Abstract: A deep-sea battery device includes: a housing, a pouch, and a protective cover. The housing defines a pressure-releasing port, the pouch seals the pressure-releasing port. The pouch includes a body, a cushioning portion, and a connection portion. The cushioning portion is disposed between the body and the connection portion. The connection portion is clamped between the protective cover and the housing. The cushioning portion at least comprises an annular cushioning protrusion surrounding a periphery of the body. The cushioning protrusion protrudes toward an interior of the housing. A side of the cushioning protrusion away from the interior of the housing defines a groove. An opening of the groove faces the protective cover. The protective cover defines a through hole, the through hole is disposed at a position corresponding to the body. The body is disposed lower than an outer side of the housing that defines the pressure-releasing port.

Abstract: The invention provides anti-VISTA antibody drug conjugates which may be used for targeted delivery of anti-inflammatory agents such as steroids to immune cells, e.g., myeloid cells. The invention also provides methods of using anti-VISTA antibody drug conjugates in the treatment of inflammatory and/or autoimmune conditions and/or for alleviating the toxicity of anti-inflammatory agents such as steroids.

Abstract: A deep-sea battery apparatus and a method for assembling the deep-sea battery apparatus. The deep-sea battery apparatus includes a casing, an upper cover), a battery pack, a pressure compensation assembly, and a fastening plate assembly. The upper cover is sealingly connected to a top of the casing, the battery pack is disposed inside the casing, the pressure compensation assembly is disposed in the casing and on a side of the battery pack, and the fastening plate assembly is annular in shape and sealingly sleeved and connected at a connection between the casing and the upper cover.

Abstract: The invention discloses an alcohol dehydrogenase mutant and use thereof. The alcohol dehydrogenase mutant of the present invention has high thermal stability and enables high catalytic efficiency and high conversion rate (i.e. space time yield) in the asymmetric reduction of prochiral diaryl ketones to produce chiral diaryl alcohols. Therefore, the alcohol dehydrogenase mutant of the present invention has extremely high prospect of application in the production of chiral diaryl alcohols, such as (S)-(4-chlorophenyl)-(pyridin-2-yl)-methanol, (R)-(4-chlorophenyl)-(pyridin-2-yl)-methanol.

Abstract: The invention discloses an alcohol dehydrogenase mutant and use thereof. The alcohol dehydrogenase mutant of the present invention has high thermal stability and enables high catalytic efficiency and high conversion rate (i.e. space time yield) in the asymmetric reduction of prochiral diaryl ketones to produce chiral diaryl alcohols. Therefore, the alcohol dehydrogenase mutant of the present invention has extremely high prospect of application in the production of chiral diaryl alcohols, such as (S)-(4-chlorophenyl)-(pyridin-2-yl)-methanol, (R)-(4-chlorophenyl)-(pyridin-2-yl)-methanol.

Abstract: Disclosed is an alcohol dehydrogenase mutant and application thereof in cofactor regeneration, and belongs to the technical fields of enzyme engineering and bioengineering. The alcohol dehydrogenase mutant is obtained by mutating valine at position 84 and/or tyrosine at position 127 in alcohol dehydrogenase having an original amino acid sequence as set forth in SEQ ID No. 1. The alcohol dehydrogenase mutant has high activity for a variety of alcohol co-substrates, and can catalyze these enzyme co-substrates for the regeneration of cofactor NADPH. Compared with the wild-type alcohol dehydrogenase KpADH, the alcohol dehydrogenase mutant has higher activity and catalytic efficiency, and for co-substrate 1,4-butanediol, its kcat value can be up to 75.9 min?1, its kcat/Km value can be up to 2009 min?1·M?1, and its Km value can be as low as 11.3 mM. Therefore, the alcohol dehydrogenase mutant has a higher value in industrial application.

Abstract: The present disclosure discloses an alcohol dehydrogenase mutant and application thereof in synthesis of diaryl chiral alcohols, and belongs to the technical field of bioengineering. The alcohol dehydrogenase mutant of the present disclosure has excellent catalytic activity and stereoselectivity, and may efficiently catalyze the preparation of a series of chiral diaryl alcohols in R- and S-configurations. By coupling alcohol dehydrogenase of the present disclosure to glucose dehydrogenase or formate dehydrogenase, the synthesis of chiral diaryl alcohol intermediates of various antihistamines may be achieved. Compared with the prior art, a method for preparing diaryl chiral alcohols through asymmetric catalytic reduction using the alcohol dehydrogenase of the present disclosure has the advantages of simple and convenient operation, high substrate concentration, complete reaction and high product purity, and has great industrial application prospects.

Abstract: The present disclosure discloses an alcohol dehydrogenase mutant and application thereof in synthesis of diaryl chiral alcohols, and belongs to the technical field of bioengineering. The alcohol dehydrogenase mutant of the present disclosure has excellent catalytic activity and stereoselectivity, and may efficiently catalyze the preparation of a series of chiral diaryl alcohols in R- and S-configurations. By coupling alcohol dehydrogenase of the present disclosure to glucose dehydrogenase or formate dehydrogenase, the synthesis of chiral diaryl alcohol intermediates of various antihistamines may be achieved. Compared with the prior art, a method for preparing diaryl chiral alcohols through asymmetric catalytic reduction using the alcohol dehydrogenase of the present disclosure has the advantages of simple and convenient operation, high substrate concentration, complete reaction and high product purity, and has great industrial application prospects.

Abstract: Disclosed is an alcohol dehydrogenase mutant and application thereof in cofactor regeneration, and belongs to the technical fields of enzyme engineering and bioengineering. The alcohol dehydrogenase mutant is obtained by mutating valine at position 84 and/or tyrosine at position 127 in alcohol dehydrogenase having an original amino acid sequence as set forth in SEQ ID No. 1. The alcohol dehydrogenase mutant has high activity for a variety of alcohol co-substrates, and can catalyze these enzyme co-substrates for the regeneration of cofactor NADPH. Compared with the wild-type alcohol dehydrogenase KpADH, the alcohol dehydrogenase mutant has higher activity and catalytic efficiency, and for co-substrate 1,4-butanediol, its kcat value can be up to 75.9 min?1, its kcat/Km value can be up to 2009 min?1·M?1, and its Km value can be as low as 11.3 mM. Therefore, the alcohol dehydrogenase mutant has a higher value in industrial application.

Abstract: The present disclosure discloses an alcohol dehydrogenase mutant and application thereof in synthesis of diaryl chiral alcohols, and belongs to the technical field of bioengineering. The alcohol dehydrogenase mutant of the present disclosure has excellent catalytic activity and stereoselectivity, and may efficiently catalyze the preparation of a series of chiral diaryl alcohols in R- and S-configurations. By coupling alcohol dehydrogenase of the present disclosure to glucose dehydrogenase or formate dehydrogenase, the synthesis of chiral diaryl alcohol intermediates of various antihistamines may be achieved. Compared with the prior art, a method for preparing diaryl chiral alcohols through asymmetric catalytic reduction using the alcohol dehydrogenase of the present disclosure has the advantages of simple and convenient operation, high substrate concentration, complete reaction and high product purity, and has great industrial application prospects.

Abstract: The present disclosure discloses an alcohol dehydrogenase mutant and application thereof in synthesis of diaryl chiral alcohols, and belongs to the technical field of bioengineering. The alcohol dehydrogenase mutant of the present disclosure has excellent catalytic activity and stereoselectivity, and may efficiently catalyze the preparation of a series of chiral diaryl alcohols in R- and S-configurations. By coupling alcohol dehydrogenase of the present disclosure to glucose dehydrogenase or formate dehydrogenase, the synthesis of chiral diaryl alcohol intermediates of various antihistamines may be achieved. Compared with the prior art, a method for preparing diaryl chiral alcohols through asymmetric catalytic reduction using the alcohol dehydrogenase of the present disclosure has the advantages of simple and convenient operation, high substrate concentration, complete reaction and high product purity, and has great industrial application prospects.

Abstract: The present disclosure discloses an alcohol dehydrogenase mutant and application thereof in synthesis of diaryl chiral alcohols, and belongs to the technical field of bioengineering. The alcohol dehydrogenase mutant of the present disclosure has excellent catalytic activity and stereoselectivity, and may efficiently catalyze the preparation of a series of chiral diaryl alcohols in R- and S-configurations. By coupling alcohol dehydrogenase of the present disclosure to glucose dehydrogenase or formate dehydrogenase, the synthesis of chiral diaryl alcohol intermediates of various antihistamines may be achieved. Compared with the prior art, a method for preparing diaryl chiral alcohols through asymmetric catalytic reduction using the alcohol dehydrogenase of the present disclosure has the advantages of simple and convenient operation, high substrate concentration, complete reaction and high product purity, and has great industrial application prospects.

Abstract: The present disclosure discloses an alcohol dehydrogenase mutant and application thereof in synthesis of diaryl chiral alcohols, and belongs to the technical field of bioengineering. The alcohol dehydrogenase mutant of the present disclosure has excellent catalytic activity and stereoselectivity, and may efficiently catalyze the preparation of a series of chiral diaryl alcohols in R- and S-configurations. By coupling alcohol dehydrogenase of the present disclosure to glucose dehydrogenase or formate dehydrogenase, the synthesis of chiral diaryl alcohol intermediates of various antihistamines may be achieved. Compared with the prior art, a method for preparing diaryl chiral alcohols through asymmetric catalytic reduction using the alcohol dehydrogenase of the present disclosure has the advantages of simple and convenient operation, high substrate concentration, complete reaction and high product purity, and has great industrial application prospects.