scholarly journals Antimicrobial Power of Organic Acids and Nature-Identical Compounds against Two Vibrio spp.: An In Vitro Study

2021 ◽  
Vol 9 (5) ◽  
pp. 966
Author(s):  
Barbara Rossi ◽  
Maria Angéles Esteban ◽  
José María García-Beltran ◽  
Giulia Giovagnoni ◽  
Alberto Cuesta ◽  
...  

Vibrosis is one of the major threats in aquaculture farming, and due to the increasing antimicrobial resistance of different Vibrio species, there is an urgent need to replace conventional treatments with more sustainable solutions. Antimicrobial molecules such as organic acids (OA) and nature-identical compounds (NIC) are currently finding a central role in the infection management of terrestrial livestock, but little is known about their usage in aquaculture. The aim of this study was to perform a preliminary screening of the in vitro antimicrobial activity of a wide panel of OA and NIC against 2 Vibrio species characteristic of the Mediterranean area, Vibrio harveyi and Vibrio anguillarum, through minimal inhibitory/bactericidal concentration tests. The active principles that showed the best effective pathogen control were medium-chain fatty acids, sorbic and benzoic acid among OA and phenolic monoterpenoids (thymol, carvacrol and eugenol) and aromatic monoterpene aldehydes (vanillin and cinnamaldehyde) among NIC. These results showed how the usage of OA and NIC can open promising perspectives in terms of Vibrio spp. load control in aquaculture. Natural or nature-identical feed additives can make aquaculture production not only more efficient by reducing the need for medicated treatments, but also more sustainable.

2002 ◽  
Vol 81 (5) ◽  
pp. 621-628 ◽  
Author(s):  
P Chaveerach ◽  
D.A. Keuzenkamp ◽  
H.A. Urlings ◽  
L.J. Lipman ◽  
F van Knapen

2021 ◽  
Vol 104 (3) ◽  
pp. 36-46
Author(s):  
Vitaly A Ryazanov ◽  
◽  
Georgy I Levakhin ◽  
Galimzhan K Duskaev ◽  
Elena V Sheyda ◽  
...  

Biology ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 1055
Author(s):  
Aurele Gnetegha Ayemele ◽  
Lu Ma ◽  
Xiumei Li ◽  
Peilong Yang ◽  
Jianchu Xu ◽  
...  

Rumen protozoa prey on feed-degrading bacteria synthesizing microbial protein, lowering nitrogen utilization efficiency in ruminants. In this in vitro study, we evaluated six plants (Adansonia digitata, Flemingia macrophylla, Kalimeris indica,Brassica rapa subsp. chinensis, Portulaca oleracea, and Calotropis gigantea) for their potential to inhibit rumen protozoa and identified the phytochemicals potentially responsible for protozoa inhibition. Rumen protozoa were anaerobically cultured in vitro in the presence of each plant at four doses. All of the tested plants reduced total rumen protozoa (p ≤ 0.05), but C. gigantea and B. rapa were the most inhibitory, inhibiting rumen protozoa by 45.6 and 65.7%, respectively, at the dose of 1.1 mg/mL. Scanning electron microscopy revealed a disruption of the extracellular structure of protozoa cells. Only C. gigantea also decreased the wasteful ammoniagenesis (p ≤ 0.05). Moreover, the A. digitata extract inhibited α-glucosidase activity by about 70% at 100 µg/mL. Reversed-phase high-performance liquid chromatography analysis detected quercetin, anthraquinone, 3-hydroxybenzoic acid, astragaloside, and myricetin in the tested plant leaves. These plants may hold potential as feed additives to reduce rumen protozoa and α- glucosidase activity. Future research is needed to identify the specific anti-protozoal compound(s), the effects on the rumen microbiome, and its fermentation characteristics.


2020 ◽  
Vol 4 (3) ◽  
Author(s):  
Youngji Rho ◽  
Rob Patterson ◽  
Iris Joye ◽  
Mario Martinez ◽  
E James Squires ◽  
...  

Abstract Treating fibrous feed ingredients with exogenous feed enzymes may improve their utilization in monogastric animals. An in vitro study was conducted to determine the effects of steeping corn distillers dried grains with solubles (DDGS) or wheat middlings (WM) with exogenous feed enzymes. Four treatments were arranged as follows: 1) co-product steeped with water (CON), 2) CON plus 0.5-g fiber degrading enzymes (FDE), 3) CON plus 0.5-g protease (PRO), and 4) CON plus 0.5-g FDE and 0.5 g PRO (FDEPRO). The FDE contained about 62,000, 37,000, and 8,000 U/g of xylanase, cellulase, and β-glucanase, respectively, whereas activities in PRO amounted to 2,500,000, 1,300,000, and 800,000 U/g of acid, alkaline, and neutral proteases, respectively. Briefly, 50 g of DDGS or WM samples (n = 8) were mixed with 500-mL water with or without enzymes and steeped for 0 to 72 h at 37 °C with continuous agitation. The pH, concentration of monosaccharides, and organic acids in the supernatant and apparent disappearance (AD) of fiber in solids were measured at 0, 12, 24, 48, and 72 h. There was treatment and time interaction (P < 0.005) on monosaccharides concentration. At 12 h, arabinose and glucose concentrations were similar (P > 0.05) between FDE and FDEPRO but higher (P = 0.002) than for CON in DDGS. For WM, FDE, and FDEPRO had higher (P < 0.001) xylose concentration than CON and PRO, whereas glucose concentration was higher (P < 0.001) for enzymes than CON at 12 h. However, FDEPRO had higher (P < 0.001) xylose concentration than CON, whereas xylose concentration for FDE and PRO was intermediate at 24 h. There was an interaction (P < 0.05) between treatment and time effect on lactic acid concentration in DDGS and WM (P < 0.005), and acetic acid concentration in WM (P < 0.001). In general, monosaccharide concentration was higher between 12 and 24 h and decreased after 48 h, whereas the pH decreased, and concentration of organic acids increased continuously over time (P < 0.05). The AD of NDF and ADF in DDGS was greater (P = 0.001) for FDE and FDEPRO than CON and PRO at 72 h. In WM, enzymes increased (P = 0.007) AD of NDF relative to CON at 72 h. Nonetheless, greater (P < 0.05) AD of fiber was observed between 48 and 72 h. In conclusion, although there were differences in responses among co-products, fiber degrading enzymes increased release of fermentable monosaccharides from co-products at 12 to 24 h of steeping and these effects were not extended with the addition of protease.


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