Characteristics of nitrite reductase activity in Lactobacillus lactis TS4
- 1 June 1985
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Microbiology
- Vol. 31 (6) , 558-562
- https://doi.org/10.1139/m85-104
Abstract
Nitrite reductase activity in Lactobacillus lactis TS4 was induced by the presence of nitrite and was active under anaerobic conditions. An electron donor was required. Glucose was the most efficient donor in whole cells, while NADH was the most efficient in cell extracts. The optimum nitrite concentration for reduction was 2.0 mM, with higher levels sharply inhibiting activity. The pH optimum for nitrite reduction by resting cell suspensions was 7.2, and the temperature optimum was 30 °C. High levels of NADH oxidase activity in cell extracts interfered with nitrite reductase activity. Fractionation of the cell extract by ultracentrifugation and ammonium sulphate precipitation decreased the specific activity of NADH oxidase by 40 and 41%, respectively. Nitrite reductase activity was detected in the supernatant fluid after centrifugation of cell extract at 226 000 × g for 1 h.This publication has 8 references indexed in Scilit:
- Incidence of Nitrite-Depleting Lactic Acid Bacteria in Cured Meats and in Meat Starter CulturesJournal of Food Protection, 1984
- Depletion of Sodium Nitrite by Lactic Acid Bacteria Isolated from Vacuum-Packed BolognaJournal of Food Protection, 1981
- Comparison of Two Methods and Improvements for Colorimetric Determination of Nitrite in Cod RoeJournal of Food Protection, 1979
- Formate‐Nitrite Reduction in Escherichia coli K12European Journal of Biochemistry, 1979
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- THE FATE OF NITRITE: REACTION WITH PROTEINJournal of Food Science, 1976
- Nitrite Reductase of Escherichia coli Specific for Reduced Nicotinamide Adenine DinucleotideJournal of Bacteriology, 1966
- Pyridine nucleotide oxidizing enzymes of Lactobacillus caseiArchives of Biochemistry and Biophysics, 1965