Abstract: A xylose isomerase (XI) enzyme which exhibits increased activity and affinity for xylose is produced by strain TC2-24 of the rumen bacterium, Prevotella ruminicola. The gene encoding this enzyme may be used to produce improved recombinant yeast capable of utilizing xylose. The recombinant yeast are preferably transformed with heterologous polynucleotide sequences coding both the P. ruminicola XI, and the xylulokinase (XKS) of a Prevotella species. Yeast transformed with the polynucleotide sequences coding both of these XI and XKS exhibit significantly increased xylose utilization and cell growth on a culture medium containing xylose as the sole carbon source, in comparison to yeast transformed with XKS and XI from other sources.

Abstract: Quebracho tannins are effective for the treatment of animal wastes which contain feces or fecal waste-containing material to inhibit odor emissions therefrom. Application of an effective amount of Quebracho tannins to the animal wastes elicits one or both of reducing gas emissions (such as total gas, hydrogen sulfide, and/or methane) therefrom, and reducing the populations or metabolic activity of anaerobic sulfate reducing bacteria therein. Reduction of odor emissions from the animal waste may also be effected by combining the Quebracho tannins with animal litter which is applied in the locus or vicinity of the animal.

Abstract: Xylose-containing plant material may be hydrolyzed to xylose using a ?-D-xylosidase which exhibits unexpectedly high activity. The enzyme has a kcat value for catalysis of approximately 185 sec?1 for 1,4-?-D-xylobiose (X2) when measured at a pH of 5.3 and a temperature of 25° C.; this is at least 10-fold greater than reported for other xylosidases at 25° C. and their optimal pH. The enzyme also has an isoelectric point of approximately 4.4. When reacted at a pH between about 4.5 and about 7.7, the ?-D-xylosidase exhibits surprisingly high activity for hydrolyzing xylose-containing plant materials to xylose. The xylose released from plant materials may then be converted to other secondary products such as ethanol by fermentation or other reaction. This ?-D-xylosidase may be used alone or in combination with other hydrolytic or xylanolytic enzymes for treatment of lignocellulosic or hemicellulosic plant materials or plant material hydrolysates or xylooligosaccharides.

Abstract: Xylose-containing plant material may be hydrolyzed to xylose using a ?-D-xylosidase which exhibits unexpectedly high activity. The enzyme has a kcat value for catalysis of approximately 185 sec?1 for 1,4-?-D-xylobiose (X2) when measured at a pH of 5.3 and a temperature of 25° C.; this is at least 10-fold greater than reported for other xylosidases at 25° C. and their optimal pH. The enzyme also has an isoelectric point of approximately 4.4. When reacted at a pH between about 4.5 and about 7.7, the ?-D-xylosidase exhibits surprisingly high activity for hydrolyzing xylose-containing plant materials to xylose. The xylose released from plant materials may then be converted to other secondary products such as ethanol by fermentation or other reaction. This ?-D-xylosidase may be used alone or in combination with other hydrolytic or xylanolytic enzymes for treatment of lignocellulosic or hemicellulosic plant materials or plant material hydrolysates or xylooligosaccharides.

Abstract: A protease has been isolated from a symbiotic bacterium found in the gland of Deshayes of the marine shipworm. The protease remains active over the pH range of about 4-12, exhibits salt tolerance up to 3M sodium chloride, retains a high level of activity above 50.degree. C. for at least 60 min, and is stimulated by oxidizing agents, particularly perborate. The properties of this protease suggest widespread utility in detergents and other low-temperature industrial applications.

Abstract: A protease has been isolated from a symbiotic bacterium found in the gland of Deshayes of the marine shipworm. The protease remains active over the pH range of about 4-12, exhibits salt tolerance up to 3M sodium chloride, retains a high level of activity above 50.degree. C. for at least 60 min, and is stimulated by oxidizing agents, particularly perborate. The properties of this protease suggest widespread utility in detergents and other low-temperature industrial applications.