Paper Report for: Trodler_2008_J.Chromatogr.A_1179_161
Reference
Title: Rational design of a new one-step purification strategy for Candida antarctica lipase B by ion-exchange chromatography Trodler P, Nieveler J, Rusnak M, Schmid RD, Pleiss J Ref: Journal of Chromatography A, 1179:161, 2008 : PubMed
A fast and efficient one-step method for purification of lipase B from Candida antarctica by ion-exchange chromatography was developed by rational design. The electrostatic properties of the enzyme were calculated and validated by isoelectric focusing and measurement of the titration curve. C. antarctica lipase B shows an unusual pH profile with a broad isoelectric region from pH 4 to 8. At pH 3 C. antarctica lipase B can be bound to a cation-exchange chromatography column and was purified to homogeneity with a purification factor of 2.4. It was stable at pH 3, the residual activity was still 80% after 6 days incubation at 20 degrees C. The broad isoelectric region of C. antarctica lipase B is unique as compared to almost all other alpha/beta-hydrolases which have a well-defined isoelectric point. A search in the lipase engineering database resulted in only one further alpha/beta-hydrolase, the Fusarium solani cutinase, which also has a broad isoelectric region.
        
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Trodler P, Nieveler J, Rusnak M, Schmid RD, Pleiss J (2008) Rational design of a new one-step purification strategy for Candida antarctica lipase B by ion-exchange chromatography Journal of Chromatography A1179: 161-7
Trodler P, Nieveler J, Rusnak M, Schmid RD, Pleiss J (2008) Journal of Chromatography A1179: 161-7