Streptococcus bovis JB1 was found to produce a 25-kDa extracellular enzyme active against beta-(1,3-1,4)-glucans. A gene was isolated encoding a specific beta-(1,3-1,4)-glucanase that corresponds to this size and belongs to glycoside hydrolase family 16. A 4- to 10-fold increase in supernatant beta-glucanase activity was obtained when the cloned beta-glucanase gene was reintroduced into S, bovis JB1 by use of constructs based on the plasmid vector pTRW10 or pIL253, The beta-(1,3-1,4)-glucanase gene was also expressed upon introduction of the pTRW10 construct pTRWL1R into Lactococcus lactis IL2661 and Enterococcus faecalis JH2-SSI although extracellular activity was 8- to 50-fold lower than that in S. bovis JB1. The beta-(1,3-1,4)-glucanase purified from the culture supernatant of S. bovis JB1 carrying pTRWL1R showed a K-m of 2.8 mg per mi and a V-max of 338 mu mol of glucose equivalents per min per mg of protein with barley beta-glucan as the substrate. The S, bovis beta-(1,3-1,4)-glucanase may contribute to the ability of this bacterium to utilize starch by degrading structural polysaccharides present in endosperm cell walls.
|Number of pages||5|
|Journal||Applied and Environmental Microbiology|
|Publication status||Published - Oct 1997|
- ACID-SEQUENCE SIMILARITIES