Lipases in asymmetric transformations: Recent advances in classical kinetic resolution and lipase–metal combinations for dynamic processes

Seddigi, Zaki S.; Malik, M. Shaheer; Ahmed, Saleh A.; Babalghith, Ahmad O.; Kamal, Ähmed

doi:10.1016/j.ccr.2017.08.008

Cited by 92 publications

(64 citation statements)

References 182 publications

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“…Thus, they can be used for catalyzing (trans, inter) esterifications of a wide range of substrates, generally taking advantage of their inherent ability to recognize stereochemistry; indeed, triglycerides possess an stereogenic carbon atom at C2 of the glycerol moiety, provided that fatty acid residues at C1 and C3 are different (in other cases, if the acyl groups at C1 and C3 are the same, C2 is then a pseudo-asymmetric carbon). For this reason, the resolution of racemic mixtures of acids, alcohols, esters, amines or amides, or rather the desymetrization of this type of compounds bearing a prochiral centre, is a very usual process catalyzed by lipases (Cunha et al, 2015;de Miranda et al, 2015;Hoyos et al, 2016;Patel, 2012;Rodríguez-Mata and Gotor-Fernández, 2015;Seddigi et al, 2017). It is worth mentioning that going deeper into the knowledge of the molecular basis explaining the stereochemical recognition of (pro)chiral substrates is also a very attractive research area (Colombo et al, 2000;Cygler et al, 1994;Juhl et al, 2009;Li et al, 2008Li et al, , 2015Park et al, 2009;Rahman et al, 2012;Sin et al, 2009;Toledo et al, 2016;Trodler et al, 2009;Trodler and Pleiss, 2008).…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

Rodrigues

Virgen-Ortíz

Santos

et al. 2019

Biotechnology Advances

481

291

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Lipases are the most widely used enzymes in biocatalysis, and the most utilized method for enzyme immobilization is using hydrophobic supports at low ionic strength. This method allows the one step immobilization, purification, stabilization, and hyperactivation of lipases, and that is the main cause of their popularity. This review focuses on these lipase immobilization supports. First, the advantages of these supports for lipase immobilization will be presented and the likeliest immobilization mechanism (interfacial activation on the support surface) will be revised. Then, its main shortcoming will be discussed: enzyme desorption under certain conditions (such as high temperature, presence of cosolvents or detergent molecules). Methods to overcome this problem include physical or chemical crosslinking of the immobilized enzyme molecules or using heterofunctional supports. Thus, supports containing hydrophobic acyl chain plus epoxy, glutaraldehyde, ionic, vinylsulfone or glyoxyl groups have been designed. This prevents enzyme desorption and improved enzyme stability, but it may have some limitations, that will be discussed and some additional solutions will be proposed (e.g., chemical amination of the enzyme to have a full covalent enzyme-support reaction). These immobilized lipases may be subject to unfolding and refolding strategies to reactivate inactivated enzymes. Finally, these biocatalysts have been used in new strategies for enzyme coimmobilization, where the most stable enzyme could be reutilized after desorption of the least stable one after its inactivation.

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Section: Accepted Manuscriptmentioning

confidence: 99%

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

Rodrigues

Virgen-Ortíz

Santos

et al. 2019

Biotechnology Advances

481

291

View full text Add to dashboard Cite

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“…Lipases are very interesting enzymes in biocatalysis due to their broad substrate specificity, their selectivity and high stability, combined in many instances with a very high enantio or regio selectivity and specificity [1][2][3][4][5][6][7][8][9][10]. Moreover, they can perform their function in a wide diversity of reaction media [11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features

2018

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Eversa is an enzyme recently launched by Novozymes to be used in a free form as biocatalyst in biodiesel production. This paper shows for first time the immobilization of Eversa (a commercial lipase) on octyl and aminated agarose beads and the comparison of the enzyme properties to those of the most used lipase, the isoform B from Candida antarctica (CALB) immobilized on octyl agarose beads. Immobilization on octyl and aminated supports of Eversa has not had a significant effect on enzyme activity versus p-nitrophenyl butyrate (pNPB) under standard conditions (pH 7), but immobilization on octyl agarose beads greatly enhanced the stability of the enzyme under all studied conditions, much more than immobilization on aminated support. Octyl-Eversa was much more stable than octyl-CALB at pH 9, but it was less stable at pH 5. In the presence of 90% acetonitrile or dioxane, octyl-Eversa maintained the activity (even increased the activity) after 45 days of incubation in a similar way to octyl-CALB, but in 90% of methanol, results are much worse, and octyl-CALB became much more stable than Eversa. Coating with PEI has not a clear effect on octyl-Eversa stability, although it affected enzyme specificity and activity response to the changes in the pH. Eversa immobilized octyl supports was more active than CALB versus triacetin or pNPB, but much less active versus methyl mandelate esters. On the other hand, Eversa specificity and response to changes in the medium were greatly modulated by the immobilization protocol or by the coating of the immobilized enzyme with PEI. Thus, Eversa may be a promising biocatalyst for many processes different to the biodiesel production and its properties may be greatly improved following a suitable immobilization protocol, and in some cases is more stable and active than CALB.

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“…The limiting factor of the use of KR is that the desired enantiomer is produced with the maximum yield of 50% at the end of reaction. [32][33][34][35] Figure 3.…”

Section: Enzyme-catalysed Kinetic and Dynamic Kinetic Resolutionsmentioning

confidence: 99%

“…On the basis of the racemising agent, DKR resolutions can be classified into two main groups metal-catalysed or induced by non-metal agents. [32][33][34][35][36][37][38][39] Metal catalysts, e.g. ruthenium, rhodium, palladium, iridium and iron, are commonly used as racemising agents in numerous DKRs, such as the resolution of secondary alcohols.…”

Section: Enzyme-catalysed Kinetic and Dynamic Kinetic Resolutionsmentioning

confidence: 99%

“…[46] Metalcatalysed racemisations of primary [47][48][49][50] and secondary amines [51] were also described through hydrogen transfer between their amine and imine forms. DKRs, in which the enzymatic resolution is induced with a metal catalyst as racemising agent, have been discussed in several reviews [32][33][34][35][36][37][38][39][52][53][54][55][56] and these reactions are no longer treated in the thesis.…”

Section: Enzyme-catalysed Kinetic and Dynamic Kinetic Resolutionsmentioning

confidence: 99%

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Kinetic and dynamic kinetic enzymatic resolutions of tetrahydro-ß-carboline and tetrahydroisoquinoline derivatives

Megyesi¹

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Lipases in asymmetric transformations: Recent advances in classical kinetic resolution and lipase–metal combinations for dynamic processes

Cited by 92 publications

References 182 publications

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features

Kinetic and dynamic kinetic enzymatic resolutions of tetrahydro-ß-carboline and tetrahydroisoquinoline derivatives

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