Abstract: Embodiments of the present disclosure provide a data processing method, an electronic device, and a storage medium. The data processing method includes: determining, in a receive agent node in response to receiving a first request data packet, a number of available buffer units in a request receiving buffer used to receive the first request data packet; and discarding, in response to the number of available buffer units being less than or equal to a first threshold, at least one request data packet stored in the request receiving buffer. The method can ensure that there is at least one available buffer unit in a buffer of the receive agent node for receiving or storing requests, thereby preventing congestion or deadlock in an interconnect network-on-chip and improving the performance of the interconnect network-on-chip.

Abstract: Embodiments of the present disclosure provide a data processing method, an electronic device, and a storage medium. The data processing method includes: determining, in a receive agent node in response to receiving a first request data packet, a number of available buffer units in a request receiving buffer used to receive the first request data packet; and discarding, in response to the number of available buffer units being less than or equal to a first threshold, at least one request data packet stored in the request receiving buffer. The method can ensure that there is at least one available buffer unit in a buffer of the receive agent node for receiving or storing requests, thereby preventing congestion or deadlock in an interconnect network-on-chip and improving the performance of the interconnect network-on-chip.

Abstract: Provided are modified cellulase enzymes exhibiting increase cellulose-hydrolyzing activity in the presence of lignin and/or reduced binding to lignin comprising modified linker peptides comprising one or more amino acid substitutions, insertions, or deletions that result in (a) a decrease in the calculated isoelectric point of the linker peptide and/or (b) an increase in the ratio of threonine:serine in the linker peptide relative to a parental linker peptide from which said modified linker peptide is derived. Also provided are genetic constructs comprising nucleic acid sequences encoding for modified cellulase enzymes, methods for the production of the modified cellulase enzymes from host strains and a process for hydrolysing cellulose with the modified cellulases in the presence of lignin.

Abstract: Provided are modified cellulase enzymes exhibiting increase cellulose-hydrolyzing activity in the presence of lignin and/or reduced binding to lignin comprising modified linker peptides comprising one or more amino acid substitutions, insertions, or deletions that result in (a) a decrease in the calculated isoelectric point of the linker peptide and/or (b) an increase in the ratio of threonine:serine in the linker peptide relative to a parental linker peptide from which said modified linker peptide is derived. Also provided are genetic constructs comprising nucleic acid sequences encoding for modified cellulase enzymes, methods for the production of the modified cellulase enzymes from host strains and a process for hydrolysing cellulose with the modified cellulases in the presence of lignin.

Abstract: Provided are modified cellulase enzymes exhibiting increase cellulose-hydrolyzing activity in the presence of lignin and/or reduced binding to lignin comprising modified linker peptides comprising one or more amino acid substitutions, insertions, or deletions that result in (a) a decrease in the calculated isoelectric point of the linker peptide and/or (b) an increase in the ratio of threonine:serine in the linker peptide relative to a parental linker peptide from which said modified linker peptide is derived. Also provided are genetic constructs comprising nucleic acid sequences encoding for modified cellulase enzymes, methods for the production of the modified cellulase enzymes from host strains and a process for hydrolyzing cellulose with the modified cellulases in the presence of lignin.

Abstract: Provided are isolated cellobiohydrolases comprising a modified Glycoside Hydrolase (GH) Family 7 catalytic domain, a GH Family 7 catalytic domain and a modified Family 1 carbohydrate binding module (CBM), or both a modified Family 7 catalytic domain and a modified Family 1 CBM. Such isolated cellobiohydrolases exhibit from 45% to about 99.9% amino acid sequence identity to amino acids 1-436 of SEQ ID NO: 1 or to amino acids 1-438 of SEQ ID NO: 2 and improved activity on process substrates. Also provided are genetic constructs and genetically modified microbes for expressing the isolated cellobiohydrolases, a process for producing the isolated cellobiohydrolases, cellulase enzyme mixtures comprising the isolated cellobiohydrolase and a process for hydrolyzing a cellulosic substrate with such cellulase enzyme mixtures.

Abstract: The present invention relates to a modified Family 5 cellulase comprising a substitution of an amino acid at position 363 with a non-native alanine, serine or threonine, the position determined from alignment of the modified Family 5 cellulase with amino acids 71-397 of a Trichoderma reesei Cel5A amino acid sequence as set forth in SEQ ID NO:1 and enzyme mixtures comprising same. Additionally provided is a genetic construct comprising a nucleic acid sequence encoding the modified Family 5 cellulase and a genetically modified microbe comprising the genetic construct. The invention also provides a process for producing the modified Family 5 cellulase.

Abstract: The present invention relates to a modified Family 5 cellulase comprising a substitution of an amino acid at position 363 with a non-native alanine, serine or threonine, said position determined from alignment of the modified Family 5 cellulase with amino acids 71-397 of a Trichoderma reesei Cel5A amino acid sequence as set forth in SEQ ID NO:1 and enzyme mixtures comprising same. Additionally provided is a genetic construct comprising a nucleic acid sequence encoding the modified Family 5 cellulase and a genetically modified microbe comprising the genetic construct. The invention also provides a process for producing the modified Family 5 cellulase.

Abstract: Provided are isolated cellobiohydrolases comprising a modified Glycoside Hydrolase (GH) Family 7 catalytic domain, a GH Family 7 catalytic domain and a modified Family 1 carbohydrate binding module (CBM), or both a modified Family 7 catalytic domain and a modified Family 1 CBM. Such isolated cellobiohydrolases exhibit from 45% to about 99.9% amino acid sequence identity to amino acids 1-436 of SEQ ID NO: 1 or to amino acids 1-438 of SEQ ID NO: 2 and improved activity on process substrates. Also provided are genetic constructs and genetically modified microbes for expressing the isolated cellobiohydrolases, a process for producing the isolated cellobiohydrolases, cellulase enzyme mixtures comprising the isolated cellobiohydrolase and a process for hydrolysing a cellulosic substrate with such cellulase enzyme mixtures.

Abstract: A modified Family 6 cellulase enzyme comprising a proline residue at position 413 is provided. Genetic constructs and genetically modified microbes comprising DNA sequences encoding the modified Family 6 cellulase are also provided. Family 6 cellulases of the invention display improved thermostability, thermophilicity, alkalophilicity, or a combination thereof, relative to the parent Family 6 cellulases. Such cellulases find use in a variety of applications in industry that require cellulase stability and activities at temperatures, pH values, or both, above that of the native enzyme.

Abstract: A modified Family 6 cellulase enzyme comprising a proline residue at position 413 is provided. Genetic constructs and genetically modified microbes comprising DNA sequences encoding the modified Family 6 cellulase are also provided. Family 6 cellulases of the invention display improved thermostability, thermophilicity, alkalophilicity, or a combination thereof, relative to the parent Family 6 cellulases. Such cellulases find use in a variety of applications in industry that require cellulase stability and activities at temperatures, pH values, or both, above that of the native enzyme.

Abstract: Provided are modified cellulase enzymes exhibiting increase cellulose-hydrolyzing activity in the presence of lignin and/or reduced binding to lignin comprising modified linker peptides comprising one or more amino acid substitutions, insertions, or deletions that result in (a) a decrease in the calculated isoelectric point of the linker peptide and/or (b) an increase in the ratio of threonine:serine in the linker peptide relative to a parental linker peptide from which said modified linker peptide is derived. Also provided are genetic constructs comprising nucleic acidsequences encoding for modified cellulase enzymes, methods for the production of the modified cellulase enzymes from host strains and a process for hydrolysing cellulose with the modified cellulases in the presence of lignin.

Abstract: A modified Family 6 cellulase enzyme comprising a proline residue at position 413 is provided. Genetic constructs and genetically modified microbes comprising DNA sequences encoding the modified Family 6 cellulase are also provided. Family 6 cellulases of the invention display improved thermostability, thermophilicity, alkalophilicity, or a combination thereof, relative to the parent Family 6 cellulases. Such cellulases find use in a variety of applications in industry that require cellulase stability and activities at temperatures, pH values, or both, above that of the native enzyme.

Abstract: A circuit and method are provided that eliminate race conditions in data storage devices. Generally, the circuit includes: (i) an input latch to which an address signal (ADD) is applied; (ii) a multiplexer (MUX) to which the ADD is coupled from the input latch and through which an output is supplied to an output latch; (iii) an address valid signal (ADV) input coupled to the output latch and to which an ADV is applied to close the output latch supplying the output to a circuit output; and (iv) a middle latch coupled between the input latch and the MUX to hold the ADD applied to the MUX until the output latch closes, independent of a change in the ADD applied to the input latch. Preferably, the circuit includes control logic configured to close the middle latch on a rising edge of ADV and reopen it when the output latch closes.

Abstract: A modified Family 6 cellulase enzyme comprising a proline residue at position 413 is provided. Genetic constructs and genetically modified microbes comprising DNA sequences encoding the modified Family 6 cellulase are also provided. Family 6 cellulases of the invention display improved thermostability, thermophilicity, alkalophilicity, or a combination thereof, relative to the parent Family 6 cellulases. Such cellulases find use in a variety of applications in industry that require cellulase stability and activities at temperatures, pH values, or both, above that of the native enzyme.