scholarly journals Nisin Activity Against Contaminant Bacteria Isolated From Bioethanol Fermentation Tanks

Author(s):  
Natalia Maia ◽  
Rachel Rigotti ◽  
Renata Silva ◽  
Bruna Lange ◽  
Giuseppe Meca ◽  
...  
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2004 ◽  
Vol 231 (1) ◽  
pp. 85-90 ◽  
Author(s):  
Olli Koponen ◽  
Timo M Takala ◽  
Ulla Saarela ◽  
Mingqiang Qiao ◽  
Per E.J Saris

2008 ◽  
Vol 74 (23) ◽  
pp. 7126-7129 ◽  
Author(s):  
Oleksandr Tokarskyy ◽  
Douglas L. Marshall

ABSTRACT The combined lactic acid, monolaurin, and nisin effects on time-to-detection (optical density at 600 nm) extension were greater (P < 0.05) than any single or paired combination effect, which demonstrates a synergistic interaction among the antimicrobials. Monolaurin exposure caused C12:0 cell membrane incorporation. Lactic acid caused increased monolaurin C12:0 membrane incorporation, while nisin had no influence. We postulate that lactic acid-enhanced monolaurin C12:0 incorporation into the cell membrane increased membrane fluidity resulting in increased nisin activity.


2014 ◽  
Vol 77 (9) ◽  
pp. 1624-1629 ◽  
Author(s):  
JULIE A. AUXIER ◽  
KARL F. SCHILKE ◽  
JOSEPH McGUIRE

The cationic, amphiphilic peptide nisin is an effective inhibitor of gram-positive bacteria whose mode of action does not encourage pathogenic resistance, and its proper incorporation into food packaging could enhance food stability, safety, and quality in a number of circumstances. Sufficiently small peptides have been shown to integrate into otherwise nonfouling polyethylene oxide (PEO) brush layers in accordance with their amphiphilicity and ordered structure, including nisin, and we have recently shown that nisin entrapment within a PEO layer does not compromise the nonfouling character of that layer. In this work we test the hypothesis that surface-bound, pendant PEO chains will inhibit displacement of entrapped nisin by competing proteins and, in this way, prolong retention of nisin activity at the interface. For this purpose, the antimicrobial activity of nisin-loaded, PEO-coated surfaces was evaluated against the gram-positive indicator strain, Pediococcus pentosaceous. The retained antimicrobial activity of nisin layers was evaluated on uncoated and PEO-coated surfaces after incubation in the presence of bovine serum albumin for contact periods up to 1 week. Nisin-loaded, uncoated and PEO-coated samples were withdrawn at selected times and were incubated on plates inoculated with P. pentosaceous to quantify nisin activity by determination of kill zone radii. Our results indicate that nisin activity is retained at a higher level for a longer period of time after entrapment within PEO than after direct adsorption in the absence of PEO, owing to inhibition of nisin exchange with dissolved protein afforded by the pendant PEO chains.


2017 ◽  
Vol 2 (2) ◽  
pp. 212
Author(s):  
Sulaxana Kumari Chauhan ◽  
R. Kumar ◽  
S. Nadanasabapathi

Nisin activity in tender coconut water using <em>Lactococcus lactis</em> subspecies <em>cremoris </em>as test microorganism was estimated using turbidimetry by measuring optical density at 600nm after 6 h. of incubation at 37<sup>0</sup>C. The test microorganism was cultivated in nutrient broth with different concentration of nisin along with tender coconut water. A standard curve was drawn between optical density and known concentration of nisin. The nisin concentration of the test samples was measured by curve fitting method using the optical density values. The results thus obtained by this method were reproducible, rapid and more accurate in tender coconut water and hence it may be employed for the determination of nisin activity in tender coconut water on regular basis for quality control purposes.


1999 ◽  
Vol 62 (9) ◽  
pp. 1004-1010 ◽  
Author(s):  
E. ALISON DAVIES ◽  
CATHERINE F. MILNE ◽  
HELEN E. BEVIS ◽  
RICHARD W. POTTER ◽  
JO M. HARRIS ◽  
...  

Lactic acid bacteria (LAB) commonly cause spoilage in minimal heat-treated vacuum-packed cured delicatessen meats. Predominant species are Lactobacillus sake and L. curvatus. LAB strains isolated from spoiled products of this type (liver sausage, ham and bologna sausage) were found to be sensitive to low nisin concentrations (maximum of 1.25 μg g−1). Addition of 25 μg g−1 nisin (as Nisaplin) inhibited the growth of LAB spoilage organisms inoculated into vacuum-packed pasteurized bologna-type sausages stored at 8°C. Control sausages became spoiled (&gt;108 LAB CFU g−1) by day 7, whereas sausages containing nisin remained unspoiled for &gt;50 days. The effect of three types of phosphates (used as emulsifiers) on nisin activity in the sausages was compared. LAB growth rate was fastest in samples containing orthophosphate, and slowest in sausages containing diphosphate. The shelf life was also greatly extended in the latter. Fat content also affected nisin activity. Nisin activity (as indicated by LAB inhibition) was greatest in samples containing 15% &gt; 25% &gt; 37% (wt/wt) fat. In a sausage formulation containing 37% fat and incorporating diphosphate as emulsifier, levels of nisin as low as 2.5 μg g−1 showed antibacterial effects. A nisin level of 6.25 μg g−1 totally inhibited LAB growth for over 4 weeks and 25 μg g−1 for 5 weeks. Spoilage control was achieved in the same sausage formulation but with 25% (wt/wt) fat; 12.5 μg g−1 nisin prevented LAB growth for 5 weeks.


1970 ◽  
Vol 16 (12) ◽  
pp. 1205-1211 ◽  
Author(s):  
A. Hurst ◽  
H. Kruse

The absorbancy of cell suspensions of Streptococcus lactis increased immediately when the suspensions were incubated in a solution of 50 mM (pH 7.2) tris buffer, 100 mM CaCl2, and 140 mM glucose. The reaction was sensitive to NaF, carbonyl cyanide m-chlorophenylhydrazine, valinomycin, and Na-iodoacetate and insensitive to ouabain, dinitrophenol, n-ethylmaleimide, and malonic acid. During the optical reaction the cells incorporated 45 Ca2+ and lost nisin bioassay activity. When Ca2+ was omitted there was a diminished optical reaction and bioassayable nisin was lost only temporarily. With Ca2+ present but glucose omitted or in the complete reaction solution plus iodoacetate, the optical reaction, incorporation of 45 Ca2+, and inactivation of nisin were all stopped. Hot acid-soluble proteins extracted from cells after the optical reaction gave electrophoretic patterns which differed significantly from the controls but the peak areas of the nisin-like proteins remained unchanged. The bioassay activity was one-sixth that of the control. Cell-free solutions of purified nisin did not interact with CaCl2. It is suggested that in the presence of glucose living cells incorporate calcium, which leads to a configurational change of the cells which is measured by the optical reaction, and that this configurational change is associated with nisin inactivation.


1999 ◽  
Vol 46 (2) ◽  
pp. 151-157 ◽  
Author(s):  
Paloma Zapico ◽  
Máximo de Paz ◽  
Margarita Medina ◽  
Manuel Nuñez

2006 ◽  
Vol 69 (4) ◽  
pp. 951-956 ◽  
Author(s):  
VIRGINIA A. STERGIOU ◽  
LINDA V. THOMAS ◽  
MARTIN R. ADAMS

Loss of nisin activity in meat has been ascribed, in part, to the formation of a nisin-glutathione adduct. Activity is lost more quickly in raw meat than in cooked meat, and this has been taken as evidence that the reaction is enzyme mediated. Formation of the nisin-glutathione adduct has been confirmed but is shown not to be enzyme mediated. Retention of activity in cooked meat is shown to be due to the loss of free sulfhydryl groups during cooking as a result of the reaction of glutathione with proteins and not a result of the inactivation of endogenous enzymes. Microbial enzymes do not appear to play a role, as similar losses are seen in raw and cooked meat extracts, both of which contained undetectable levels of microorganisms.


2019 ◽  
Vol 72 (2) ◽  
pp. 282-286
Author(s):  
Zuleyka S Oros‐Flores ◽  
Blanca E García‐Almendárez ◽  
José E Barboza‐Corona ◽  
Rubén Salcedo‐Hernández
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