Asymchem Life Science (tianjin) Co., Ltd

Asymchem Laboratories (tianjin) Co., Ltd.

Jilin Asymchem Laboratories Co., Ltd.

Asymchem Laboratories (fuxin) Co., Ltd.

Tianjin Asymchem Pharmaceutical Co., Ltd.

Tianjin Asymchem Pharmaceuticals Co., Ltd.

Other

China Tiesiju Civil Engineering Group Co., Ltd.

The Third Construction Co., Ltd. of Ctce Group

Asymchem Life Sciences (tianjin) Co., Ltd.

Asymchem Life Science Co., Ltd.

Hao Hong

Jiangping Lu

Gage James

Na Zhang

Wenyan Yu

Kejian Zhang

Yulei Ma

James Gage

Xin Huang

Jiuyuan Li

Xuecheng Jiao

Yanjun Li

Fang Liu

Rui Li

Yibing Cheng

Chaoyong Chen

Xingfu Xu

Litao Shen

Yu Xuan Zhang

Feng Gao

Changfeng Li

Yan Zhou

Shuangyong Liu

Juan Gao

Junlu Wei

Lina Guo

Changming Dong

Xin Hui Zhang

Lei Zhang

Yan Zhang

Enxuan Zhang

Huiyan Mu

Yiming Yang

Fuliang Wei

Xin Zhang

Jiadong Zhao

Yuxia Cui

Sihang Yang

Lihui Liu

Shaohe Li

Gaochao Huang

Xuewu Dong

Rui Yuan

Lin Qin

Gang Huang

Qianchao Yin

Jianlong Yan

Mingmin Hao

Hongying Tian

Shangyong Liu

A method for preventing sudden subsidence of an open caisson in a soft foundation includes the following steps: a position of the open caisson is determined; grouting is carried out to reinforce a foundation of the open caisson; an open caisson manufacturing site is leveled; sections of the open caisson are manufactured and installed; the step of sections of the open caisson are manufactured and installed is repeated until all the sections are manufactured and the open caisson subsides in place as a whole.

Method for preventing sudden subsidence of open caisson in soft foundation

A transaminase mutant and use hereof, the amino acid sequence of the transaminase mutant is an amino acid sequence in which the amino acid sequence as represented by SEQ ID NO: 1 is mutated, the mutated amino acid position being one or more selected from among F89, K193, P243, V234, I262, Q280, V379, R416, A417 and C418. The enzymatic activity and/or stability of the transaminase mutant is improved.

Transaminase mutant and use thereof

Disclosed is a method for continuously synthesizing a propellane compound. The method includes the following steps: using 1,1-dibromo-2,2-bis(chloromethyl)cyclopropane or a derivative thereof as a raw material to form a ring with a lithium metal agent by a continuous reaction, so as to synthesize the propellane compound. A technical scheme of the present disclosure is applied, and a continuous reaction device is used.

Method for continuously synthesizing propellane compound

Provided are a proline hydroxylase and uses thereof. The proline hydroxylase comprises having the amino acid sequence of SEQ ID NO: 2 with the exception of a mutation of one or more amino acids; wherein the mutation of one or more amino acids must comprises E27K, and the mutation of one or more amino acids selected from the group consisting of: H14R, L16N, T25R, F26L, E27K, D30S, S33N, E34N, E34G, E34L, E34S, E34D, Y35W, Y35K, S37W, S37F, S37E, S37N, S37T, S37C, W40F, K41E, D54G, H55Q, S57L, I58T, I58Y, I58A, I58R, I58V, I58S, I58C, K86P, T91A, F95Y, C97Y, I98V, K106V, K106T, K106Q, F111S, K112E, K112R, S154A, K162E, L166M, I118F, I118V, I118R, H119R, H119F, I120V, K123D, K123N, K123Q, K123S, K123I, K123T, T130N, D134G, V135K, N165H, D173G, K209R, I223V and S225A, and having proline hydroxylase activity.

Proline hydroxylase and uses thereof

The present application relates to the technical field of genetic engineering, and provides a monooxygenase mutant, a preparation method and application thereof. The monooxygenase mutant has any one of the amino acid sequences shown in (I) and (II): (I) an amino acid sequence having at least 80% identity with the amino acid sequence shown in SEQ ID NO. 1; and (II) an amino acid sequence obtained by modifying, substituting, deleting, or adding one or several amino acids to the amino acids at 23 to 508 positions of the amino acid sequence shown in SEQ ID NO. 1, the substituting referring to a substitution of 1 to 34 amino acids, wherein the mutant has the activity of monooxygenase.

Monooxygenase mutant, preparation method and application thereof

Provided is an amino acid dehydrogenase mutant. The amino acid sequence of the mutant is obtained by mutating the amino acid sequence shown in SEQ ID NO:1. The mutation includes at least one of the following mutation sites: 64th, 94th, 133rd, 137th, 148th, 168th, 173rd, 183 rd, 191st, 207th, 229th, 248th, 255th and 282nd sites; or the amino acid sequence of the amino acid dehydrogenase mutant is an amino acid sequence having the mutation sites in the mutated amino acid sequence and having a 80% or more homology with the mutated amino acid sequence. The mutant enzyme activity is more than 50 times higher than that of wild amino acid dehydrogenase, and the enzyme specificity is also correspondingly improved.

Amino acid dehydrogenase mutant and use thereof

Disclosed are transaminase mutants and use thereof. The amino acid sequence of the transaminase mutant is obtained by the mutation of the amino acid sequence as shown in SEQ ID NO: 1, and the mutation at least comprises one of the following mutation sites: the 19-th site, the 41-th site, the 43-th site, the 72-th site, the 76-th site, the 92-th site, the 107-th site, the 125-th site, the 132-th site, the 226-th site, the 292-th site, the 295-th site, the 308-th site, and the 332-th site; and the 19-th site is mutated into a serine, the 41-th site is mutated into a serine, the 43-th site is mutated into an asparagine, a glycine in the 72-th site is mutated into a leucine, etc.; or the amino acid sequence of the transaminase mutant has the mutation sites in the mutanted amino acid sequence, and has more than 80% homology to the mutanted amino acid sequence.

The invention provides a transaminase mutant and application thereof, wherein the amino acid sequence of the transaminase mutant is formed after mutation of the amino acid sequence as shown in SEQ ID NO: 1, and mutated amino acid sites comprise T7C+S47C sites. The transaminase mutant having the mutation sites can be further prepared into an immobilized enzyme through an immobilization technology, the immobilized enzyme has relatively high activity and high stability, can be recycled for multiple times, and is applicable to continuous flow reaction in a packed bed.

Transaminase mutant and application thereof

A ketoreductase mutant and use thereof are provided. The amino acid sequence of the ketoreductase mutant is an amino acid sequence obtained by mutation of the amino acid sequence shown in SEQ ID NO: 1, wherein the mutation at least comprises one of the following mutation sites: position 6, position 94, position 96, position 117, position 144, position 156, position 193, position 205, position 224, position 176, position 85 and position 108; alternatively, the amino acid sequence of the ketoreductase mutant has a mutation site in a mutated amino acid sequence and an amino acid sequence having 80% or more homology with the mutated amino acid sequence.

Ketoreductase mutant and application thereof

Provided are a proline hydroxylase and uses thereof. The proline hydroxylase comprises (a) a protein having the amino acid sequence as shown in SEQ ID NO: 2; (b) a protein having an amino acid sequence of SEQ HD NO: 2 with a mutation of one or more amino acids and having a proline hydroxylase activity; or (c) a protein retaining the mutation of one or more amino acids as in (b), and having the proline hydroxylase activity and having at least 78% homology with the amino acid sequence of the protein in (b). Protein having the amino acid sequence as shown in SEQ HD NO: 2 and mutants obtained by genetically engineering have higher catalytic specificity or significantly increased catalytic activity when compared to proline hydroxylases in prior art.

The present invention relates to a preparation method for a chiral intermediate for use in statins, acquired with chloroacetic acid and benzyl alcohol as starting materials via a series of reactions, namely etherification, condensation, substitution, and asymmetric reduction. The preparation method provided in the present invention has a novel route of synthesis, allows an intermediate compound to be introduced conveniently into the chiral center of a glycol via enzyme reduction, and not only is low in costs, but also is reliable in quality. The route of synthesis provided in the present invention uses raw materials of low costs, has an easy to operate process, and provides a final product of great purity and high yield.

Preparation method for chiral intermediate for use in statins

A polymer containing a carboxyl group, a preparation method and an application thereof, a supported catalyst and a preparation method thereof and preparation methods of penem antibiotic intermediate are disclosed. The polymer has high rigidity and hardness, thus the mechanical properties of the polymer is effectively improved. Meanwhile, in the polymer, the carboxyl group is used as a main functional group, and is used as a carrier to prepare, by means of a coordination reaction between the carboxyl group and a heavy metal, a supported metal catalyst which has better connection stability between the metal and the polymer. The above two factors can improve the stability of the supported metal catalyst, such that the catalyst can be recycled without losing the catalytic activity. Meanwhile, loss of a heavy metal active ingredient and production cost can be reduced.

Polymer containing carboxyl group, preparation method and application thereof, supported catalyst and preparation methods thereof and preparation methods of penem antibiotic intermediate

A method for preparing sulfobutyl ether-&#x3b2;-cyclodextrin. &#x3b2;-cyclodextrin and 1,4-sulfobutyrolactone are used as raw materials, and a proper amount of an organic solvent is introduced into an alkaline aqueous solution, so that the solubility of the 1,4-sulfobutyrolactone is increased, and the synthesis yield of the sulfobutyl ether-&#x3b2;-cyclodextrin is improved. Operations including ultrasonic dialysis, active carbon decoloration, freeze-drying and so on are performed on the obtained product solution, so as to obtain a powder product of the sulfobutyl ether-beta-cyclodextrin.

Method for preparing sulfobutyl ether-&#x3b2;-cyclodextrin

The application provides a Diketoreductase (DKR) mutant, its nucleotide coding sequence, and an expression cassette, recombinant vector and host cell containing the sequence, as well as a method for application of the mutant to the preparation of 3R,5S-dicarbonyl compound. An ee value of the obtained 3R,5S-dicarbonyl compound is higher than 99%, and a de value is about 90%. The DKR mutant is a key pharmaceutical intermediate, and particularly provides an efficient catalyst for synthesis of a chiral dicarbonyl hexanoic acid chain of a statin drug.

Diketoreductase mutant and application thereof

A transaminase and a use thereof are provided. The transaminase has the amino acid sequences as shown in SEQ ID NO: 2 or 4, or has at least 80% identity to the amino acid sequences as shown in SEQ ID NO: 2 or 4, or has amino acid sequences which are obtained by the substitution, deletion or addition of one or more amino acids and have an the activity of an omega-transaminase with high stereoselective R-configuration catalytic activity, wherein the high stereoselective refers to the content of one of the stereoisomers being at least about 1.1 times that of the other.

Transaminase and uses thereof

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Tianjin, China

Hao Hong