Microbes and Us Essay Example | Topics and Well Written Essays - 500 words

Microbes and Us - Essay Example They are capable of utilizing diverse sources of carbon and nitrogen; and have an efficient energy metabolism (Hobson and Stewart, 15). The fermentation products in a glucose medium are succinic, formic and acetic acid (Bryant et al., 18). They are generalists capable of degrading a many carbohydrates except celluloses. Degradation of starch due to amylase activity converts starch into maltose and maltodextrins. The ÃŽ ±-amylases breakdown the carbohydrate chain randomly. Polysaccharides such as xylans and pectins present in plant cell walls are also degraded by caboxymethylcellulase and xylanase activity due to both extracellular and intracellular CM-cellulases and pectinases. The xylanase activity of the P. ruminicola has been attributed to multiple xylanase genes encoding endoglucanase, endoxylanase and oxygen sensitive exoxylanase activity (Gasparic et al., 2958) while proteolytic ability is due to a unique dipeptidylpeptidase activity (DAP1) (Hobson and Stewart, 15). It helps overcome lack of free transport of amino acids in the cell (Mackie & Morrison, 7). Obligate anaerobes P. ruminicola are among the most abundant (19%) of the rumen and hind gut microbiota cattle and sheep (Hobson and Stewart, 15). P. ruminicola are also indigenous population of human oral cavity and surface (Haraldsson, 23). As a consequence of the symbiotic relationship of P. ruminicola along with other similar microbes with the ruminants, the latter are able to derive nutrition from the herbaceous materials made of starch and hemicelluloses. Further due to the proteolytic activity of P. ruminicola low quality protein sources ingested by the host animal are converted into high quality microbial cell proteins that are then made available to the host animal. 3. Gasparic, A, et al. "A xylan hydrolase gene cluster in Prevotella ruminicola B14: sequence relationships, synergistic interactions, and oxygen sensitivity of a novel enzyme with exoxylanase and