Lipase-Driven Epoxidation Is A Two-Stage Synergistic Process

Abstract

Lipases show high stability in lipophilic solvents and catalyze reactions at the water‐oil interfaces, which are of great industrial interest. One promising application of lipases is the production of epoxides from alkenes and hydrogen peroxide. So far, little attention has been given to uncover the reaction mechanism for this in detail at the molecular level. Here, we present structural and mutational analysis of a lipase from Penicillium camembertii that indicates a two‐stage synergistic mechanism for this reaction. Surprisingly, a mutant devoid of the catalytic serine retains a fraction of activity while histidine from the catalytic triad is absolutely critical to maintain the enzyme activity. Histidine appears to perform a dual‐activation role acting both towards hydrogen peroxide and the catalytic serine. These results thus allow a better understanding of enzymatic epoxidation and engineering of more potent, stable and selective enzymes.

Masking the Peroxidase‐Like Activity of the Molybdenum Disulfide Nanozyme Enables Label‐Free Lipase Detection

“…We believe that the biological function of lipase could interfere with electron transfer between H 2 O 2 and TMB and, therefore, competes with TMB oxidation. As a result, the blue‐colored TMB ox product is not observed, and the reaction of lipase with H 2 O 2 could be the reason for this observation . Later, to test our hypothesis, we performed a postincubation study, in which the inhibitor was added 2 h after the reaction was set with lipase, MoS 2 2D‐nps, TMB, and H 2 O 2 .…”

Epoxidación enzimática de metil ésteres de ácidos grasos de origen vegetal y sus aplicaciones como alternativa para sustituir a los derivados del petróleo

“…Dentro de esta amplia gama de biocatalizadores, las lipasas son las enzimas que mayor atención han recibido debido a que han demostrado ser estables en diversos solventes orgánicos y soportar un amplio rango de temperaturas (Guncheva & Zhiryakova, 2011;Tang et al, 2016). Una de las lipasas con mayor potencial de aplicación en la industria oleoquímica es la lipasa B de Candida antarctica que se encuentra comercialmente disponible en forma inmovilizada dentro de una resina acrílica (Novozym 435) o inmovilizada en un gel de sílica (CALB-sílica) (Milchert, Malarczyk & Kłos, 2015), que ha sido empleada para catalizar la síntesis de un gran número de epóxidos como los derivados de ésteres de aceite de girasol, en donde se obtuvieron rendimientos del 99 % al llevarse a cabo la reacción en un sistema bifásico CH 2 Cl 2 /H 2 O a 30 °C (Schneider, Lara, Bitencourt, Nascimento & dos Santos-Nunes, 2009) o bien, en el caso de la epoxidación de ésteres de aceite de soya en donde la reacción fue llevada a cabo en presencia de tolueno como solvente a 55 °C para obtener productos con 98 % de rendimiento (Lu et al, 2010).…”

Production and immobilization of lipase PCL and its application in synthesis of α-linolenic acid-rich diacylglycerol

“…In this study, the lipase PCL from Penicillieum camembertii was chosen, which has a strong specificity toward MAG and DAG but not TAG. Lipase PCL has been intensively investigated by us and others for various applications such as synthesis of conjugated linoleic acid glycerides (Hernández‐Martín, Hill, & Otero, ; Watanabe et al, ) or as catalyst for esterification and epoxidation reactions (Tang et al, ). Currently, no studies have specifically reported on the synthesis of α‐linolenic acid‐rich diacylglycerol using the lipase PCL.…”

“…Lipase PCL has been intensively investigated by us and others for various applications such as synthesis of conjugated linoleic acid glycerides (Hern andez-Martín, Hill, & Otero, 2009;Watanabe et al, 2002Watanabe et al, , 2004Watanabe et al, , 2005 or as catalyst for esterification and epoxidation reactions (Tang et al, 2016). Currently, no studies have specifically reported on the synthesis of a-linolenic acid-rich diacylglycerol using the lipase PCL.…”