Baeyer-Villiger Oxidation of Cyclohexanone in Aqueous Medium with In Situ Generation of Peracid Catalyzed by Perhydrolase CLEA

被引：16

作者：

Chavez, Georgina ^{[1
,2
,3
]}

Rasmussen, Jo-Anne ^{[2
]}

Janssen, Michiel ^{[2
]}

Mamo, Gashaw ^{[1
]}

Hatti-Kaul, Rajni ^{[1
]}

Sheldon, Roger A. ^{[2
]}

机构：

[1] Lund Univ, Dept Biotechnol, S-22100 Lund, Sweden

[2] CLEA Technol BV, NL-2628 XH Delft, Netherlands

[3] Univ Mayor San Andres, Inst Invest Farmaco Bioquim, La Paz 3239, Bolivia

来源：

TOPICS IN CATALYSIS | 2014年 / 57卷 / 05期

关键词：

Perhydrolase; CLEA; Baeyer-Villiger; Oxidation; Epoxidation; Aqueous medium; Caprolactone; CHEMOENZYMATIC EPOXIDATION; HYDROGEN-PEROXIDE; PERACETIC-ACID;

D O I：

10.1007/s11244-013-0190-3

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

A perhydrolase, immobilized as a cross linked enzyme aggregate (CLEA), was employed to catalyze the in situ formation of peracetic acid (PAA) from ethylene glycol diacetate (EGDA) and hydrogen peroxide. The produced PAA was used for the Baeyer-Villiger oxidation of cyclohexanone, which afforded caprolactone in 63 % yield. The effect of type and amount of acyl donor, solvent, pH, temperature and ratio of cyclohexanone to hydrogen peroxide on the production of caprolactone was studied. The highest caprolactone yield was obtained with 100 mM EGDA as the acyl donor at pH 6 and room temperature using a ratio of cyclohexanone to hydrogen peroxide ratio of 1:4. Interestingly, the perhydrolase CLEA exhibited the highest activity in aqueous medium in contrast to the well studied lipase B from Candida antarctica. The perhydrolase CLEA proved to be a very efficient catalyst; the K (m) and V-max values were 118 mM and 56.3 mu mol min(-1), respectively.

引用

页码：349 / 355

页数：7