scholarly journals Assessment of the Antimicrobial Potentiality and Functionality of Lactobacillus plantarum Strains Isolated from the Conventional Inner Mongolian Fermented Cheese Against Foodborne Pathogens

Pathogens ◽  
2019 ◽  
Vol 8 (2) ◽  
pp. 71 ◽  
Author(s):  
Zafarullah Muhammad ◽  
Rabia Ramzan ◽  
Amro Abdelazez ◽  
Adnan Amjad ◽  
Muhammad Afzaal ◽  
...  
Keyword(s):  
Organic Acids ◽  
Mixed Culture ◽  
Lactobacillus Plantarum ◽  
Foodborne Pathogens ◽  
Heat Stability ◽  
Control Agent ◽  
Partial Purification ◽  
Molecular Weight Range ◽  
Sds Page

Lactobacillus plantarum are amongst the diversified lactic acid bacteria (LAB) species which are being utilized abundantly in the food industry. Numerous L. plantarum strains have been reported to produce several antimicrobial compounds. Diacetyl, hydrogen peroxide, organic acids, as well as bacteriocins can also be exemplified by a variable spectrum of actions. The current study was intended to conduct the screening and characterization of antimicrobial prospective of L. plantarum from traditional Inner Mongolian fermented hard cheese. Foodborne pathogens, Salmonella typhimurium, Escherichia coli O157:H7, Listeria monocytogenes, and Staphylococcus aureus, were examined by using the Oxford cup technique and the mixed culture inhibition assays. The resulting analyses disclosed that L. plantarum KLDS1.0344 indicated broad antimicrobial spectrum against all selected pathogens as compared to other LAB used in this study. Additionally, the decrement of the pathogen population was observed up to 3.47 logs in mixed culture inhibition assays. L. plantarum KLDS 1.0344 acid production was recorded up to 71.8 ± 3.59 °D in mixed culture while antimicrobial particles released in cell free supernatants demonstrated bacteriocin-like characteristics showing substantial pH stability (2.0–6.0), proteolytic enzyme reduced the antibacterial activity (15.2 ± 0.6 mm–20.4 ± 0.8 mm), heat stability (20 min at 120 °C) against selected pathogens. Moreover, the spectrum range of antimicrobial peptides after the partial purification was decreased as compared to the crude bacteriocin-like compound. The SDS-PAGE analysis showed the molecular weight range of partially purified bacteriocin from 12 to 45 kDa. After analyzing the obtained data from the current experimentation showed that the capability of L. plantarum KLDS 1.0344 to oppose the pathogen growth in vitro relies on the occurrence of organic acids along with bacteriocin-like compounds proving L. plantarum KLDS 1.0344 as a potentially appropriate candidate as an alternative bio-control agent against foodborne pathogens.

scholarly journals CLONING, EXPRESSION, AND PARTIAL PURIFICATION OF PLANTARICIN W LOCUS PRODUCED BY Lactobacillus plantarum S34

2017 ◽  
Vol 16 (1) ◽  
Author(s):  
Rifqiyah Nur Umami ◽  
Apon Zaenal Mustopa ◽  
Linda Sukmarini ◽  
Hasim Danuri ◽  
Andini Setyanti Putri ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Western Blot ◽  
Lactobacillus Plantarum ◽  
Partial Purification ◽  
E Coli ◽  
Sds Page

Lactobacillus plantarum S34 dilaporkan mempunyai aktivitas antibakteri yang terkait dengan produksi bakteriosin. Bagian dari gen yang menyandikan salah satu lokus bakteriosin yang diproduksi oleh L. plantarum S34, disebut dengan plantarisin W (plnW), diamplifikasi dari plasmid dan dikloning menggunakan sistem vektor pGEM®-T Easy ke dalam Escherichia coli DH5?. Sekuens nukleotida plnW (± 405 pb) diidentifikasi sebagai protein integral membran. Lebih lanjut, plnW diekspresikan secara heterologus sebagai fusi protein dengan His(6)-tag tioredoksin menggunakan vektor ekspresi pET-32a(+) ke dalam E. coli BL21 (DE3) pLysS. Protein fusi rekombinan plnW terdapat dalam sitoplasma sel, tetapi selain fraksi terlarut terdapat juga fraksi tidak terlarut berupa badan inklusi. Purifikasi parsial dilakukan menggunakan kromatografi afinitas ligan Co2+ untuk fraksi terlarut dan metode elektroelusi gel poliakrilamid untuk fraksi tidak terlarut. Massa molekul berukuran kurang lebih 33 kDa terdeteksi berdasarkan pemisahan SDS-PAGE dan dikonfirmasi dengan Western blot sebagai protein fusi rekombinan plnW. Protein yang sudah terpurifikasi bermanfaat untuk mengetahui kaitan antara struktur dan fungsi bakteriosin.

Partial purification and characterization ofGigantocotyle explanatumsomatic antigens

2004 ◽  
Vol 78 (2) ◽  
pp. 95-99 ◽  
Author(s):  
G. Ahmad ◽  
M.K. Saifullah ◽  
W.A. Nizami
Keyword(s):  
Molecular Weight ◽  
Western Blotting ◽  
Bubalus Bubalis ◽  
Partial Purification ◽  
Low Molecular Weight ◽  
Purification And Characterization ◽  
Molecular Weight Range ◽  
Weight Range ◽  
Sds Page

AbstractSoluble extracts ofGigantocotyle explanatum, isolated from the liver of buffaloBubalus bubaliswere fractionated on Sephadex G-200 columns. Nine major fractions referred to as F1, F2, F3, F4, F5, F6, F7, F8 and F9 were separated. Each fraction was tested by ELISA for antigenicity using sera fromG. explanatum-infected field buffaloes. Fractions F1 and F2 were highly antigenic, F3, F4, F6 and F7 were moderately antigenic and F5, F8 and F9 were poorly antigenic. Analyses by SDS–PAGE revealed that each fraction comprised several polypeptide(s) in the molecular weight range of <29 to >205 kDa. Results of Western blotting indicated that not all polypeptides which appeared in the SDS–PAGE were antigenic. The antigenic molecules of each fraction were mostly in the low molecular weight range of <14 to >94 kDa with the polypeptides in the range of >14, 14, 18, 21–25 and 34–36 kDa.

scholarly journals Inhibitory Effect of Lactobacillus plantarum FL75 and Leuconostoc mesenteroides FL14 against Foodborne Pathogens in Artificially Contaminated Fermented Tomato Juices

2019 ◽  
Vol 2019 ◽  
pp. 1-11 ◽  
Author(s):  
Aïssé Bah ◽  
Helena Albano ◽  
Joana Bastos Barbosa ◽  
Imene Fhoula ◽  
Yosra Gharbi ◽  
...  
Keyword(s):  
Organic Acids ◽  
Lactobacillus Plantarum ◽  
Foodborne Pathogens ◽  
Pathogenic Bacteria ◽  
Leuconostoc Mesenteroides ◽  
Foodborne Pathogen ◽  
Inhibitory Effect ◽  
Hplc Method ◽  
Tomato Juice ◽  
High Survival

Tomatoes and tomato based-foods contain beneficial microorganisms and various organic acids that have important nutritional values for human. The objective of this study was to access the physiochemical properties of fermented tomatoes juices and to evaluate the competitiveness of lactic acid bacteria (LAB) against Listeria monocytogenes, Listeria innocua, and Salmonella spp., in artificially contaminated tomato juice. Microbial counting (LAB, fungi Salmonella spp., and Listeria spp.) was performed after fermentation and weekly during storage. Different organic acids (Lactic, succinic, and acetic) and ethanol were also monitored using HPLC method. Color parameters were also determined. The results showed an increase of lactic and acetic acid content, during fermentation and storage of juices inoculated with Lactobacillus plantarum and Leuconostoc mesenteroides at 25°C. Besides, citric acid and ethanol revealed higher content at the end of storage compared to that registered at 4°C. The pH from tomatoes juices decreased from an initial value of 4.5 to below 3.2. Alongside, foodborne pathogen population was significantly suppressed in tomatoes juices when the samples were coinoculated with LAB strains. Moreover, the inhibition of Salmonella species was faster compared to that of Listeria. After four weeks of storage at 4°C, Lb. plantarum and Lc. mesenteroides showed high survival rate, while pathogenic bacteria, yeasts, and molds cell numbers decreased drastically in all the contaminated vials. This work highlights the efficiency of Lb. plantarum and Lc. mesenteroides as potential starters for developing nutritious and safe fermented tomato juice products.

The Anticoagulant Properties of a Modified Form of Protein S

1988 ◽  
Vol 60 (02) ◽  
pp. 298-304 ◽  
Author(s):  
C A Mitchell ◽  
S M Kelemen ◽  
H H Salem
Keyword(s):  
Monoclonal Antibody ◽  
Anticoagulant Activity ◽  
Activated Protein C ◽  
Factor Xa ◽  
Protein S ◽  
Human Neutrophil Elastase ◽  
Factor X ◽  
Sds Page

SummaryProtein S (PS) is a vitamin K-dependent anticoagulant that acts as a cofactor to activated protein C (APC). To date PS has not been shown to possess anticoagulant activity in the absence of APC.In this study, we have developed monoclonal antibody to protein S and used to purify the protein to homogeneity from plasma. Affinity purified protein S (PSM), although identical to the conventionally purified protein as judged by SDS-PAGE, had significant anticoagulant activity in the absence of APC when measured in a factor Xa recalcification time. Using SDS-PAGE we have demonstrated that prothrombin cleavage by factor X awas inhibited in the presence of PSM. Kinetic analysis of the reaction revealed that PSM competitively inhibited factor X amediated cleavage of prothrombin. PS preincubated with the monoclonal antibody, acquired similar anticoagulant properties. These results suggest that the interaction of the monoclonal antibody with PS results in an alteration in the protein exposing sites that mediate the observed anticoagulant effect. Support that the protein was altered was derived from the observation that PSM was eight fold more sensitive to cleavage by thrombin and human neutrophil elastase than conventionally purified protein S.These observations suggest that PS can be modified in vitro to a protein with APC-independent anticoagulant activity and raise the possibility that a similar alteration could occur in vivo through the binding protein S to a cellular or plasma protein.

In Vitro Stability of a Tissue-Type Plasminogen Activator Mutant, BM 06.022, in Human Plasma

1994 ◽  
Vol 72 (06) ◽  
pp. 906-911 ◽  
Author(s):  
D C Rijken ◽  
E Groeneveld ◽  
M M Barrett-Bergshoeff
Keyword(s):  
Plasminogen Activator ◽  
Half Life ◽  
Polyacrylamide Gel Electrophoresis ◽  
Tissue Type ◽  
Single Chain ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator ◽  
Sds Page ◽  
Chain Form

SummaryBM 06.022 is a non-glycosylated mutant of human tissue-type plasminogen activator (t-PA) comprising only the kringle-2 and proteinase domains. The in vivo half-life of BM 06.022 antigen is 4- to 5-fold longer than that of t-PA antigen. The in vitro half-life of the activity of BM 06.022 at therapeutic concentrations in plasma is shorter than that of t-PA. In this study the inactivation of BM 06.022 in plasma was further investigated.Varying concentrations of BM 06.022 were incubated in plasma for 0-150 min. Activity assays on serial samples showed a dose-dependent decline of BM 06.022 activity with a half-life from 72 min at 0.3 μg/ml to 38 min at 10 μg/ml. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) followed by fibrin autography showed the generation of several BM 06.022-complexes. These complexes could be completely precipitated with antibodies against Cl-inactivator, α2-antiplasmin and α1-antitrypsin.During the incubation of BM 06.022 in plasma, plasmin was generated dose-dependently as revealed by varying degrees of a2-anti-plasmin consumption and fibrinogen degradation. SDS-PAGE and immunoblotting showed that single-chain BM 06.022 was rapidly (i. e. within 45 min) converted into its two-chain form at concentrations of 5 μg/ml BM 06.022 and higher.In conclusion, BM 06.022 at therapeutic concentrations in plasma was inactivated by Cl-inactivator, a2-antiplasmin and a j-antitrypsin. The half-life of the activity decreased at increasing BM 06.022 concentrations, probably as a result of the generation of two-chain BM 06.022 which may be inactivated faster than the single-chain form.

scholarly journals Application of Selected Inoculant Producing Antifungal and Fibrinolytic Substances on Rye Silage with Different Wilting Time

Processes ◽  
2021 ◽  
Vol 9 (5) ◽  
pp. 879
Author(s):  
Seong-Shin Lee ◽  
Jeong-Seok Choi ◽  
Dimas Hand Vidya Paradhipta ◽  
Young-Ho Joo ◽  
Hyuk-Jun Lee ◽  
...  
Keyword(s):  
Lactobacillus Plantarum ◽  
Dry Matter ◽  
Lactobacillus Brevis ◽  
Neutral Detergent Fiber ◽  
Dry Matter Digestibility ◽  
Fiber Digestibility ◽  
Aerobic Stability ◽  
Commercial Inoculant

This research was conducted to determine the effects of selected inoculant on the silage with different wilting times. The ryes were unwilted or wilted for 12 h. Each rye forage was ensiled for 100 d in quadruplicate with commercial inoculant (Lactobacillus plantarum sp.; LPT) or selected inoculant (Lactobacillus brevis 100D8 and Leuconostoc holzapfelii 5H4 at 1:1 ratio; MIX). In vitro dry matter digestibility and in vitro neutral detergent fiber digestibility were highest in the unwilted MIX silages (p < 0.05), and the concentration of ruminal acetate was increased in MIX silages (p < 0.001; 61.4% vs. 60.3%) by the increase of neutral detergent fiber digestibility. The concentration of ruminal ammonia-N was increased in wilted silages (p < 0.001; 34.8% vs. 21.1%). The yeast count was lower in the MIX silages than in the LPT silages (p < 0.05) due to a higher concentration of acetate in MIX silages (p < 0.05). Aerobic stability was highest in the wilted MIX silages (p < 0.05). In conclusion, the MIX inoculation increased aerobic stability and improved fiber digestibility. As a result of the wilting process, ammonia-N in silage decreased but ruminal ammonia-N increased. Notably, the wilted silage with applied mixed inoculant had the highest aerobic stability.

Sign in / Sign up

Export Citation Format

Share Document