Our Top Choice Compound:Methyl 3-phenyl-2-propenoate

Welcome to talk about 103-26-4, If you have any questions, you can contact de los Santos, YL; Chew-Fajardo, YL; Brault, G; Doucet, N or send Email.. SDS of cas: 103-26-4

SDS of cas: 103-26-4. In 2019.0 SCI REP-UK published article about ANTARCTICA-LIPASE-B; DIRECTED EVOLUTION; CINNAMIC ACID; WEB SERVER; CONFORMATIONAL DYNAMICS; SYNTHETIC ACTIVITY; ENZYME; RESIDUE; NETWORK; CYTOSCAPE in [de los Santos, Yossef Lopez; Chew-Fajardo, Ying Lian; Brault, Guillaume; Doucet, Nicolas] Univ Quebec, Inst Natl Rech Sci, Ctr Armand Frappier Sante Biotechnol, 531 Blvd Prairies, Laval, PQ H7V 1B7, Canada; [Doucet, Nicolas] Univ Laval, Quebec Network Res Prot Funct Engn & Applicat, PROTEO, 1045 Ave Med, Quebec City, PQ G1V 0A6, Canada in 2019.0, Cited 76.0. The Name is Methyl 3-phenyl-2-propenoate. Through research, I have a further understanding and discovery of 103-26-4.

A key event in the directed evolution of enzymes is the systematic use of mutagenesis and selection, a process that can give rise to mutant libraries containing millions of protein variants. To this day, the functional analysis and identification of active variants among such high numbers of mutational possibilities is not a trivial task. Here, we describe a combinatorial semi-rational approach to partly overcome this challenge and help design smaller and smarter mutant libraries. By adapting a liquid medium transesterification assay in organic solvent conditions with a combination of virtual docking, iterative saturation mutagenesis, and residue interaction network (RIN) analysis, we engineered lipase B from P. antarctica (CalB) to improve enzyme recognition and activity against the bulky aromatic substrates and flavoring agents methyl cinnamate and methyl salicylate. Substrate-imprinted docking was used to target active-site positions involved in enzyme-substrate and enzyme-product complexes, in addition to identifying ‘hot spots’ most likely to yield active variants. This iterative semi-rational design strategy allowed selection of CalB variants exhibiting increased activity in just two rounds of site-saturation mutagenesis. Beneficial replacements were observed by screening only 0.308% of the theoretical library size, illustrating how semi-rational approaches with targeted diversity can quickly facilitate the discovery of improved activity variants relevant to a number of biotechnological applications.

Welcome to talk about 103-26-4, If you have any questions, you can contact de los Santos, YL; Chew-Fajardo, YL; Brault, G; Doucet, N or send Email.. SDS of cas: 103-26-4

Reference:
Article; Weng, Shiue-Shien; Ke, Chih-Shueh; Chen, Fong-Kuang; Lyu, You-Fu; Lin, Guan-Ying; Tetrahedron; vol. 67; 9; (2011); p. 1640 – 1648;,
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