Removal of Yersinia enterocolitica from fresh parsley by washing with acetic acid or vinegar

Karapınar, Mehmet; Gönül, Şahika Aktuğ

doi:10.1016/0168-1605(92)90086-i

Cited by 53 publications

(24 citation statements)

References 10 publications

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“…The lack of extracellular processing enzymes within enteric pathogens suggests that these microorganisms may depend upon preliminary pectin depolymerization catalyzed by other intestinal flora such as Bacterioides sp. In addition, pectin degradation may also be a salvage pathway for energy generation during environmental persistence because Y. enterocolitica has been isolated directly from vegetable food sources (43)(44)(45)(46). This possibility has direct or indirect implications for human health because the consumption of such contaminated fruits and vegetables present a ubiquitous vector for food-borne Yersiniosis and other gastrointestinal infectious diseases.…”

mentioning

confidence: 99%

A Family 2 Pectate Lyase Displays a Rare Fold and Transition Metal-assisted β-Elimination

Abbott

Boraston

2007

Journal of Biological Chemistry

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The family 2 pectate lyase from Yersinia enterocolitica (YePL2A), solved to 1.5 Å , reveals it to be the first prokaryotic protein reported to display the rare (␣/␣) 7 barrel fold. In addition to its apo form, we have also determined the structure of a metal-bound form of YePL2A (to 2.0 Å ) and a trigalacturonic acid-bound substrate complex (to 2.1 Å ). Although its fold is rare, the catalytic center of YePL2A can be superimposed with structurally unrelated families, underlining the conserved catalytic amino acid architecture of the ␤-elimination mechanism. In addition to its overall structure, YePL2A also has two other unique features: 1) it utilizes a metal atom other than calcium for catalysis, and 2) its Brønstead base is in an alternate conformation and directly interacts with the uronate group of the substrate.Recently, a conserved pectin utilization pathway was discovered in a variety of human pathogens from Enterobacteraciae (1). This pathway is an abridged form of the efficient and highly decorated extracellular pectin degradation systems found in soft rot-causing bacteria from the genus Erwinia (2). Pectin is a heterogeneous polysaccharide primarily composed of an ␣-D-1,4-linked polygalacturonic acid backbone. The main function of this carbohydrate is to stabilize structural polysaccharides such as cellulose and xylan, providing rigidity to the cell wall. Degradation of this structural "glue" by the enzymes of plant pathogens therefore results in the characteristic cell necrosis and tissue maceration during soft rot infections.The majority of structural biology within this field has focused on the primary secreted agents of pathogenesis, which include pectate lyases (3, 4), polygalacturonases (5, 6), and pectin methylesterases (7,8). Although these enzymes utilize distinct catalytic mechanisms, they commonly display a righthanded parallel ␤-helix topology (9). There is a notable exception, however, because family 10 pectate lyases adopt an (␣/␣) 6 toroid conformation (10, 11). Interestingly, superimposition of bound oligogalacturonide substrates within the active sites of these two different pectate lyase folds showed that despite the disparity in overall structure, there is remarkable similarity in the architecture of the catalytic residues (10). This suggested that the process of galacto-configured uronic acid ␤-elimination by distinct enzymes demands a conserved framework within the active site.Following polygalacturonic acid depolymerization, oligogalacturonides are shuttled into the periplasm through a specific porin, KdgM (12,13). Within the periplasmic compartment there are commonly four conserved proteins present to further process oligo-and polygalacturonic acid substrates for intracellular transport (1, 14, 15) that we have structurally and functionally characterized. These proteins include a family 32 carbohydrate-binding module (CBM32) (16); a family 2 polysaccharide lyase (PL2A) and a family 28 glycoside hydrolase (GH28) (17), both of which are pectinases; and TogB, the specificity determi...

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confidence: 99%

A Family 2 Pectate Lyase Displays a Rare Fold and Transition Metal-assisted β-Elimination

Abbott

Boraston

2007

Journal of Biological Chemistry

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“…The efficacy of vinegar and other organic acids as a sanitizer is also confirmed by several others studies. Reduction in counts of Yersinia enterocolitica inoculated onto parsley leaves from 10 7 CFU/g to <1 CFU/g by washing in a solution containing 40 percent vinegar for 15 minutes was achieved by Karapinar & Gonul (1992). Treatment of ready-to-use salads with 90 ppm peracetic acid has been shown to reduce total counts and fecal coliforms by nearly 100-fold, which is similar to reductions with 100 ppm chlorine (Masson, 1990).…”

Section: Consumer Levelmentioning

confidence: 53%

Safe Re-use Practices in Wastewater-Irrigated Urban Vegetable Farming in Ghana

Keraita

Abaidoo

Beernaerts

et al. 2012

JAFSCD

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“…In addition, treatment in 5 % acetic acid for 30 min did not result in any recovery of aerobic bacteria, while treatment with vinegar gave a 3-6 log decrease in aerobic counts. The inactivation depended upon vinegar concentration and contact time (Karapinar and Gönül 1992 ).…”

Section: Organic Acidsmentioning

confidence: 99%

“…Karapinar and Gönül ( 1992 ) evaluated the use of acetic acid to inactivate Yersiniaenterocolitica on fresh parsley. The results showed a reduction of more than 7 log cycles after washing for 15 min in solutions of 2 % acetic acid or 40 % vinegar.…”

Section: Organic Acidsmentioning

confidence: 99%