Immobilization of lipases on porous polypropylene: Reduction in esterification efficiency at low loading

• Published in: Journal of the American Oil Chemists' Society
• Main Authors: Bosley, John A., Peilow, Alan D.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 1997
• Subjects: Antarc*; Antarctica
• Online Access: http://dx.doi.org/10.1007/s11746-997-0153-6; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1007%2Fs11746-997-0153-6; https://onlinelibrary.wiley.com/doi/full/10.1007/s11746-997-0153-6

Abstract Rhizomucor miehei, Humicola sp., Rhizopus niveus , and Candida antarctica B lipases were immobilized by physical adsorption onto a macroporous polypropylene support. In an esterification reaction, the enzyme efficiency, and therefore cost‐effectiveness, is greatly affected by enzyme loading, with an apparent suppression of efficiency at low lipase loadings for both R. miehei and Humicola sp. lipases. This results in the appearance of a pronounced maximum in the efficiency‐loading relationship at approximately 100,000 lipase units (LU)/g for R. miehei lipase (10% of its saturation loading) and at approximately 200,000 LU/g for Humicola sp. lipase (50% of its saturation loading). The other lipases studied do not show similar trends. At low loadings, only a small portion of the surface area is occupied and gives the lipase the opportunity to spread; it is hypothesized that the reduction in efficiency at low loadings is due to a distortion of the active molecular conformation caused by the lipase maximizing its contact with the support as a result of its high affinityfor the support surface. The relationship between efficiency and loading was different for each of the lipases studied, which may reflect both differences in the strength of the affinity of the lipase for the support and in the ease at which the molecular conformation of the lipase can be distorted.