Talamond Pascale, Noirot Michel, Kochko Alexandre de. (2006). The mechanism of action of alpha-amylase from Lactobacillus fermentum on maltooligosaccharides. Journal of Chromatography B Analytical Technologies in the Biomedical and Life Sciences, 834 (1-2), p. 42-47. ISSN 1570-0232.
Titre du document
The mechanism of action of alpha-amylase from Lactobacillus fermentum on maltooligosaccharides
Talamond Pascale, Noirot Michel, Kochko Alexandre de
Source
Journal of Chromatography B Analytical Technologies in the Biomedical and Life Sciences, 2006,
834 (1-2), p. 42-47 ISSN 1570-0232
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.
