%0 Journal Article
%9 ACL : Articles dans des revues avec comité de lecture répertoriées par l'AERES
%A Talamond, Pascale
%A Noirot, Michel
%A Kochko, Alexandre de
%T The mechanism of action of alpha-amylase from Lactobacillus fermentum on maltooligosaccharides
%D 2006
%L fdi:010035621
%G ENG
%J Journal of Chromatography B Analytical Technologies in the Biomedical and Life Sciences
%@ 1570-0232
%K alpha amylase ; maltooligosaccharide hydrolysis kinetics ; Lacrobacillus fermentum ; maltooligosaccharides ; catalytic efficiency
%M CC:0002369276-0005
%N 1-2
%P 42-47
%R 10.1016/j.jchromb.2006.02.005
%U https://www.documentation.ird.fr/hor/fdi:010035621
%> https://www.documentation.ird.fr/intranet/publi/2006/05/010035621.pdf
%V 834
%W Horizon (IRD)
%X The action pattern of Lactobacillus fermentum alpha-amylase (FERMENTA) was examined using a series of maltooligosaccharides (G2-G7) as substrates. Structurally, this enzyme has a molecular mass (106 kDa) almost twofold higher than alpha-amylases from mammalians and cereals. The 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. The 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. The 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)). These action pattern results revealed that FERMENTA can readily cleave the third linkage from the reducing end of the maltooligosaccharides (G5-G7). (c) 2006 Elsevier B.V. All rights reserved.
%$ 076