Immobilization and characterization of benzoylformate decarboxylase from Pseudomonas putida on spherical silica carrier

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• 作者：Stephanie Peper (1) peper@hsu-hh.de
  Selin Kara (2)
  Wei Sing Long (1)
  Andreas Liese (2)
  Bernd Niemeyer (1)
• 关键词：Immobilization – ; Benzoylformate decarboxylase – ; Silicagel – ; Enantioselectivity
• 刊名：Bioprocess and Biosystems Engineering
• 出版年：2011
• 出版时间：August 2011
• 年：2011
• 卷：34
• 期：6
• 页码：671-680
• 全文大小：397.9 KB
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• 作者单位：1. Institute of Thermodynamics, Helmut-Schmidt-University Hamburg, Holstenhofweg 85, 22043 Hamburg, Germany2. Institute of Technical Biocatalysis, Hamburg University of Technology, Denickestrasse 15, 21073 Hamburg, Germany
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Biotechnology
  Industrial Chemistry and Chemical Engineering
  Industrial and Production Engineering
  Waste Management and Waste Technology
  Waste Water Technology, Water Pollution Control, Water Management and Aquatic Pollution
  Food Science
  
• 出版者：Springer Berlin / Heidelberg
• ISSN：1615-7605

文摘

If an adequate biocatalyst is identified for a specific reaction, immobilization is one possibility to further improve its properties. The immobilization allows easy recycling, improves the enzyme performance, and it often enhances the stability of the enzyme. In this work, the immobilization of the benzoylformate decarboxylase (BFD) variant, BFD A460I-F464I, from Pseudomonas putida was accomplished on spherical silica. Silicagel is characterized by its high mechanical stability, which allows its application in different reactor types without restrictions. The covalently bound enzyme was characterized in terms of its activity, stability, and kinetics for the formation of chiral 2-hydroxypropiophenone (2-HPP) from benzaldehyde and acetaldehyde. Moreover, temperature as well as pressure dependency of immobilized BFD A460I-F464I activity and enantioselectivity were analyzed. The used wide-pore silicagel shows a good accessibility of the immobilized enzyme. The activity of the immobilized BFD A460I-F464I variant was determined to be 70% related to the activity of the free enzyme. Thereby, the enantioselectivity of the enzyme was not influenced by the immobilization. In addition, a pressure-induced change in stereoselectivity was found both for the free and for the immobilized enzyme. With increasing pressure, the enantiomeric excess (ee) of (R)-2-HPP can be increased from 44% (0.1 MPa) to 76% (200 MPa) for the free enzyme and from 43% (0.1 MPa) to 66% (200 MPa) for the immobilized enzyme.