Giraud Eric auteur aut IRD Gosselin L. auteur aut IRD Marin Bernard auteur aut IRD Parada J.L. auteur aut IRD Raimbault Maurice auteur aut IRD text journalArticle eng text/pdf reformatted digital access 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) specialized ENZYME PURIFICATION METHODE ANALYSE ACTIVITE ENZYMATIQUE BACTERIE LACTIQUE AMYLASE ELECTROPHORESE CARACTERISTIQUE BIOCHIMIQUE 084FERMEN01 75 276-282 1993 0021-8847 https://www.documentation.ird.fr/hor/fdi:39192 0021-8847 [F B39192] 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 IRD - Base Horizon / Pleins textes 1994-03-29 2006-05-31 fdi:39192 fre