@article{fdi:39192,
  title = {{P}urification and characterization of an extracellular amylase from {L}actobacillus plantarum strain {A}6},
  author = {{G}iraud, {E}ric and {G}osselin, {L}. and {M}arin, {B}ernard and {P}arada, {J}.{L}. and {R}aimbault, {M}aurice},
  editor = {},
  language = {{ENG}},
  abstract = {{E}xtracellular amylase from #{L}actobacillus plantarum$ {A}6 was purified by fractionated precipitation with ammonium sulphate and by anion exchange chromatography. {T}he 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 k{D}a. {I}t was identified as an alpha-amylase, with an optimum p{H} of 5.5, an optimum temperature of 65°{C} and {K}m value of 2.38 g l-1 with soluble starch substrate. {T}he enzyme was inhibited by {N}-bromosuccinimide, iodine and acetic acid. {T}he enzyme activation energy was 30.9 k{J} mol-1. ({R}{\'e}sum{\'e} d'auteur)},
  keywords = {{ENZYME} ; {PURIFICATION} ; {METHODE} ; {ANALYSE} ; {ACTIVITE} {ENZYMATIQUE} ; {BACTERIE} {LACTIQUE} ; {AMYLASE} ; {ELECTROPHORESE} ; {CARACTERISTIQUE} {BIOCHIMIQUE}},
  booktitle = {},
  journal = {{J}ournal of {A}pplied {B}acteriology},
  volume = {75},
  numero = {},
  pages = {276--282},
  ISSN = {0021-8847},
  year = {1993},
  URL = {https://www.documentation.ird.fr/hor/fdi:39192},
}