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Cold Plasma Synthesis of Poly(ethylene glycol)-like Layers on Stainless-Steel Surfaces to Reduce Attachment and Biofilm Formation by Listeria monocytogenes (2003)

WANG, Y. ; SOMERS, E. B. ; MANOLACHE, S. ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

Journal of food science 68 (2003), S. 0

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ISSN: 1750-3841

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology

Notes: Poly(ethylene glycol) (PEG)-like structures were generated on stainless steel under di(ethylene glycol) vinyl ether (DiEGVE) radio frequency-plasma environments. Electron spectroscopy for chemical analysis and attenuated total reflectance Fourier transform infrared spectroscopy indicated a PEG-like deposition, which was stable to cleaning, sanitizing, and storage for up to 2 mo. Atomic force microscopy and water contact angle analysis indicated that the modified stainless-steel surfaces were less rough and more hydrophilic than the unmodified surfaces. Listeria monocytogenes attachment and biofilm formation on modified surfaces decreased more than 90% compared with the unmodified stainless steel (P 〈 0.01). DiEGVE cold plasma was demonstrated to be a promising technique to reduce bacterial contamination on surfaces encountered in food-processing environments.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1365-2621.2003.tb05803.x

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The salCAB operon of Azospirillum irakense, required for growth on salicin, is repressed by SalR, a transcriptional regulator that belongs to the LacI/GalR family (2000)

Somers, E. ; Keijers, V. ; Ptacek, D. ; [et al.]

Springer

Molecular genetics and genomics 263 (2000), S. 1038-1046

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ISSN: 1617-4623

Keywords: Key wordsβ-Glucoside ; Azospirillum irakense ; Transcriptional repressor ; LacI

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract The salAB genes of Azospirillum irakense KBC1, which encode two aryl-β-glucosidases, are required for growth on salicin. In the 4-kb region upstream of the salAB genes, two additional genes, salC and salR, were identified. SalC shows characteristics of the outer membrane receptors in the FepA/FhuA family. The salCAB genes are transcribed as a polycistronic mRNA. The salR gene encodes a protein homologous to the LacI/GalR family of transcriptional repressors. Expression of the sal operon, measured by means of a salC-gusA translational fusion in A. irakense KBC1, requires the presence of aryl-β-glucosides such as arbutin and salicin. Expression is markedly enhanced when a simple carbon source, like glucose, cellobiose or malate, is added to the medium. In a salR mutant, expression of the salC-gusA fusion does not require an aryl-β-glucoside inducer. Expression of a salR-gusA fusion is constitutive. The product of arbutin hydrolysis (hydroquinone) partly inhibits the expression of a salC-gusA fusion in arbutin- or salicin-containing minimal medium. This effect is independent of SalR. Salicylalcohol, the hydrolysis product of salicin, also partly inhibits salC expression in a SalR-independent fashion, but only in salicin-containing minimal medium.