Amylosucrase from Neisseria polysaccharea: novel catalytic properties.

FEBS Lett

Centre de Bioingénierie Gilbert Durand, UMR CNRS 5504, UMR INRA 792, INSA, Complexe Scientifique de Rangueil, 31077, Toulouse, France.

Published: April 2000

Amylosucrase is a glucosyltransferase that synthesises an insoluble alpha-glucan from sucrose. The catalytic properties of the highly purified amylosucrase from Neisseria polysaccharea were characterised. Contrary to previously published results, it was demonstrated that in the presence of sucrose alone, several reactions are catalysed, in addition to polymer synthesis: sucrose hydrolysis, maltose and maltotriose synthesis by successive transfers of the glucosyl moiety of sucrose onto the released glucose, and finally turanose and trehalulose synthesis - these two sucrose isomers being obtained by glucosyl transfer onto fructose. The effect of initial sucrose concentration on initial activity demonstrated a non-Michaelian profile never previously described.

Download full-text PDF

Source
http://dx.doi.org/10.1016/s0014-5793(00)01406-xDOI Listing

Publication Analysis

Top Keywords

amylosucrase neisseria
8
neisseria polysaccharea
8
catalytic properties
8
synthesis sucrose
8
sucrose
6
polysaccharea novel
4
novel catalytic
4
properties amylosucrase
4
amylosucrase glucosyltransferase
4
glucosyltransferase synthesises
4

Similar Publications

In this study, waxy corn starch was modified with 230 U or 460 U of amylosucrase (AS) from (NP) to elongate the glucan. The amylose content of the AS-modified starches was determined using iodine and concanavalin A (Con A) methods, and their in vivo digestion, thermal, swelling, and pasting properties were evaluated. The amylose content of AS-treated starches was not significantly different ( > 0.

View Article and Find Full Text PDF

The branching ratio of enzymatically synthesized α-glucans impacts microbiome and metabolic outcomes of in vitro fecal fermentation.

Carbohydr Polym

July 2024

Food Engineering Department, Engineering Faculty, Necmettin Erbakan University, Konya 42090, Turkiye; Medical and Cosmetic Plants Application and Research Center, Necmettin Erbakan University, Konya 42090, Turkiye. Electronic address:

The aim of this study was to evaluate the impacts of enzymatically synthesized α-glucans possessing α-1,4- and α-1,6-glucose linkages, and varying in branching ratio, on colonic microbiota composition and metabolic function. Four different α-glucans varying in branching ratio were synthesized by amylosucrase from Neisseria polysaccharea and glycogen branching enzyme from Rhodothermus obamensis. The branching ratios were found to range from 0 % to 2.

View Article and Find Full Text PDF

Secretory expression of amylosucrase in Bacillus licheniformis through twin-arginine translocation pathway.

J Ind Microbiol Biotechnol

January 2024

Department of Biological Chemical Engineering, College of Chemical Engineering and Materials Science, Tianjin University of Science and Technology, Tianjin 300457, China.

Unlabelled: Amylosucrase (EC 2.4.1.

View Article and Find Full Text PDF

Amylosucrase from Neisseria polysaccharea (NpAS) produces the linear amylose-like α-glucans by the elongation property from sucrose, and 4,3-α-glucanotransferase from Lactobacillus fermentum NCC 2970 (4,3-αGT) newly synthesizes the α-1,3 linkages after cleaving the α-1,4 linkages by the glycosyltransferring property. This study focused on the synthesis of high molecular α-1,3/α-1,4-linked glucans by combining NpAS and 4,3-αGT and analyzed their structural and digestive properties. The enzymatically synthesized α-glucans have a molecular weight of >1.

View Article and Find Full Text PDF

Production of branched glucan polymer by a novel thermostable branching enzyme of Bifidobacterium thermophilum via one-pot biosynthesis containing a dual enzyme system.

Carbohydr Polym

June 2023

Department of Food Science and Biotechnology, Carbohydrate Bioproduct Research Center, Sejong University, Seoul 05006, Republic of Korea. Electronic address:

Glycogen-like particles (GLPs) are applied in food, pharmaceutical, and cosmetics. The large-scale production of GLPs is limited by their complicated multi-step enzymic processes. In this study, GLPs were produced in a one-pot dual-enzyme system using Bifidobacterium thermophilum branching enzyme (BtBE) and Neisseria polysaccharea amylosucrase (NpAS).

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!