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1373832-85-9

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1373832-85-9 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 1373832-85-9 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,3,7,3,8,3 and 2 respectively; the second part has 2 digits, 8 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 1373832-85:
(9*1)+(8*3)+(7*7)+(6*3)+(5*8)+(4*3)+(3*2)+(2*8)+(1*5)=179
179 % 10 = 9
So 1373832-85-9 is a valid CAS Registry Number.

1373832-85-9Downstream Products

1373832-85-9Relevant academic research and scientific papers

Solvent-free kinetic resolution of primary amines catalyzed by Candida antarctica lipase B: Effect of immobilization and recycling stability

Paeivioe, Mari,Perkioe, Paeivi,Kanerva, Liisa T.

, p. 230 - 236 (2012)

Highly enantioselective (E >200) N-acylation of nine racemic primary amines with isopropyl methoxyacetate in the presence of Candida antarctica lipase B (Novozym 435) has been reported to yield the unreacted (S)-amines (ee ≥98%) and produced the (R)-amides (ee ≥95%) at 50% conversion under solvent-free conditions. One of the amines and the acyl donor have been used in an equimolar ratio at room temperature (23 °C). Under the reaction conditions, the reuse stability of Novozym 435 with 1-phenylethylamine (as a model compound) has been shown to be poor while somewhat improved stability has been observed with an in-house prepared sol-gel CAL-B catalyst.

Artificial plant cell walls as multi-catalyst systems for enzymatic cooperative asymmetric catalysis in non-aqueous media

B?ckvall, Jan-E.,Córdova, Armando,Deiana, Luca,Naidu, Veluru Ramesh,Rafi, Abdolrahim A.,Tai, Cheuk-Wai

supporting information, p. 8814 - 8817 (2021/09/07)

The assembly of cellulose-based artificial plant cell wall (APCW) structures that contain different types of catalysts is a powerful strategy for the development of cascade reactions. Here we disclose an APCW catalytic system containing a lipase enzyme and nanopalladium particles that transform a racemic amine into the corresponding enantiomerically pure amide in high yieldviaa dynamic kinetic resolution.

Chemoenzymatic Dynamic Kinetic Resolution of Primary Benzylic Amines using Pd0-CalB CLEA as a Biohybrid Catalyst

Gustafson, Karl P. J.,G?rbe, Tamás,de Gonzalo-Calvo, Gonzalo,Yuan, Ning,Schreiber, Cynthia L.,Shchukarev, Andrey,Tai, Cheuk-Wai,Persson, Ingmar,Zou, Xiaodong,B?ckvall, Jan-E.

supporting information, p. 9174 - 9179 (2019/07/04)

Herein, we report on the use a biohybrid catalyst consisting of palladium nanoparticles immobilized on cross-linked enzyme aggregates of lipase B of Candida antarctica (CalB CLEA) for the dynamic kinetic resolution (DKR) of benzylic amines. A set of amines were demonstrated to undergo an efficient DKR and the recyclability of the catalysts was studied. Extensive efforts to further elucidate the structure of the catalyst are presented.

An approach to chemoenzymatic DKR of amines in Soxhlet apparatus Dedicated to Prof. Maria José Calhorda on the occasion of her 65th birthday.

Mavrynsky, Denys,Leino, Reko

, p. 161 - 166 (2014/05/06)

The coexistence of thermolabile enzyme and metal catalyst for racemization of amines in chemoenzymatic dynamic kinetic resolution, requiring high temperature of operation, is enabled by carrying out the reaction in modified Soxhlet extraction system. Init

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