Immobilization of active lipase B from Candida antarctica on the surface of polyhydroxyalkanoate inclusions
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  • 作者:Anika C. Jahns (1) (2) (4)
    Bernd H. A. Rehm (1) (2) (3)

    1. Institute of Fundamental Sciences
    ; Massey University ; Private Bag 11222 ; Palmerston North ; 4442 ; New Zealand
    2. PolyBatics Ltd
    ; BioCommerce Centre ; Dairy Farm Road ; Palmerston North ; 4442 ; New Zealand
    4. Department of Medical Biosciences
    ; Ume氓 University ; 90185 ; Ume氓 ; Sweden
    3. MacDiarmid Institute for Advanced Materials and Nanotechnology
    ; Kelburn Parade ; Wellington ; 6140 ; New Zealand
  • 关键词:Beads ; Lipase ; PHA synthase (PhaC) ; Polyhydroxyalkanoate beads
  • 刊名:Biotechnology Letters
  • 出版年:2015
  • 出版时间:April 2015
  • 年:2015
  • 卷:37
  • 期:4
  • 页码:831-835
  • 全文大小:552 KB
  • 参考文献:1. Chen, B, Hu, J, Miller, EM, Xie, W, Cai, M, Gross, RA (2008) Candida antarctica lipase B chemically immobilized on epoxy-activated micro鈥攁nd nanobeads: catalysts for polyester synthesis. Biomacromolecules 9: pp. 463-471 CrossRef
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    4. Jaeger, K-E, Reetz, MT (1998) Microbial lipases form versatile tools for biotechnology. Trends Biotechnol 16: pp. 396-403 CrossRef
    5. Jahns, AC, Haverkamp, RG, Rehm, BHA (2008) Multifunctional inorganic-binding beads self-assembled inside engineered bacteria. Bioconjug Chem 19: pp. 2072-2080 CrossRef
    6. Mateo, C, Palomo, JM, Fernandez-Lorente, G, Guisan, JM, Ferndandez-Lafuente, R (2007) Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme Microb Technol 40: pp. 1451-1463 CrossRef
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    14. Uppenberg, J, Hansen, MT, Patkar, S, Jones, TA (1994) The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Sequence 2: pp. 293-308
  • 刊物类别:Biomedical and Life Sciences
  • 刊物主题:Life Sciences
    Microbiology
    Biotechnology
    Applied Microbiology
    Biochemistry
  • 出版者:Springer Netherlands
  • ISSN:1573-6776
文摘
Polyhydroxyalkanoate (PHA) beads, recombinantly produced in Escherichia coli, were functionalized to display lipase B from Candida antarctica as translational protein fusion. The respective beads were characterized in respect to protein content, functionality, long term storage capacity and re-usability. The direct fusion of the PHA synthase, PhaC, to lipase B yielded active PHA lipase beads capable of hydrolyzing glycerol tributyrate. Lipase B beads showed stable activity over several weeks and re-usability without loss of function.

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