Giraud Eric, Gosselin L., Marin Bernard, Parada J.L., Raimbault Maurice. (1993). Purification and characterization of an extracellular amylase from Lactobacillus plantarum strain A6. Journal of Applied Bacteriology, 75, p. 276-282. ISSN 0021-8847.
Titre du document
Purification and characterization of an extracellular amylase from Lactobacillus plantarum strain A6
Année de publication
1993
Type de document
Article
Auteurs
Giraud Eric, Gosselin L., Marin Bernard, Parada J.L., Raimbault Maurice
Source
Journal of Applied Bacteriology, 1993,
75, p. 276-282 ISSN 0021-8847
Extracellular amylase from Lactobacillus plantarum A6 was purified by fractionated precipitation with ammonium sulphate and by anion exchange chromatography. The homogeneity of the purified fraction was tested by polyacrylamide gel electrophoresis and showed multiple amylase forms. A major form had an estimated molecular weight of 50 kDa. It was identified as an alpha-amylase, with an optimum pH of 5.5, an optimum temperature of 65°C and Km value of 2.38 g l-1 with soluble starch substrate. The enzyme was inhibited by N-bromosuccinimide, iodine and acetic acid. The enzyme activation energy was 30.9 kJ mol-1. (Résumé d'auteur)
