Improved activity and stability of lipase immobilized in cage-like large pore mesoporous organosilicas

Beitrag in einer Fachzeitschrift


Details zur Publikation

Autor(en): Zhou Z, Inayat A, Schwieger W, Hartmann M, Hartmann M
Zeitschrift: Microporous and Mesoporous Materials
Verlag: Elsevier
Jahr der Veröffentlichung: 2012
Band: 154
Seitenbereich: 133-141
ISSN: 1387-1811


Abstract


Lipase from Thermomyces lanuginosus has been immobilized in different mesoporous organosilicas (PMOs) containing ethane and benzene groups with large cage-like pores. The immobilization of lipase as well as the application of these catalysts in hydrolysis and transesterification reactions is studied in detail. The results show that the structural properties of the support employed have a significant influence on the adsorption capacity. In general, materials with high specific surface areas and pore volumes show high adsorption capacity. However, in the case of monolayer adsorption, the hydrophobicity of the surface has a significant impact on the adsorption efficiency due to strong hydrophobic interactions. Furthermore, the transesterification of vinyl propionate with 1-butanol catalyzed by immobilized lipase was studied. The influence of lipase loading, the effect of water content in the reaction mixture and the influence of different solvents were investigated. The results show that lipase immobilized in the most hydrophobic material (LPbenzene) exhibits excellent catalytic performance, which is attributed to the enhanced interfacial activity of lipase due to the interaction between lipase and the hydrophobic surface of the material. In order to further disclose the influence of the hydrophobic surface on the lipase activity, ATR-FTIR spectroscopy was used to study the secondary structure of lipase immobilized on different supports. The results confirm that a structural transition of entrapped lipase to the open-lid conformation takes place on LPbenzene, which shows that the observed increase in enzymatic activity is triggered by interfacial activation of lipase. (C) 2012 Elsevier Inc. All rights reserved.



FAU-Autoren / FAU-Herausgeber

Hartmann, Martin Prof. Dr.
Professur für Katalyse
Inayat, Alexandra Dr.-Ing.
Lehrstuhl für Chemische Reaktionstechnik
Schwieger, Wilhelm Prof. Dr.
Professur für Technische Chemie (Reaktionstechnik)
Zhou, Zhou Dr.
Interdisziplinäres Zentrum Erlangen Catalysis Resource Center (ECRC)


Zitierweisen

APA:
Zhou, Z., Inayat, A., Schwieger, W., Hartmann, M., & Hartmann, M. (2012). Improved activity and stability of lipase immobilized in cage-like large pore mesoporous organosilicas. Microporous and Mesoporous Materials, 154, 133-141. https://dx.doi.org/10.1016/j.micromeso.2012.01.003

MLA:
Zhou, Zhou, et al. "Improved activity and stability of lipase immobilized in cage-like large pore mesoporous organosilicas." Microporous and Mesoporous Materials 154 (2012): 133-141.

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