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Synthetic activity enhancement of membrane-bound lipase from Rhizopus chinensis by pretreatment with isooctane

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Abstract

The cell-bound lipase from Rhizopus chinensis CCTCC M201021 with high catalysis ability for ester synthesis was located as a membrane-bound lipase by the treatments of Yatalase™ firstly. In order to improve its synthetic activity in non-aqueous phase, the pretreatments of this enzyme with various organic solvents were investigated. The pretreatment with isooctane improved evidently the lipase synthetic activity, resulting in about 139% in relative synthetic activity and 115% in activity recovery. The morphological changes of mycelia caused by organic solvent pretreatments could influence the exposure of the membrane-bound enzyme from mycelia and the exhibition of the lipase activity. The pretreatment conditions with isooctane and acetone were further investigated, and the optimum effect was obtained by the isooctane pretreatment at 4°C for 1 h, resulting in 156% in relative synthetic activity and 126% in activity recovery. When the pretreated lipases were employed as catalysts for the esterification production of ethyl hexanoate in heptane, higher initial reaction rate and higher final molar conversion were obtained using the lipase pretreated with isooctane, compared with the untreated lyophilized one. This result suggested that the pretreatment of the membrane-bound lipase with isooctane could be an effective method to substitute the lyophilization for preparing biocatalysts used in non-aqueous phase reactions.

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Acknowledgments

This work was financially supported by the National Natural Science Foundation of China (No. 30470046) and the Program for Changjiang Scholars and Innovative Research Team in University (PCSIRT) under IRT0532.

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Correspondence to Yan Xu.

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Wang, D., Xu, Y. & Teng, Y. Synthetic activity enhancement of membrane-bound lipase from Rhizopus chinensis by pretreatment with isooctane. Bioprocess Biosyst Eng 30, 147–155 (2007). https://doi.org/10.1007/s00449-006-0097-5

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  • DOI: https://doi.org/10.1007/s00449-006-0097-5

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