Lipase-enhanced activity in flavour ester reactions by trapping enzyme conformers in the presence of interfaces

Abstract

In order to improve the lipase‐catalyzed synthesis of flavour esters, we have used the reported strategy of interfacial activation‐based molecular (bio)imprinting [Mingarro et al. 1995. Proc. Natl. Acad. Sci. U.S.A. 92: 3308], later called trapping in the presence of amphiphile interfaces (TPI) [Mingarro et al. 1996. Biochemistry 35: 9935]. Five lipases of fungal and mammalian origin typically used for esterification process have been explored to improve production by TPI treatment. A marked enhancement of enzymatic activity has been observed in all TPI‐treated lipases assayed and the activation factor obtained was up to 90‐fold. The dependence on chain length of acyl donors in the esterification of geranyl alcohol has been investigated, showing clear differences between activated and nonactivated lipase. The results indicate that this rational approach leads to conversion yields that are remarkably higher, not only than its counterpart pH‐optimized control lipase, but also the “protected” lipase by conventional methods (lyoprotectans or salts). We propose this strategy as a promising tool to be used in more industrial biotransformations. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 59:122–127, 1998.

Designing Liquid‐Infused Surfaces for Medical Applications: A Review

“…Such a transition can lead to the creation of interfacial networks over the interface, which can be made stronger by using proteins with more rigid initial internal structural bonding . On a functional level, trapping of some types of enzymes, such as lipases, at a bulk or droplet liquid–liquid interface can also either activate or enhance their catalytic activity . Building on this concept, liquid‐infused surfaces could be used as a way to control the interactions of proteins and other biomolecules at liquid–liquid interfaces for biochemical reactions or molecular synthesis that is easier to handle than bulk liquid–liquid interfaces.…”

Immobilization of lipase B from Candida antarctica on porous styrene–divinylbenzene beads improves butyl acetate synthesis

“…These esters, when biotechnologically produced, are considered natural flavors in many countries, therefore with economical advantages 4. Thus, lipase‐catalyzed esterification is the target of many current researches aiming at finding a suitable biocatalyst to make this process viable in large scale 5–14…”

Synthesis of biologically active molecules by imprinting polymerisation

“…The ability of polymers to enhance the stability and activity of thylakoids and enzymes has previously been demonstrated [13][14][15], though this effect has been ascribed to the inhibition of proteolysis or non-specific stabilisation of the protein structure by restricting unfolding [16]. In our experiments, how ever, we were able to select the molecular target in the photosystem complex for the interaction with MIPs and enhance the biological effect using imprin ting with Dl protein.…”