Fructose 6-phosphate phosphoketolase activity in wild-type strains of Lactobacillus, isolated from the intestinal tract of pigs

Phosphoketolases are key enzymes of the phosphoketolase pathway of heterofermentative lactic acid bacteria, which include lactobacilli. In heterofermentative lactobacilli xylulose 5-phosphate phosphoketolase (X5PPK) is the main enzyme of the phosphoketolase pathway. However, activity of fructose 6-p...

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Bibliographic Details
Published in:Applied biochemistry and microbiology 2012-09, Vol.48 (5), p.444-451
Main Authors: Bolado-Martínez, E, Acedo-Félix, E, Peregrino-Uriarte, A. B, Yepiz-Plascencia, G
Format: Article
Language:English
Subjects:
Bacteria
Biochemistry
Biomedical and Life Sciences
Digestive system
Enzymatic activity
enzyme activity
Enzymes
fructose 6-phosphate
gene expression
genes
Hogs
intestines
lactic acid bacteria
Lactobacillus
Lactobacillus mucosae
Lactobacillus reuteri
Lactobacillus salivarius
Life Sciences
Medical Microbiology
Microbiology
pentose phosphate cycle
phosphoketolase
polymerase chain reaction
Sugar
swine
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Summary:Phosphoketolases are key enzymes of the phosphoketolase pathway of heterofermentative lactic acid bacteria, which include lactobacilli. In heterofermentative lactobacilli xylulose 5-phosphate phosphoketolase (X5PPK) is the main enzyme of the phosphoketolase pathway. However, activity of fructose 6-phosphate phosphoketolase (F6PPK) has always been considered absent in lactic acid bacteria. In this study, the F6PPK activity was detected in 24 porcine wild-type strains of Lactobacillus reuteri and Lactobacillus mucosae, but not in the Lactobacillus salivarius or in L. reuteri ATCC strains. The activity of F6PPK increased after treatment of the culture at low-pH and diminished after porcine bile-salts stress conditions in wild-type strains of L. reuteri. Colorimetric quantification at 505 nm allowed to differentiate between microbial strains with low activity and without the activity of F6PPK. Additionally, activity of F6PPK and the X5PPK gene expression levels were evaluated by real time PCR, under stress and nonstress conditions, in 3 L. reuteri strains. Although an exact correlation, between enzyme activity and gene expression was not obtained, it remains possible that the xpk gene codes for a phosphoketolase with dual substrate, at least in the analyzed strains of L. reuteri.
ISSN:0003-6838
1608-3024
DOI:10.1134/S000368381205002X