engleski

Influence of ionic strength on lipase immobilization on Eupergit CM

Lipases produces by fungi, yeasts and bacteria have found wide application in industrial scale production of fine chemicals. Besides, they have been found applicable for biodiesel synthesis. However, their use for industrial scale biodiesel production is still in the process of research. The main obstacle for industrial scale implementation is high cost of enzyme due to inability of reuse and/or enzyme stability. This can be improved by use of immobilized enzymes. Therefore, this research investigated immobilization of Thermomyces lanuginosus (TLL) lipase on solid support Eupergit CM. Covalent binding of TLL on Eupergit CM was performed in the presence of phosphate buffered saline (PBS ; pH = 7.5) at three different concentrations 0.01, 0.1 and 1 M, during 12 and 24 hours at 25°C. Immobilization efficiency was monitored by determination of protein concentration in filtrates remained after immobilization. The maximal enzyme retention on solid support, Eupergit CM, was achieved by use of 1M phosphate buffered saline after 24 hours, where 97% of proteins were found covalently bound on Eupergit CM, but significant amount of enzyme (92%) was also found after 12 hours of immobilization. Use of phosphate buffered saline of lower ionic strength resulted with significantly lower enzyme retention. Obtained results indicate importance of ionic strength for immobilization of Thermomyces lanuginosus lipase on Eupergit CM.

biodiesel ; enzyme retention ; Eupergit CM ; immobilization ; Thermomyces lanuginosus lipase

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