Effect of glucanases of bacteroides oralis ig4a on artificial plaque of Streptococcus mutans.

Cloning and Expression of an α-1,3-Glucanase Gene fromBacillus circulansKA-304: The Enzyme Participates in Protoplast Formation ofSchizophyllum commune

“…RM1 enzyme. Many bacterial -1,3-glucanases, such as those of Flavobacterium sp., 15) Pseudomonas sp., 18) Streptomyces chartreuses, 19) Bacteroides oralis, 20,21) and Bacillus circulans, 22) have been studied from the same point of view as that for the Bacillus sp. RM1 enzyme to remove tooth plaque created by oral bacteria, but the gene of these enzymes has not been cloned, except for that of the Bacillus sp.…”

“…RM1 -1,3-glucanase was named as mutanase (EC.3.2.1.59) that hydrolyzes mutan formed by an oral bacterium, Streptococcus mutans. The presence of mutanases has been also reported in several bacteria [14][15][16][17][18][19][20][21][22] and filamentous fungi. [23][24][25][26][27][28][29][30][31][32][33] Among these -1,3-glucanases, the genes of y To whom correspondence should be addressed.…”

Subcellular Localization of D-Glucanases in Bacteroides oralis Ig4a

“…Alternatively the release of D-glucose was measured by using D-glucose oxidase (Dahlqvist, 1961). Unless otherwise noted, the reactions were performed by the addition of 0.5 ml of a suitably diluted enzyme solution to 0.5 ml 20 mM-phosphate buffer, pH 7.0, containing 0.2% dextran, and incubating at 37 "C for 30 min (Takahashi, 1982). The mutanase activity was estimated in the same way except that a 0.2% suspension of pseudonigeran was used as the substrate instead of dextran (Hasegawa et ul., 1968).…”

“…1971) was assessed by assaying for alkaline phosphatase (Malamy & Horecker, 1961), principally a periplasmic enzyme, and P-Dgalactosidase (Zipser, 1963), principally a cytoplasmic enzyme. The various D-glucan-hydrolysing enzymes in the cytoplasmic and periplasmic fractions of B. oralis Ig4a were isolated by sequential chromatography on DEAEcellulose and Bio-Gel A-0.5 m (Bio-Rad) as described previously (Takahashi, 1982).…”

“…In order to examine this possibility, enzymes in the periplasmic and cytoplasmic fractions were separated by sequential chromatography on DEAE-cellulose and Bio-Gel A-0.5 m columns (Takahashi, 1982). Fractions containing enzyme activity were pooled, concentrated in an Amicon pressure cell with a Diaflo PM-10 membrane, and dialysed against 20 mwphosphate buffer, pH 7.0.…”