Regulation of aspartokinase in Lactobacillus plantarum
β Scribed by O.O. Adebawo; J.L. Ruiz-Barba; P.J. Warner; G.B.O. Oguntimein
- Book ID
- 108837427
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 551 KB
- Volume
- 82
- Category
- Article
- ISSN
- 1364-5072
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π SIMILAR VOLUMES
Fractionation of cell-free extracts of Lactobacillus casei NCDO 151 (grown in Man's et al. (1960) broth) by polyacrylamide disc electrophoresis showed the presence of 4 constitutive peptidases. The enzymes appear to be a tripeptidase with a narrow substrate specificity, two true dipeptidases with id
Whole cell suspensions of some strains of each Lactobacillus casei and Lactobacillus plantarum were assayed for their caseinolytic activity in 0.1 M NaH,PO, buffer, pH 6.5, at 30 "C, using different assay methods. Azocasein was not as sensitive as casein (HAMMARSTEN) as a substrate. Inclusion of glu