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: An auxiliary frame for detachably mounting in front of a spectacle frame includes a mounting frame and a retention arrangement. The mounting frame supports two shelter lenses for detachably mounting on a spectacle bridge. The retention arrangement includes two guiding members and two urging members. The two guiding members are rearwardly extended from two inner sides of the shelter lenses respectively and defined a guiding distance between the two guiding members which is smaller than the lens distance of the spectacle frame. The two urging members define an urging distance which is larger than the lens distance of the spectacle frame, such that when the guiding members are extended at the two inner sides of the spectacle lens respectively, the two urging members are adapted for applying an urging force against the two inner sides of the spectacle lens respectively.

Abstract: Described herein are four phenolic acid esterases, three of which correspond to domains of previously unknown function within bacterial xylanases, from XynY and XynZ of Clostridium thermocellum and from a feruloyl esterase of Ruminococcus. The fourth specifically exemplified phenolic acid esterase is a protein encoded within the genome of Orpinomyces PC-2. The amino acids of these polypeptides and nucleotide sequences encoding them are provided. Recombinant host cells, expression vectors and methods for the recombinant production of phenolic acid esterases are also provided. Further provided are methods for improving nutrient availability and ferulic acid availability when food or feed, or other material is treated with a phenolic acid esterase, desirably in combination with a xylanase.

Abstract: The present disclosure provides methods and DNA molecules for the synthesis of heterologous proteins in the fungus Aureobasidium pullulans either intracellularly or with secretion out of the cells using a regulated xylanase promoter and for secreted protein synthesis, a signal sequence. Further described are kits containing host cells for recombinant protein production, a vector containing an XynA transcription regulatory sequence, and instructions for using the vector to transform the host cells.

Abstract: Described herein are four phenolic acid esterases, three of which correspond to domains of previously unknown function within bacterial xylanases, from XynY and XynZ of Clostridium thermocellum and from a xylanase of Ruminococcus. The fourth specifically exemplified xylanase is a protein encoded within the genome of Orpinomyces PC-2. The amino acids of these polypeptides and nucleotide sequences encoding them are provided. Recombinant host cells, expression vectors and methods for the recombinant production of phenolic acid esterases are also provided.

Abstract: The present invention provides three fungal cellulases, their coding sequences, recombinant DNA molecules comprising the cellulase coding sequences, recombinant host cells and methods for producing same. The present cellulases are from Orpinomyces PC-2.

Abstract: The present invention provides three fungal cellulases, their coding sequences, recombinant DNA molecules comprising the cellulase coding sequences, recombinant host cells and methods for producing same. The present cellulases are from Orpinomyces PC-2.

Abstract: Provided is a novel &bgr;-glucosidase from Orpinomyces sp. PC2, nucleotide sequences encoding the mature protein and the precursor protein, and methods for recombinant production of this &bgr;-glucosidase.

Abstract: A cigarette lighter which has a safety locking device utilizing a spring biased latch. The cigarette lighter comprises a case, a top cover hingeably attached to an upper part of the case, a lighter seat, a press-down button, and the safety locking device. The latch is slidable mounted on top of the press-down button of the cigarette lighter. The latch is biased by an internal coil spring, which urges the latch to be engaged with the lighter seat, thereby preventing the press-down button from being pressed-down. When a user intends to use the cigarette lighter, the latch can be slid laterally against the spring force of the coil spring to disengage the latch from the lighter seat, thereby allowing the press-down button to be pressed down and ignite the cigarette lighter. Once the user releases the press-down button, it returns upwardly while the latch is biased back by the coil spring and automatically engages with the lighter seat again and thereby locks the press-down button.

Abstract: A cDNA (1,520 bp), designated celF, consisting of an open reading frame (ORF) encoding a polypeptide (CelF) of 432 amino acids was isolated from a cDNA library of the anaerobic rumen fungus Orpinomyces PC-2 constructed in Escherichia coli. Analysis of the deduced amino acid sequence showed that starting from the N-terminus, CelF consists of a signal peptide, a cellulose binding domain (CBD) followed by an extremely Asn-rich linker region which separate the CBD and the catalytic domains. The latter is located at the C-terminus. The catalytic domain of CelF is highly homologous to CelA and CelC of Orpinomyces PC-2, to CelA of Neocallimastix patriciarum and also to cellobiohydrolase IIs (CBHIIs) from aerobic fungi. However, Like CelA of Neocallimastix patriciarum, CelF does not have the noncatalytic repeated peptide domain (NCRPD) found in CelA and CelC from the same organism.

Abstract: A CDNA designated celE cloned from Orpinomyces PC-2 encodes a polypeptide (CelE) of 477 amino acids. CelE is highly homologous to CelB of Orpinomyces (72.3% identity) and Neocallimastix (67.9% identity), and like them, it has a non-catalytic repeated peptide domain (NCRPD) at the C-terminal end. The catalytic domain of CelE is homologous to glycosyl hydrolases of Family 5, found in several anaerobic bacteria. The gene of celE is devoid of introns. The recombinant proteins CelE and CelB of Orpinomyces PC-2 randomly hydrolyze carboxymethylcellulose and cello-oligosaccharides in the pattern of endoglucanases.

Abstract: The present invention provides a fungal lichenase, i.e., an endo-1,3-1,4-.beta.-D-glucanohydrolase, its coding sequence, recombinant DNA molecules comprising the lichenase coding sequences, recombinant host cells and methods for producing same. The present lichenase is from Orpinomyces PC-2.

Abstract: Xylanases having high specific activities from Orpinomyces sp. strain PC-2 are provided as well as methods for their purification. DNA sequences encoding these proteins are also provided.