Stereoselective Promiscuous Reactions Catalyzed by Lipases

Abstract

The ability of lipases to display activity beyond their physiological reactions, so-called “catalytic promiscuity”, has gained increasing interest in the last two decades as an important tool for expanding the application of these enzymes in organic synthesis. Some lipases have been shown to be effective in catalyzing a variety of C-C bond formation reactions and most of the investigations have been directed to the optimization of the products yield through a careful tuning of the experimental parameters. Despite the fact that new stereogenic carbons are formed in many of the tested reactions, the target products have been often obtained in racemic form and examples of an efficient asymmetric induction by the used lipases are quite limited. The aim of this review, mainly focused on those lipase-catalyzed promiscuous reactions in which optically active products have been obtained, is to offer a current state of art together with a perspective in this field of asymmetric synthesis.

Microbial Lipases and Their Potential in the Production of Pharmaceutical Building Blocks

“…This property in an enzyme is known as catalytic promiscuity, although it is not the only promiscuity type ( Figure 6 ). Next, we will focus on the molecular origins of promiscuity in microbial lipases, a topic covered more extensively in the articles of Kazlauzkas [ 129 ], Gupta et al [ 31 , 78 ], Wang et al [ 130 ] and recently for Dewivedee et al [ 131 ] and Patti et al [ 132 ], but with an emphasis on the way in which this property can be modulated so that this versatility may favor lipase application in industry.…”

Promiscuous Lipase-Catalyzed Knoevenagel–Phospha–Michael Reaction for the Synthesis of Antimicrobial β-Phosphono Malonates

“…Generally, lipases are employed to perform three types of reactions: hydrolysis, esterification, and transesterification [ 33 ]. An increasing number of reports on lipase-catalyzed, unconventional reactions have directed attention towards lipase promiscuity [ 34 , 35 , 36 , 37 , 38 ]. As a continuation of our research on seeking new catalytic activities for hydrolases [ 39 , 40 , 41 , 42 , 43 ], we focused our efforts to elaborate sustainable metal-free methods towards desired β-phosphonomalononitriles and β-phosphononitriles ( Figure 2 and Figure 3 ).…”

The Chemistry and Applications of Metal–Organic Frameworks (MOFs) as Industrial Enzyme Immobilization Systems

“…Furthermore, enzymes are biocompatible and biodegradable structures that can be derived from renewable resources [ 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 ]. Unlike conventional organic syntheses, in enzymatic biocatalysis, the reactions of multifunctional molecules are carried out without the need for previous activation or the use of temporary protection for functional groups, resulting in more economical processes and less waste generation [ 29 , 30 , 31 , 32 , 33 , 34 ].…”

“…However, there are clear hurdles to the use of free enzymes, such as degradation (or denaturation) at high temperatures, the need for strict pH control during reactions, their difficult recovery and reuse, high production costs, and their instability under unfavorable environmental conditions, all of which hinder a more widespread implementation across different industries [ 19 , 20 , 22 , 30 , 31 , 35 , 36 , 37 , 38 , 39 ]. A suitable approach used for overcoming these problems is the immobilization of enzymes onto insoluble or solid supports [ 40 , 41 , 42 , 43 , 44 , 45 , 46 , 47 , 48 , 49 , 50 ].…”