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Application 1027

Screening of immobilized lipases using rotating bed reactors

The SpinChem rotating bed reactor (RBR) has been proven to be a time and labor-efficient tool in the screening of biocatalysts. Here, we present the quick simultaneous screening of six different immobilized lipases for the esterification of lauric acid to propyl laurate using our pre-packed MagRBR lipase screening kit.

The use of enzymes to catalyze the synthesis of organic compounds is an efficient and widely applied science due to the high selectivity and specificity of these biocatalysts. A frequently employed group of biocatalysts is lipases. These enzymes are used to catalyze important steps within the processing of food, production of biofuels as well as in the synthesis of fine chemicals, cosmetics and pharmaceuticals. Reactions mediated by lipases include the hydrolysis of lipids into fatty acids, and the synthesis of esters and amides.

The rotating bed reactor is a tool for screening of biocatalysts and biocatalytic reactions. The RBR consists of a hollow, cylinder, packed with immobilized enzyme that is held in place by filters. This tool is designed to preserve resin integrity and eliminate the need for filtration of the reaction solution.

As the RBR is spun in substrate solution, the solution is repeatedly pushed through the packed bed within by the centrifugal forces created by the rotary movement. This allows soluble substrate to do multiple passages through the bed, leading to fast and convenient reaction screenings.

The process proved fast and simple, as efficient sampling and monitoring of the process was achieved without filtration steps, by keeping the immobilized catalyst confined inside the RBR.

The formation of propyl laurate over time for esterification reactions catalyzed by immobilized lipases CalB (lipase B from Candida antarctica), RM (lipase from Rhizomucor miehei) PS (lipase from Pseudomonas cepacia). In the file you can also see data for CalA (lipase A from Candida antarctica), TL (lipase from Thermomyces lanuginosa), and CR (lipase from Candida rugosa).

The formation of propyl laurate over time for esterification reactions catalyzed by immobilized lipases CalB (lipase B from Candida antarctica), RM (lipase from Rhizomucor miehei) PS (lipase from Pseudomonas cepacia). In the file you can also see data for CalA (lipase A from Candida antarctica), TL (lipase from Thermomyces lanuginosa), and CR (lipase from Candida rugosa).

Industries Pharmaceutical

Topics Biocatalysis, Reaction Screening

Products

Details

Conditions: Six MagRBRs, each packed with 0.5 mL of one of the immobilized enzymes, were spun in parallel on a six-position magnetic plate at 500 rpm for 1 h in preheated (60°C) substrate solution containing lauric acid (8.01 g, 40 mmol/vial), 1-propanol (2.4 g, 40 mmol/vial), and water (0.32 g, 18 mmol/vial). Samples were collected at 0, 10, 20, 30 and 60 min. Analysis of the propyl laurate product was done using GC-FID after 1:50 dilution in heptane containing internal standards (tetradecane). Formation of propyl laurate over time for esterification reactions catalysed by immobilized lipases CalB (lipase B from Candida antarctica), CalA (lipase A from Candida antarctica), TL (lipase from Thermomyces lanuginosa), RM (lipase from Rhizomucor miehei), CR (lipase from Candida rugosa) and PS (lipase from Pseudomonas cepacia).