Use of Protease from Bacillus licheniformis as Promiscuous Catalyst for Organic Synthesis: Applications in CC and CN Bond Formation Reactions

Abstract

Commercially available protease from Bacillus licheniformis has been used in different non-conventional biotransformations showing remarkable activity values. The promiscuous behaviour of this enzyme used in the cross-linked enzyme aggregates immobilized form (Alcalase-CLEA ), has been successfully demonstrated for the first time in C À C bond formation processes such as aldol, Henry and Mannich reactions. On the other hand, the Bayllis-Hillman reaction between 4-nitrobenzaldehyde and methyl vinyl ketone occurred through unspecific catalysis. Interestingly, azaMichael addition reactions of secondary amines (di-A C H T U N G T R E N N U N G ethylamine, piperidine and pyrrolidine) to acrylonitrile have been also efficiently catalyzed, observing with diethylamine the most remarkable differences between the enzyme-mediated reaction and the one in the absence of catalyst. Higher reactivities were attained with pyrrolidine demonstrating the versatility of hydrolases in organic synthesis.

C–C Bond formation catalyzed by natural gelatin and collagen proteins

“…At this point, and in order to draw a meaningful comparison with other known biocatalytic systems (i.e., chitosan [29], bovine serum albumin (BSA) [30–31]) we carried out the kinetic analysis of the model reaction for each case [8]. Fig.…”

Application of Deep Eutectic Solvents in Promiscuous Lipase‐Catalysed Aldol Reactions

“…The mixture composed by choline chloride and glycerol (ChCl:Gly, 1:1.5 mol/mol) was selected as initial starting point based on the suitability of this hydrogen bond donor and acceptor in previous studied biotransformations. Three enzymes were initially selected based on their already demonstrated activity as efficient catalyst in the formation of aldol products: Candida antarctica lipase type B (CAL-B), 19 protease from Bacillus lincheniformis (Alcalase-CLEA ® ) 20 and porcine pancreas lipase (PPL). 21 Attempts to follow the biotransformations by GC analysis were unsuccessful since the retro-aldol reaction occurred at the high temperatures used in the analysis, so we decided to fix a 1 day reaction time and measure the conversions using 1 H-NMR analysis.…”

Lipase-Mediated Amidation of Anilines with 1,3-Diketones via C–C Bond Cleavage

“…This process is a representative case of enzyme catalytic promiscuity, which indicates the capability of an enzyme to catalyze chemical reactions different from its physiological reactions [25][26][27]. The in situ generated peracids from lipase-catalyzed perhydrolysis have been successfully utilized in Baeyer-Villiger reactions, the epoxidation of alkenes, and the oxidation of amines [28][29][30][31][32][33].…”