Non starch polysaccharide hydrolyzing enzyme preparations analyzed in this study were composed of up to nine (1-3, 1-4)-beta-glucanase activities and up to six xylanase activities with different molecular weights in the range from 100 kD down to 18 kD as determined with SDS/PAGE zymograms. Partially purified enzyme fractions differed in terms of pH-optima, isoelectric point and thermal stability in aquaeous solutions. Different beta-glucanase activities were found in different production strains, although some enzymes were conserved over genus boundaries. Enzyme preparations from the same or related strains exhibited different patterns of enzyme activity, indicating modification of strain and/or fermentation conditions. Some enzyme preparations contained significant amounts of polygalacturonase and/or galactomannase activity. The pH profiles of whole enzyme preparations resulted from pH optima of isoenzyme fractions. Temperature optima for all preparations were between 50 and 60 degrees C. Thermal stability of high molecular weight components tended to be lower than for low molecular weight fractions. Fractions with cellulase activity were most stable, followed by (1-3, 1-4)-beta-glucanase activities, while fractions with xylanase activities exhibited low thermal stabilities. Incubation of enzyme preparations and their respective active fractions in digesta supernatants revealed only small differences in residual xylanase activity. Digesta from gizzard samples led to the highest inactivation. It is concluded that commercial enzyme preparations display different modes of action and that the development of improved enzyme preparations depends not only on thermal stability, but also on pH profile, substrate specificity and proteolytic stability within the digestive tract.