Horizon 1 1 17 ACLN : Articles dans des revues avec comité de lecture non répertoriées par l'AERES Journal of Applied Bacteriology 276-282 ENZYME PURIFICATION METHODE ANALYSE ACTIVITE ENZYMATIQUE BACTERIE LACTIQUE AMYLASE ELECTROPHORESE CARACTERISTIQUE BIOCHIMIQUE 1993 fdi:39192 ENG Journal of Applied Bacteriology 0021-8847 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 75 Horizon (IRD) 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