Abstract
In this study, hydrophobic macroporous resin NKA was employed as matrix for immobilization of free Rhizopus oryzae lipase (ROL). The performance of the immobilized ROL was significantly enhanced. The recovery activity was up to 1,293.78 % and the specific activity increased to 152,914 U/g-protein, which was 46-fold higher than that of the free lipase. Moreover, the immobilized lipase showed higher thermostability and better pH-resistance than its free counterpart. Additionally, three different nonaqueous modification strategies (including bioimprinting, lecithin coating, and lyophilization protection) were further utilized to improve the performance of the immobilized lipase. The corresponding enhancements were 33.68 %, 31.98 %, and 99.86 %. When these modifications were combined together, the activity improved 209.51 %. In order to confirm its practical application, the modified ROL was used to biorefine rapeseed oil deodorizer distillate (RODD) for biodiesel production. The highest conversion yield reached 98.23 %, much close to that (97.46 %) of Novozym 435. The results suggest that the prepared lipase in this study is a promising biocatalyst with high stability, efficiency and operational reusability.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have