Abstract: A fan-out wafer level multilayer wiring package structure, wherein the package structure comprises a plurality of semiconductor chips, a multilayer interposer, a vertical interconnection interposer, molding materials and a redistribution layer; the back surface of the semiconductor chip is bonded to the back surface of the multilayer wiring interposer with the bonding material, and is placed on the same horizontal plane as the vertical interconnection interposer and packaged as a whole with the molding material, the redistribution layer is provided on the surface of the structure; the semiconductor chip, the multilayer interposer, the conductive material of the vertical interconnection interproser and the solder ball are connected by the conductive metal layer of the redistribution layer to achieve the signal interconnection between the semiconductor chip and the multilayer interposer and the I/O signal transfer of the semiconductor chip.

Abstract: Disclosed are methods for the synthesis of chiral alcohols by Sortase A-mediated oxidoreductase oligomers, which relates to the field of biocatalysis. In the present disclosure, oxidoreductase oligomers were used as biocatalysts for chiral alcohol preparation. Compared to wild-type enzymes, the oxidoreductase oligomers significantly improved catalytic activity and thermal stability. The sortase A-mediated oxidoreductase oligomers had 6-8 folds improvement in specific activity over that of the wild-type enzymes. The oligomers displayed a Tm value 6-12° C. higher than that of the wild-type, suggesting the sortase A-mediated oxidoreductase oligomers significantly improved thermostability of the enzymes. The oxidoreductase oligomers catalyzed asymmetric transformation to produce (S)-1-phenyl-1,2-ethanediol or (R)-1-phenethyl alcohol within 3-6 hr, with an optical purity of 98%-100% and a yield of 98%-99%.

Abstract: A fan-out wafer level multilayer wiring package structure, wherein the package structure comprises a plurality of semiconductor chips, a multilayer interposer, a vertical interconnection interposer, molding materials and a redistribution layer; the back surface of the semiconductor chip is bonded to the back surface of the multilayer wiring interposer with the bonding material, and is placed on the same horizontal plane as the vertical interconnection interposer and packaged as a whole with the molding material, the redistribution layer is provided on the surface of the structure; the semiconductor chip, the multilayer interposer, the conductive material of the vertical interconnection interproser and the solder ball are connected by the conductive metal layer of the redistribution layer to achieve the signal interconnection between the semiconductor chip and the multilayer interposer and the I/O signal transfer of the semiconductor chip.

Abstract: Provided are novel hetero-oligomers of (S)-carbonyl reductases and their application in catalyzing the reduction of polyphenyl ketones. Also provided are recombinant strains expressing hetero-oligomers of SCR/SCR2 or SCR2/SCR3, which can catalyze the reduction of polyphenyl ketones. The hetero-oligomer of SCR/SCR2 is capable of catalyzing 2,4-dichlorobenzophenone, 2-naphthalenone and [(E)-2-[3-[3-[2-(7-chloro-2-quinolinyl)ethenyl]phenyl]-3-oxopropyl]benzoic acid methyl ester (Keto Easter M) with a specific activity of 4.55 U/mg, 2.43 U/mg and 0.86 U/mg, respectively. The hetero-oligomer of SCR2/SCR3 is capable of catalyzing 2,4-dichlorobenzophenone and [(E)-2-[3-[3-[2-(7-chloro-2-quinolinyl)ethenyl]phenyl]-3-oxopropyl]benzoic acid methyl ester (Keto Easter M) with a specific activity of 4.42 U/mg and 1.21 U/mg, respectively.

Abstract: Disclosed are methods for the synthesis of chiral alcohols by Sortase A-mediated oxidoreductase oligomers, which relates to the field of biocatalysis. In the present disclosure, oxidoreductase oligomers were used as biocatalysts for chiral alcohol preparation. Compared to wild-type enzymes, the oxidoreductase oligomers significantly improved catalytic activity and thermal stability. The sortase A-mediated oxidoreductase oligomers had 6-8 folds improvement in specific activity over that of the wild-type enzymes. The oligomers displayed a Tm value 6-12° C. higher than that of the wild-type, suggesting the sortase A-mediated oxidoreductase oligomers significantly improved thermostability of the enzymes. The oxidoreductase oligomers catalyzed asymmetric transformation to produce (S)-1-phenyl-1,2-ethanediol or (R)-1-phenethyl alcohol within 3-6 hr, with an optical purity of 98%-100% and a yield of 98%-99%.