@article{fdi:010035621,
  title = {{T}he mechanism of action of alpha-amylase from {L}actobacillus fermentum on maltooligosaccharides},
  author = {{T}alamond, {P}ascale and {N}oirot, {M}ichel and {K}ochko, {A}lexandre de},
  editor = {},
  language = {{ENG}},
  abstract = {{T}he action pattern of {L}actobacillus fermentum alpha-amylase ({FERMENTA}) was examined using a series of maltooligosaccharides ({G}2-{G}7) as substrates. {S}tructurally, this enzyme has a molecular mass (106 k{D}a) almost twofold higher than alpha-amylases from mammalians and cereals. {T}he product pattern was investigated through an analysis of products and substrates using {HPAEC} with pulsed amperometric detection. {FERMENTA} was consistent with an endo-type of amylase. {T}he bond cleavage frequencies were studied using maltooligosaccharides of various chain lengths as substrate, i.e. maltose up to maltoheptaose and {DP} 4900-amylose catalyzed by {FERMENTA}. {T}he catalytic efficiency (k(cat)/{K}-m) increased with chain length from maltose (8.7 x 10(4){M} (-1)s(-1)) up to amylose (1 x 10(9) {M}(-1)s(-1)). {T}hese action pattern results revealed that {FERMENTA} can readily cleave the third linkage from the reducing end of the maltooligosaccharides ({G}5-{G}7). (c) 2006 {E}lsevier {B}.{V}. {A}ll rights reserved.},
  keywords = {alpha amylase ; maltooligosaccharide hydrolysis kinetics ; {L}acrobacillus fermentum ; maltooligosaccharides ; catalytic efficiency},
  booktitle = {},
  journal = {{J}ournal of {C}hromatography {B} {A}nalytical {T}echnologies in the {B}iomedical and {L}ife {S}ciences},
  volume = {834},
  numero = {1-2},
  pages = {42--47},
  ISSN = {1570-0232},
  year = {2006},
  DOI = {10.1016/j.jchromb.2006.02.005},
  URL = {https://www.documentation.ird.fr/hor/fdi:010035621},
}