Abstract: A display panel includes a first substrate, pixel structures, a first common pad, a second substrate, a second common electrode, a display medium and a conductive particle. The pixel structures are disposed on an active area of the first substrate. The first common pad is disposed on a peripheral area of the first substrate, and is electrically connected to first common electrodes of the pixel structures. The second common electrode is disposed on the second substrate. The conductive particle is disposed on the first common pad, and is electrically connected to the first common pad and the second common electrode. The conductive particle includes a core and a conductive film disposed on a surface of the core, where the conductive film has a main portion and raised portions, and a film thickness of each of the raised portions is greater than a film thickness of the main portion.

Abstract: A hose connecting device has a connector, an inner locking ring, an outer connector and a tubal body. The connector has an insertion section and an engaging section, the engaging section has a size greater than the insertion section, and the engaging section further has a stopping ring at a top end. The inner locking ring is jacketed onto the engaging section of the connector and abutting the stopping ring of the connector. The inner locking ring has an outer threaded section and an abutting portion disposed at a bottom end of the inner locking ring. The outer connector has one of a female connector and a male connector, and a channel, the channel has a positioning step at a middle portion, an inner threaded section disposed below the positioning step of the channel. The tubal body is jacketed onto the insertion section of the connector.

Abstract: A hose connecting device has a connector, an inner locking ring, an outer connector and a tubal body. The connector has an insertion section and an engaging section, the engaging section has a size greater than the insertion section, and the engaging section further has a stopping ring at a top end. The inner locking ring is jacketed onto the engaging section of the connector and abutting the stopping ring of the connector. The inner locking ring has an outer threaded section and an abutting portion disposed at a bottom end of the inner locking ring. The outer connector has one of a female connector and a male connector, and a channel, the channel has a positioning step at a middle portion, an inner threaded section disposed below the positioning step of the channel. The tubal body is jacketed onto the insertion section of the connector.

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 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: 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.

Abstract: A ?-mannanase having increased enzymaic 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 216 with Tryptophan.

Abstract: A ?-mannanase having increased enzymaic 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 216 with Tryptophan.

Abstract: A xylanase having increased enzymaic activity is disclosed. The xylanase has a modified amino acid sequence of SEQ ID NO: 2, wherein Tryptophan at position 125 is substituted with Phenylalanine and Phenylalanine at position 163 is substituted with Tryptophan.