G. Bryant

Bio: G. Bryant is an academic researcher from United States Department of Agriculture. The author has contributed to research in topics: Dextransucrase & Leuconostoc mesenteroides. The author has an hindex of 2, co-authored 2 publications receiving 216 citations.

The effect of certain cultural factors on production of dextransucrase by Leuconostoc mesenteroides.

Abstract: Present knowledge on the characteristics of dextransucrase and its mode of action is based primarily on the important investigations of Hehre (1941, 1946, 1951) and Hehre and Sugg (1942). Hitherto, a serious impediment to studies of this interesting enzyme has been the difficulty of procuring dextransucrase. Development of further knowledge about it would be greatly facilitated by the availability of culture liquors rich in dextransucrase. The rapid formation of dextransucrase in high yields has been reported in a preliminary note (Koepsell and Tsuchiya, 1952). The present report deals in greater detail with our observations on factors affecting production of dextransucrase from Leuconostoc mesenteroides, strain NRRL B-512.2 However, culture liquors high in activity have been obtained from a large number of the organisms tested. The dextran produced by strain NRRL B-512 in the conventional whole culture procedure contains about 95 per cent a-1,6-glucopyranosidic linkage. Although the non-1,6 linkages have been assumed to be of the a-1,4 type, definite proof on this point is lacking (Jeanes and Wilham, 1950). L. mesenteroides, strain NRRL B-512, or its substrains, is the organism principally used in investigations of clinical dextran in the United States. Although the term \"dextransucrase\" is used in the singular for convenience, the possibility that more than one enzyme may be involved in the synthesis of dextran is recognized.

Structure-Function Relationships of Glucansucrase and Fructansucrase Enzymes from Lactic Acid Bacteria

Abstract: Lactic acid bacteria (LAB) employ sucrase-type enzymes to convert sucrose into homopolysaccharides consisting of either glucosyl units (glucans) or fructosyl units (fructans). The enzymes involved are labeled glucansucrases (GS) and fructansucrases (FS), respectively. The available molecular, biochemical, and structural information on sucrase genes and enzymes from various LAB and their fructan and a-glucan products is reviewed. The GS and FS enzymes are both glycoside hydrolase enzymes that act on the same substrate (sucrose) and catalyze (retaining) transglycosylation reactions that result in polysacchande formation, but they possess completely different protein structures. GS enzymes (family GH70) are large multidomain proteins that occur exclusively in LAB. Their catalytic domain displays clear secondary-structure similarity with α-amylase enzymes (family GH13), with a predicted permuted (β/α)8 barrel structure for which detailed structural and mechanistic information is available. Emphasis now is on identification of residues and regions important for GS enzyme activity and product specificity (synthesis of α-glucans differing in glycosidic linkage type, degree and type of branching, glucan molecular mass, and solubility). FS enzymes (family GH68) occur in both gram-negative and gram-positive bacteria and synthesize β-fructan polymers with either β-(2→6) (inulin) or β-(2→1) (levan) glycosidic bonds. Recently, the first high-resolution three-dimensional structures have become available for FS (levansucrase) proteins, revealing a rare five-bladed β-propeller structure with a deep, negatively charged central pocket. Although these structures have provided detailed mechanistic insights, the structural features in FS enzymes dictating the synthesis of either β-(2→6) or β-(2→1) linkages, degree and type of branching, and fructan molecular mass remain to be identified. Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Leuconostoc dextransucrase and dextran: production, properties and applications

Abstract: This review covers the production, properties and applications of the biopolysaccharide dextran; this biopolymer can be produced via fermentation either with Leuconostoc mesenteroides strains and other lactic acid bacteria or with certain Gluconobacter oxydans strains. The former strains convert sucrose into dextran with the dextransucrase enzyme whereas the latter convert maltodextrins into dextran with the dextran dextrinase enzyme. Emphasis is mainly focused on Leuconostoc strains as producer organisms of dextransucrase and dextran types. In addition to industrial fermentation processes producing the enzymes and/or the dextrans, biocatalysis principles are also being developed, whereby enzyme preparations convert sucrose or maltodextrins, respectively, into (oligo)dextrans. The chemical and physical properties of different dextrans are discussed in detail, together with the characteristics and molecular mode of action of dextransucrase. Subsequently, useful applications of dextran and some problems associated with undesirable formation of dextran are outlined. Copyright © 2005 Society of Chemical Industry

Glucansucrases: mechanism of action and structure–function relationships

Abstract: Glucansucrases are produced principally by Leuconostoc mesenteroides and oral Streptococcus species, but also by the lactic acid bacteria (Lactococci, Lactobacilli). They catalyse the synthesis of high molecular weight d-glucose polymers, named glucans, from sucrose. In the presence of efficient acceptors, they catalyse the synthesis of low molecular weight oligosaccharides. Glucosidic bond synthesis occurs without the mediation of nucleotide activated sugars and cofactors are not necessary. Glucansucrases have an industrial value because of the production of dextrans and oligosaccharides and a biological importance by their key role in the cariogenic process. They were identified more than 50 years ago. The first glucansucrase encoding gene was cloned more than 10 years ago. But the mechanism of their action remains incompletely understood. However, in order to synthesise oligosaccharides of biological interest or to develop vaccines against dental caries, elucidation of the factors determining the regiospecificity and the regioselectivity of glucansucrases is necessary. The cloning of glucansucrase encoding genes in addition to structure–function relationship studies have allowed the identification of important amino acid residues and have shown that glucansucrases are composed of two functional domains: a core region (ca. 1000 amino acids) involved in sucrose binding and splitting and a C-terminal domain (ca. 500 amino acids) composed of a series of tandem repeats involved in glucan binding. Enzymology studies have enabled different models for their action mechanism to be proposed. The use of secondary structure prediction has led to a clearer knowledge of structure–function relationships of glucansucrases. However, mainly due to the large size of these enzymes, data on the three-dimensional structure of glucansucrases (given by crystallography and modelling) remain necessary to clearly identify those features which determine function.