Stereoselective oxidation of R-(+)-limonene by chloroperoxidase from Caldariomyces fumago

Abstract

The oxidation of R-(+)-limonene by chloroperoxidase (CPO) from Caldariomyces fumago is reported. The reaction was performed in 60 mM phosphate buffer at pH 3.0 and 6.0, and in the absence and in the presence of chloride ions. In the absence of chloride ions, at both pH values, the reaction was regio and stereoselective with a diasteromeric excess (de) >99% of (1S,2S)-4R-limonene-1,2-diol. On the other hand, when the reaction was carried out in the presence of chloride ions an enhancement in the reaction rate was observed, maintaining the regioselectivity, but not the stereoselectivity (de <5.4). The reaction products under these conditions were identified as (1S,2S)-4R-limonene-1,2-diol and (1R,2R)-4R-limonene-1,2-diol. It seems that in the absence of chloride ions the stereoselectivity is determined by stereospecific interaction of limonene with CPO active site, as supported by docking analysis, while in the presence of potassium chloride the limonene oxidation also occurs by the produced hypochlorite without stereoselectivity.

Immobilization of Chloroperoxidase in Metal Organic Framework and Its Catalytic Performance

“…吸附法 [7,8] [19] , 目前被认为是过氧化物 酶家族中催化活性最广泛的酶之一, 因此 CPO 的应用 范围非常广, 尤其是在不对称有机合成 [20,21] 以及环境污 染物降解 [22,23] 等方面的应用引人瞩目. 衍射峰位相同, 也与文献报道的特征衍射峰相符(2θ＝ 7.4°、12.7°、18.0°) [25] .…”

Enzymatic synthesis of (R)-modafinil by chloroperoxidase-catalyzed enantioselective sulfoxidation of 2-(diphenylmethylthio) acetamide

“…In this work, an enantioselective synthesis protocol was presented by chloroperoxidase (CPO) catalyzed sulfoxidation of 2-(diphenylmethylthio) acetamide. CPO [13][14][15][16], especially, the epoxidation and sulfoxidation catalyzed by CPO cause great interests [17,18]. However, the actual technical application of CPO was limited because CPO is a highly hydrophilic enzyme, but the poor solubility of organic substrates in aqueous solution prohibits the yield.…”

Bienzymatic nanoreactors composed of chloroperoxidase–glucose oxidase on Au@Fe3O4 nanoparticles: Dependence of catalytic performance on the bioarchitecture

“…Chloroperoxidase (CPO), a heme-thiolate protein secreted by the marine fungus Caldariomyces fumago, is recognized as a versatile catalyst for various organic transformations including halogenation, Materials and Design 111 (2016) [414][415][416][417][418][419][420] oxidation, peroxidation, epoxidation and hydroxylation with high enantioselectivity [1][2][3][4]. However, the use of CPO in large-scale industrial applications is often handicapped by a lack of long-term operational stability, difficult recovery and the inability to be recycled [5].…”