Abstract: The disclosure provides a sealing system applicable for an ocean power generation device, which includes at least one first seal and a water leakage protection device. The water leakage protection device is located at a side of at least one first seal away from seawater, and includes a sealed water storage tank and a drain pipe. The sealed water storage tank collects and stores seawater leaked from the at least one first seal. One end of the drain pipe is communicated with the sealed water storage tank, and the seawater stored in the sealed water storage tank is discharged through the drain pipe.

Abstract: A display substrate is provided, including: a base substrate and a plurality of sub-pixels disposed on the base substrate. Each sub-pixel includes a pixel driving circuit, and the pixel driving circuit includes a writing transistor, a compensation transistor, a first reset transistor, and a storage capacitor. The display substrate includes a semiconductor layer, a first conductive layer and a second conductive layer disposed in sequence on the base substrate. Gates of the writing transistor, the compensation transistor and the first reset transistor are in the first conductive layer and are implemented as an integral structure. Active layers of the writing transistor, the compensation transistor and the first reset transistor are in the semiconductor layer. A first storage capacitor electrode of the storage capacitor is in the first conductive layer, and a second storage capacitor electrode of the storage capacitor is in the second conductive layer.

Abstract: An R-3-aminobutyric acid preparation method with high efficiency and high stereoselectivity. The method comprises using aspartase with stereoisomerization catalytic activity derived from Escherichia coli to efficiently convert butenoic acid into R-3-aminobutyric acid. After only 24 h of reaction, the conversion rate is as high as ?98%, and the ee value is ?99.9%. The conversion efficiency is greatly improved, the reaction time is shortened, and the production costs are reduced. The method features a high yield, a high conversion rate, low costs, a short production cycle, a simple process, ease of enlargement, suitability for mass production and the like.

Abstract: A genetically engineered bacterium and a preparation method and use thereof are disclosed. The genetically engineered bacteria contain a gene encoding ?-1,2-fucosyltransferase, and a gene encoding a protein tag is connected to the gene encoding ?-1,2-fucosyltransferase; the protein tag is MBP, SUMO1, SUMO2 or TrxA, the amino acid sequence of the MBP is shown in SEQ ID NO: 2, the amino acid sequence of the SUMO1 is shown in SEQ ID NO: 3, the amino acid sequence of the SUMO2 is shown in SEQ ID NO: 4, the amino acid sequence of the TrxA is shown in SEQ ID NO: 5. Fermentation with the genetically engineered bacteria can greatly increase the yield of 2?-fucosyllactose compared to the genetically engineered bacteria that only expresses ?-1,2-fucosyltransferase exogenously, and the yield can be more than doubled in a preferred case.

Abstract: The present invention discloses a genetically engineered bacteria, which is E. coli integrated with lysogenic ?DE3, and lacZ gene is completely inactivated, but does not affect exogenous protein expression of the genetically engineered bacteria. The present invention also discloses a method for culturing the genetically engineered bacteria, and a method for preparing human milk oligosaccharides using the same, and use of the genetically engineered bacteria. The genetically engineered bacteria of the present invention can efficiently produce human milk oligosaccharides, such as 2?-fucosyllactose, and have wide industrial application prospects.

Abstract: The invention discloses a genetically engineered bacterium and its application in the preparation of sialyllactose. The genetically engineered bacterium has an N-acetylneuraminic acid biosynthesis pathway, includes multiple copies of a gene neuB for encoding sialic acid synthase, and the gene neuB is initiated for expression by a strong promoter. Using the genetically engineered bacteria of the invention to produce sialyllactose has the advantages of high yield and low overall cost.

Abstract: The invention discloses a genetically engineered bacterium and a method for preparing a fucosylated oligosaccharide using the same. The method includes: transferring a fucosyl group of a donor to an oligosaccharide receptor by a fucosyltransferase heterologously expressed in a genetically engineered bacterium; wherein the donor is a nucleotide-activated donor, the fucosyltransferase has ?-1,2-fucosyltransferase activity; wherein, the fucosyltransferase is selected from one or more of the enzymes corresponding to NCBI Accession Numbers WP_109047124.1, RTL12957.1, MBP7103497.1, WP_120175093.1, RYE22506.1, WP_140393075.1 and HJB91111.1. The preparation method of the invention has high yield, greatly improved substrate conversion rate and product conversion rate, and has the potential to be applied to industrial production.

Abstract: Provided is a display substrate. The display substrate includes including a base substrate having a first display region and a second display region; in the pixel circuit included in the pixels in the second display region, the conductive line connected to the metal layer is a transparent conductive line, and the transparent conductive line is disposed between the two existing insulating layers.

Abstract: A glycosyltransferase and an application thereof, the amino acid sequence of the glycosyltransferase being shown as in SEQ ID NO: 112 or an amino acid sequence having at least 99% sequence identity to SEQ ID NO: 112. The glycosyltransferase of the present invention has high enzyme activity and good stability and, when used for the preparation of steviol glycosides, has a significant improvement in catalytic activity and significantly improved conversion rate compared to the parent glycosyltransferase, solving the problem of the high price of the glycosyl donor UDPG (and/or ADPG), and thereby reducing the reaction costs and facilitating industrial production.

Abstract: A display substrate includes a normal display area and a transmissive display area provided within the normal display area, the normal display area being configured to perform image display, the transmissive display area including at least one pixel island, the pixel island being configured to perform image display and transmit light; the pixel island of the transmissive display area including an initial transmission line for transmitting an initial signal and at least one pixel drive circuit connected to the initial transmission line, the initial transmission line including a first transmission line with a main part extending in a first direction and a second transmission line with a main part extending in a second direction, the first transmission line and the second transmission line being connected to form a grid structure.

Abstract: Use of a stereoselective transaminase in the asymmetric synthesis of a chiral amine. In particular, provided is use of a polypeptide in the production of a chiral amine or a downstream product using a chiral amine as a precursor. Further provided is a method for producing a chiral amine, comprising culturing a strain expressing the polypeptide so as to obtain a chiral amine. Further provided are novel prochiral compounds, a chiral amine production strain and a method for constructing the chiral amine production strain. The stereoselective transaminase has a broad substrate spectrum and thus has a broad application potential in the preparation of a chiral amine.

Abstract: Disclosed in the present invention is an L-glutamate dehydrogenase mutant, the sequence of the L-glutamate dehydrogenase mutant being a sequence in which amino acid residue A at position 175 in SEQ ID NO: 1 is mutated to be G, and amino acid residue V at position 386 is mutated to be an amino acid residue having less steric hindrance. Further disclosed in the present invention is an application of the described L-amino acid dehydrogenase mutant in the preparation of L-glufosinate-ammonium or a salt thereof. When the L-glutamate dehydrogenase mutant of the present invention is used to prepare L-glufosinate-ammonium or a salt thereof, compared to an L-glutamate dehydrogenase mutant in which only position 175 or 386 is mutated, the specific enzyme activity is higher. Therefore, the action efficiency of the enzyme is improved, reaction costs are reduced, and industrial production is facilitated.

Abstract: Provided are a class of compounds, represented by formula (I??), as selective EGFR inhibitors, a pharmaceutical composition containing the compounds, useful intermediates for preparing the compounds, and a method for using the compounds of the present invention to treat cell proliferative diseases, such as cancers.

Abstract: Provided are an L-glutamate dehydrogenase mutant and an application thereof, the mutant mutating the amino acid residue A at position 166 and/or the amino acid residue V at position 376 shown in SEQ ID NO. 1 into a hydrophilic or small sterically hindered amino acid residue, the application performing an amination reaction of 2-oxo-4-(hydroxymethylphosphinyl)butyrate in the presence of an L-amino acid dehydrogenase mutant, an inorganic amino donor, and a reduced coenzyme NADPH, and performing an acidification reaction on the obtained L-glufosinate salt to obtain L-glufosinate. Compared to wild L-glutamate dehydrogenase, the present L-glutamate dehydrogenase mutant has a higher concentration of substrates that can be catalysed when preparing L-glufosinate, thereby increasing the efficiency of the action of the enzyme and reducing reaction costs.

Abstract: The present invention provides a novel aminopyrimidine compound as a fourth-generation EGFR (T790M/C797S mutation) selective inhibitor, a pharmaceutical composition comprising the compound, an intermediate useful for preparing the compound, and a method for treating a cell proliferative disease, such as a cancer, by using the compound of the present invention.

Abstract: Use of a stereoselective transaminase in the asymmetric synthesis of a chiral amine. In particular, provided is use of a polypeptide in the production of a chiral amine or a downstream product using a chiral amine as a precursor. Further provided is a method for producing a chiral amine, comprising culturing a strain expressing the polypeptide so as to obtain a chiral amine. Further provided are novel prochiral compounds, a chiral amine production strain and a method for constructing the chiral amine production strain. The stereoselective transaminase has a broad substrate spectrum and thus has a broad application potential in the preparation of a chiral amine.

Abstract: Provided are a class of compounds, represented by formula (I??), as selective EGFR inhibitors, a pharmaceutical composition containing the compounds, useful intermediates for preparing the compounds, and a method for using the compounds of the present invention to treat cell proliferative diseases, such as cancers.

Abstract: Disclosed in the present invention is an L-glutamate dehydrogenase mutant, the sequence of the L-glutamate dehydrogenase mutant being a sequence in which amino acid residue A at position 175 in SEQ ID NO: 1 is mutated to be G, and amino acid residue V at position 386 is mutated to be an amino acid residue having less steric hindrance. Further disclosed in the present invention is an application of the described L-amino acid dehydrogenase mutant in the preparation of L-glufosinate-ammonium or a salt thereof. When the L-glutamate dehydrogenase mutant of the present invention is used to prepare L-glufosinate-ammonium or a salt thereof, compared to an L-glutamate dehydrogenase mutant in which only position 175 or 386 is mutated, the specific enzyme activity is higher. Therefore, the action efficiency of the enzyme is improved, reaction costs are reduced, and industrial production is facilitated.

Abstract: Provided is a D-amino acid oxidative enzyme mutant. The sequence of the mutant comprises a sequence by mutating the 54th amino acid residue N, the 58th amino acid residue F, the 211th amino acid residue C, and the 213th amino acid residue M of the sequence shown in SEQ ID NO:1 or the sequence having at least 76% identity with SEQ ID NO:1. The D-amino acid oxidative enzyme mutant has a higher enzyme activity, enzyme activity stability and/or ammonium resistance than a mild D-amino acid oxidative enzyme mutant. Also provided is an application of the D-amino acid oxidative enzyme mutant in preparing 2-oxo-4-(hydroxymethylphosphinyl)butyric acid.

Abstract: Provided are an L-glutamate dehydrogenase mutant and an application thereof, the mutant mutating the amino acid residue A at position 166 and/or the amino acid residue V at position 376 shown in SEQ ID NO. 1 into a hydrophilic or small sterically hindered amino acid residue, the application performing an amination reaction of 2-oxo-4-(hydroxymethylphosphinyl)butyrate in the presence of an L-amino acid dehydrogenase mutant, an inorganic amino donor, and a reduced coenzyme NADPH, and performing an acidification reaction on the obtained L-glufosinate salt to obtain L-glufosinate. Compared to wild L-glutamate dehydrogenase, the present L-glutamate dehydrogenase mutant has a higher concentration of substrates that can be catalysed when preparing L-glufosinate, thereby increasing the efficiency of the action of the enzyme and reducing reaction costs.