Identification of Proteins Possibly Involved in Glucosinolate Metabolism in L. agilis R16 and E. coli VL8
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Tarih
2015
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info:eu-repo/semantics/closedAccess
Özet
This study was aimed to identify sinigrin-induced bacterial proteins potentially involved in the metabolism of glucosinolate in two glucosinolate-metabolising
bacteria Lactobacillus agilis R16 and Escherichia coli VL8.
Sinigrin (2 mM) was used to induce the proteins in both
bacteria under anaerobic incubation for 8 h at 30 C for L.
agilis R16 and 37 C for E. coli VL8 and the controls without
sinigrin were performed. Allyl isothiocyanate and allyl nitrile
as two degradation products of sinigrin were detected in
sinigrin-induced cultures of L. agilis R16 (27 % total products) and E. coli VL8 (38 % total products) from a complete
sinigrin degradation in 8 h for both bacteria. 2D gel electrophoresis was conducted to identify induced proteins with
at least twofold increased abundance. Sinigrin-induced L.
agilis R16 and the control produced 1561 and 1543 protein
spots, respectively. For E. coli VL8, 1363 spots were detected in sinigrin-induced and 1354 spots in the control. A
combination of distinct proteins and upregulated proteins of
32 and 35 spots in L. agilis R16 and E. coli VL8, respectively
were detected upon sinigrin induction. Of these, 12 and 16
spots from each bacterium respectively were identified by
LC–MS/MS. In both bacteria most of the identified proteins
are involved in carbohydrate metabolism, oxidoreduction
system and sugar transport while the minority belong to
purine metabolism, hydrolysis, and proteolysis. This indicated that sinigrin induction led to the expressions of proteins
with similar functions in both bacteria and these proteins may
play a role in bacterial glucosinolate metabolism.
