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Inhibition of proteolytic enzymes from Pseudomonas fluorescens ATCC 948 and of angiotensin I-converting enzyme by peptides from zein, hordein and gluten hydrolyzates
The proteolytic system of Lactobacillus sanfrancisco CB1: purification and characterization of a proteinase, dipeptidase and aminopeptidase
Purification and characterization of a proteinaceous compound from Pseudomonas fluorescens ATCC 948 with inhibitory activity against lactic acid bacteria
INHIBITION OF PROTEOLYTIC ENZYMES FROM PSEUDOMONAS FLUORESCENS ATCC 948 AND ANGIOTENSIN I-CONVERTING ENZYME BY PEPTIDES FROM ZEIN, HORDEIN AND GLUTEN HYDROLYZATES
La microflora degli impasti acidi. Localizzazione cellulare e caratterizzazione degli enzimi proteolitici dei batteri lattici
Antibacterial activity of sourdough lactic acid bacteria: isolation of a bacteriocin-like inhibitory substance from Lactobacillus sanfrancisco C57
Purification and characterization of a proteinaceous compound from Pseudomonas fluorescens ATCC 948 with inhibitory activity against some Gram-positive and Gram-negative bacteria of dairy interest
Purification and characterization of cystathionine γ-liase from Lactobacillus fermentum DT41
A homo-tetrameric ca. 140-kDa cystathionine y-lyase was purified to homogeneity from Luctobacillus,f~rmentum DT41 by four chromatographic steps. This was the first enzyme responsible for amino acid catabolism purified from lactobacilli. The activity is pyridoxal-5’-phosphate d pendent and the enzyme catalyzes the a,y-elimination reaction of L-cystathionine producing L-cysteine, ammonia and a-ketobutyrate. The cystathionine y-lyase produced a free thiol group, a keto acid component and ammonia from several amino acids, including L-cysteine and methionine, and amino acid derivatives. L-Cystine was the best substrate. The enzyme was stable in the conditions of cheese ripening and may contribute to the biosynthesis o
PURIFICATION AND CHARACTERIZATION OF A CELL SURFACE-ASSOCIATED ESTERASE FROM LACTOBACILLUS FERMENTUM DT 41
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