Climatic Chamber Stability Tests of Lipase-Catalytic Octyl-Sepharose Systems

• Published in: Catalysts
• Main Authors: Tomasz Siódmiak, Joanna Siódmiak, Rafał Mastalerz, Natalia Kocot, Jacek Dulęba, Gudmundur G. Haraldsson, Dorota Wątróbska-Świetlikowska, Michał Piotr Marszałł
• Format: Text
• Language: English
• Published: Multidisciplinary Digital Publishing Institute 2023
• Subjects: lipase B from Candida antarctica; lipase from Candida rugosa; stability tests; Octyl-Sepharose; immobilization protocols; Rugosa; Antarc*; Antarctica
• Online Access: https://doi.org/10.3390/catal13030501

The application of the climatic chamber presented in this paper to assess the storage stability of immobilized lipases is a new approach characterized by the potential of unifying the study conditions of biocatalysts created in various laboratories. The data achieved from storing lipases in the climatic chambers may be crucial for the chemical and pharmaceutical industry. Our paper describes the developed protocols for immobilization via interfacial activation of lipase B from Candida antarctica (CALB) and lipase OF from Candida rugosa (CRL-OF) on the Octyl-Sepharose CL-4B support. Optimization included buffers with different pH values of 4–9 and a wide range of ionic strength from 5 mM to 700 mM. It has been shown that the optimal medium for the CALB immobilization process on the tested support is a citrate buffer at pH 4 and high ionic strength of 500 mM. Implementing new optimal procedures enabled the hyperactivation of immobilized CALB (recovery activity 116.10 ± 1.70%) under the applicable reaction conditions using olive oil as a substrate. Importantly, CALB storage stability tests performed in a climatic chamber under drastic temperature and humidity conditions proved good stability of the developed biocatalyst (residual activity 218 ± 7.3% of dry form, after 7 days). At the same time, the low storage stability of CRL OF in a climatic chamber was demonstrated. It should be emphasized that the use of a climatic chamber to test the storage stability of a dry form of the studied lipases immobilized on Octyl-Sepharose CL-4B is, to our knowledge, described for the first time in the literature.