An aminotransferase from Lactococcus lactis initiates conversion of amino acids to cheese flavor compounds

Article Abstract:

The aminotransferase from Lactococcus lactis transaminates the aromatic amino acids, leucine and methionine, producing flavor compounds, thus giving flavor to cheese. The aminotransferase uses ketoacids and alph-ketoglutarate in this process. The enzyme does not use use oxaloacetate as second substrate and fails to act on aspartate. It is a pyridoxal 5'-phosphate-dependent enzyme, optimally active between pH 6.5 and 8 and between 35 and 45 degree celsius. It is active under cheese-ripening conditions also.

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Cell density-dependent gene contributes to efficient seed colonization by Pseudomonas putida KT2440

Article Abstract:

The gene involved in seed colonization by Pseudomonas putida KT2440, whose expression responds to cell density and to seed exudates, is analyzed. This is the first evidence that P. putida KT2440 possesses an as-yet-uncharacterized quorum-sensing system and suggests that cell-cell and cell-host communications are important for spermosphere colonization.

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Expression of a Pseudomonas putida aminotransferase involved in lysine catabolism is induced in the rhizosphere

Article Abstract:

Researchers have identified a gene in Pseudomonas putida that produces a delta-aminovalerate aminotransferase involved in lysine catabolism. Gene expression increases in the presence of corn root exudates.

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