Role of Streptococcus mutans in human dental decay.

Lactic acid bacteria (LAB) constitute a group of gram-positive bacteria united by a constellation of morphological, metabolic, and physiological characteristics The general description of the bacteria included in the group is gram-positive, nonsporing, nonrespiring cocci or rods, which produce lactic acid as the major end product during the fermentation of carbohydrates The LAB term is intimately associated with bacteria involved in food and feed fermentation, including related bacteria normally associated with the (healthy) mucosal surfaces of humans and animals The boundaries of the group have been subject to some controversy, but historically the genera Lactobacillus, Leuconostoc, Pediococcus, and Streptococcus form the core of the group Taxonomic revisions of these genera and the description of new genera mean that LAB could, in their broad physiological definition, comprise around 20 genera However, from a practical, food-technology point of view, the following genera are considered the principal LAB: Aerococcus, Carnobacterium, Enterococcus, Lactobacillus, Lactococcus, Leuconostoc, Oenococcus, Pediococcus, Streptococcus, Tetragenococcus, Vagococcus, and Weissella The genus Bifidobacterium, often considered in the same context as the genuine lactic acid bacteria and sharing some of their typical features, is phylogenetically unrelated and has a unique mode of sugar fermentation The classification of lactic acid bacteria into different genera is largely based on morphology, mode of glucose fermentation, growth at different temperatures, configuration of the lactic acid produced, ability to grow at high salt concentrations, and acid or alkaline tolerance Chemotaxonomic markers such as fatty acid composition and constituents of the cell wall are also used in classification In addition, the present taxonomy relies partly on true phylogenetic relationships,

Lactic acid bacteria: classification and physiology.

Factors affecting the fermentative lactic acid production from renewable resources1

Another explanation for the toxicity of fermentation acids at low pH: anion accumulation versus uncoupling

Citrate metabolism plays an important role in many food fermentations involving lactic acid bacteria. Since citrate is a highly oxidized substrate, no reducing equivalents are produced during its degradation, resulting in the formation of metabolic end products other than lactic acid. Some of these end products, such as diacetyl and acetaldehyde, have very distinct aroma properties and contribute significantly to the quality of the fermented foods. In this review the metabolic pathways involved in product formation from citrate are described, the bioenergetic consequences of this metabolism for the lactic acid bacteria are discussed and detailed information on some key enzymes in the citrate metabolism is presented. The combined knowledge is used for devising strategies to avoid, control or improve product formation from citrate.

Citrate metabolism in lactic acid bacteria

Pyruvate formate-lyase (EC 2.3.1.54) from Streptococcus mutans strain JC2 was purified in an anaerobic glove box, giving a single band on disk and sodium dodecyl sulfate electrophoresis. This enzyme was immediately inactivated by exposure to the air. Enzyme activity was unstable even when stored anaerobically, but the activity was restored by preincubating the inactivated crude enzyme with S-adenosyl-L-methionine, oxamate, and reduced for ferredoxin or methylviologen. On the other hand, the purified enzyme was not reactivated. Either D-glyceraldehyde 3-phosphate or dihydroxyacetone phosphate strongly inhibited this enzyme. The inhibitory effects of these compounds were largely influenced by enzyme concentration. The inhibition of these triose phosphates in cooperation with the reactivating effect of ferredoxin and the fluctuations of both the enzyme and the triose phosphate levels may efficiently regulate the pyruvate formate-lyase activity in S. mutans in vivo.

T Yamada

Papers

Purification of pyruvate formate-lyase from Streptococcus mutans and its regulatory properties.