Abstract: A method for fabricating semiconductor devices includes forming channel regions over a substrate. The channel regions, in parallel with one another, extend along a first lateral direction. Each channel region includes at least a respective pair of epitaxial structures. The method includes forming a gate structure over the channel regions, wherein the gate structure extends along a second lateral direction. The method includes removing, through a first etching process, a portion of the gate structure that was disposed over a first one of the channel regions. The method includes removing, through a second etching process, a portion of the first channel region. The second etching process includes one silicon etching process and one silicon oxide deposition process. The method includes removing, through a third etching process controlled based on a pulse signal, a portion of the substrate that was disposed below the removed portion of the first channel region.

Abstract: A nucleic acid extracting device includes a reagent containing unit, a mixing unit, and a flow channel unit. The reagent containing unit contains a specimen, a magnetic bead, and a reagent for extracting. The mixing unit includes a mixing chamber and a stirring assembly. The mixing chamber includes a chamber portion and a tube portion. The stirring assembly includes a main body and an extension. The main body is provided in the chamber portion. The tube portion connects the chamber portion. And the extension connects the main body and extends into the tube portion. The extension and an inner wall of the tube portion have first and second gaps therebetween respectively along first and second directions of the tube portion. The first gap is less than the second gap. The flow channel unit is connected between the reagent containing unit and the mixing unit.

Abstract: A nucleic acid extracting device includes a reagent containing unit, a mixing unit, and a flow channel unit. The reagent containing unit contains a specimen, a magnetic bead, and a reagent for extracting. The mixing unit includes a mixing chamber and a stirring assembly. The mixing chamber includes a chamber portion and a tube portion. The stirring assembly includes a main body and an extension. The main body is provided in the chamber portion. The tube portion connects the chamber portion. And the extension connects the main body and extends into the tube portion. The extension and an inner wall of the tube portion have first and second gaps therebetween respectively along first and second directions of the tube portion. The first gap is less than the second gap. The flow channel unit is connected between the reagent containing unit and the mixing unit.

Abstract: A biological sample processing device includes a base, a purification unit, a metering unit and a first tube. The purification unit is disposed on the base and is configured to purify a sample. The metering unit is disposed on the base and has an inlet, at least one metering trough and an overflow trough. The inlet is connected to the purification unit via the first tube, and the metering trough is connected between the inlet and the overflow trough. The sample from the purification unit is configured to enter the metering unit through the inlet to be moved toward the metering trough, and to be moved toward the overflow trough after the metering trough is filled with the sample.

Abstract: A beta-glucosidase having improved enzymatic activity is disclosed. The amino acid sequence of the beta-glucosidase is a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is a substitution of tyrosine at position 286 with phenylalanine, or a substitution of asparagine at position 639 with glutamate.

Abstract: A xylosidase having improved enzymatic activity is disclosed. The amino acid sequence of the xylosidase is a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is a substitution of phenylalanine at position 35 with glutamate, and/or a substitution of glutamine at position 41 with histidine.

Abstract: A xylosidase having improved enzymatic activity is disclosed. The amino acid sequence of the xylosidase is a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is a substitution of phenylalanine at position 35 with glutamate, and/or a substitution of glutamine at position 41 with histidine.

Abstract: A glucose oxidase having improved thermostability is disclosed. The amino acid sequence of the glucose oxidase is a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is a substitution of glutamate at position 129 with proline, and/or a substitution of glutamine at position 243 with valine.

Abstract: A phytase having improved thermostability is disclosed. The phytase has a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is one of mutations A to D. The mutation A is to substitute amino acids at positions 143 and 262 with cysteine, the mutation B is to substitute amino acids at positions 259 and 312 with cysteine, the mutation C is to substitute amino acids at positions 205 and 257 with cysteine, and the mutation D is to substitute amino acids at positions 264 and 309 with cysteine.

Abstract: A biological sample processing device includes a base, a purification unit, a metering unit and a first tube. The purification unit is disposed on the base and is configured to purify a sample. The metering unit is disposed on the base and has an inlet, at least one metering trough and an overflow trough. The inlet is connected to the purification unit via the first tube, and the metering trough is connected between the inlet and the overflow trough. The sample from the purification unit is configured to enter the metering unit through the inlet to be moved toward the metering trough, and to be moved toward the overflow trough after the metering trough is filled with the sample.

Abstract: A cellulase having improved thermostability is disclosed. The cellulase comprises a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is adding a cysteine in N terminal and adding a glycine and a cysteine or adding a proline and a cysteine in C terminal.

Abstract: A cellulase having improved enzymatic activity is disclosed. The cellulase comprises a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is a substitution of Tyrosine at position 161 with Histidine.

Abstract: A phytase having improved thermostability is disclosed. The phytase has a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is one of mutations A to D. The mutation A is to substitute amino acids at positions 143 and 262 with cysteine, the mutation B is to substitute amino acids at positions 259 and 312 with cysteine, the mutation C is to substitute amino acids at positions 205 and 257 with cysteine, and the mutation D is to substitute amino acids at positions 264 and 309 with cysteine.

Abstract: A cellulase having improved thermostability is disclosed. The cellulase comprises a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is adding a cysteine in N terminal and adding a glycine and a cysteine or adding a proline and a cysteine in C terminal.

Abstract: A pectinase having improved thermostability is disclosed. The pectinase has a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is a substitution of serine at position 181 with phenylalanine, methionine or leucine.

Abstract: A pectinase having improved thermostability is disclosed. The pectinase has a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is a substitution of serine at position 181 with phenylalanine, methionine or leucine.

Abstract: One embodiment of the disclosure provides a kit for detecting a mutation and/or polymorphism of a specific region in a target nucleotide sequence, including: at least one first primer consisting of a first segment and a second segment, wherein the first segment is a complementary strand of a first sequence and the second segment is a second sequence, and the 3? end of the first segment connects to the 5? end of the second segment; a second primer being a third sequence; at least one third primer consisting of a third segment and a fourth segment, wherein the third segment is a fourth sequence and the fourth segment is a complementary strand of a fifth sequence, and the 3? end of the third segment connects to the 5? end of the fourth segment; and a fourth primer being a complementary strand of a sixth sequence, wherein the specific region includes rs1799853, rs1057910, rs2108622, rs9923231 and rs9934438.

Abstract: A phytase having improved enzymatic activity is disclosed. The phytase has a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is a substitution of Valine at position 90 with Threonine. Alternatively, the phytase has a modified amino acid sequence of SEQ ID NO: 6, wherein the modification is a substitution of Asparagine at position 204 with Alanine or a substitution of Serine at position 206 with Alanine.

Abstract: A ?-mannanase having increased production yield and enzymatic activity is disclosed. The ?-mannanase has a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is a substitution of Tyrosine at position 25 with Histidine.

Abstract: A phytase having improved enzymaic activity is disclosed. The phytase has a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is a substitution of Valine at position 90 with Threonine. Alternatively, the phytase has a modified amino acid sequence of SEQ ID NO: 6, wherein the modification is a substitution of Asparagine at position 204 with Alanine or a substitution of Serine at position 206 with Alanine.