mitochondrial targeting sequences. The possible role of this sequence in targeting this CIT2 product to a nonmitochondrial organelle is discussed.


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