%0 Journal Article
%9 ACL : Articles dans des revues avec comité de lecture non répertoriées par l'AERES
%A Giraud, Eric
%A Gosselin, L.
%A Marin, Bernard
%A Parada, J.L.
%A Raimbault, Maurice
%T Purification and characterization of an extracellular amylase from Lactobacillus plantarum strain A6
%D 1993
%L fdi:39192
%G ENG
%J Journal of Applied Bacteriology
%@ 0021-8847
%K ENZYME ; PURIFICATION ; METHODE ; ANALYSE ; ACTIVITE ENZYMATIQUE
%K BACTERIE LACTIQUE ; AMYLASE ; ELECTROPHORESE ; CARACTERISTIQUE BIOCHIMIQUE
%P 276-282
%U https://www.documentation.ird.fr/hor/fdi:39192
%> https://horizon.documentation.ird.fr/exl-doc/pleins_textes/pleins_textes_6/b_fdi_33-34/39192.pdf
%V 75
%W Horizon (IRD)
%X 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)
%$ 084FERMEN01