Stability and catalytic properties of lipase immobilized on chitosan encapsulated magnetic nanoparticles cross-linked with genipin and glutaraldehyde

Journal of Chemical Technology & BiotechnologyVolume 91, Issue 5 p. 1359-1367 Research Article Stability and catalytic properties of lipase immobilized on chitosan encapsulated magnetic nanoparticles cross-linked with genipin and glutaraldehyde Yun Liu, Corresponding Author Yun Liu Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029 ChinaCorrespondence to: Yun Liu, Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029 China. E-mail: [email protected] or [email protected]Search for more papers by this authorHua Zhou, Hua Zhou Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029 ChinaEqual contributorsSearch for more papers by this authorLiuyang Wang, Liuyang Wang Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029 ChinaEqual contributorsSearch for more papers by this authorShihui Wang, Shihui Wang Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029 ChinaSearch for more papers by this author Yun Liu, Corresponding Author Yun Liu Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029 ChinaCorrespondence to: Yun Liu, Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029 China. E-mail: [email protected] or [email protected]Search for more papers by this authorHua Zhou, Hua Zhou Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029 ChinaEqual contributorsSearch for more papers by this authorLiuyang Wang, Liuyang Wang Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029 ChinaEqual contributorsSearch for more papers by this authorShihui Wang, Shihui Wang Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029 ChinaSearch for more papers by this author First published: 23 May 2015 https://doi.org/10.1002/jctb.4732Citations: 19 Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Abstract BACKGROUND Among many cross-linkers for enzyme immobilization, genipin (Gen) and glutaraldehyde (Glu) as cross-linkers have been commonly investigated to improve the catalytic performance of enzyme immobilized on chitosan encapsulated magnetic nanoparticles (CMNPs). In this work, we compared the stability and catalytic properties of lipase Candida rugosa (CRL) immobilized on CMNPs cross-linked with Gen and Glu, respectively. The CMNPs were first characterized by TEM, XRD and FT-IR. Moreover, some crucial parameters affecting catalytic performances were optimized for Gen-CMNPs-CRL and Glu-CMNPs-CRL preparation. RESULTS The Gen-CMNPs-CRL showed maximum activity at pH 8.0 and 40°C, and retained more than 95% of its initial activity after 7 days storage at 25°C. After 5 cycles re-usage, Gen-CMNPs-CRL still retained over 80% of its initial activity, while Glu-CMNPs-CRL retained only 26% of its initial activity. Kinetic studies confirmed that Gen-CMNPs-CRL and Glu-CMNPs-CRL presented higher substrate affinity characteristics (Km) than free CRL. FT-IR analysis showed that the variance of β-sheet element in the secondary structure of CRL might contribute to the stability and activity enhancement of Gen-CMNPs-CRL. CONCLUSIONS Gen-CMNPs-CRL showed higher pH, temperature, storage and operational stabilities than Glu-CMNPs-CRL. Thus, genepin is a better promising cross-linker than glutaraldehyde for lipase immobilization on CMNPs. © 2015 Society of Chemical Industry Citing Literature Volume91, Issue5May 2016Pages 1359-1367 RelatedInformation