Abstract:
:Recombinant plasmids containing fusion proteins composed of two different modules were constructed and expressed in Escherichia coli. The modules encoded the lactase LacA (LacZ) from the thermophilic bacterium Thermoanaerobacter ethanolicus and the cellulase CelD, a cellulose-binding module (CBM) from Anaerocellum thermophilum. The CelD CBM provides a spontaneous and strong sorption of the fusion proteins onto a cellulose carrier. The enzymatic activities of both the free LacA protein and LacA-CelD CBM fusion proteins immobilized onto the cellulose carrier were assessed. The LacA activity of the fusion protein was dependent upon its position with respect to the CBM. The highest level of lactase activity and stability was observed when the lactase domain was localized at its N terminus. A continuous-flow column reactor of lactase immobilized on a cellulose carrier was constructed, and its activity was assessed. The lactose hydrolysis rate for a 150 mM (5%) solution at a flow rate of 1 reactor volume per min was 75%, which is a value optimal for further whey transformation into glucose/galactose syrup.
journal_name
Appl Environ Microbioljournal_title
Applied and environmental microbiologyauthors
Velikodvorskaya GA,Tikhonova TV,Gurvits ID,Karyagina AS,Lavrova NV,Sergienko OV,Tashlitskii VN,Lunina NA,Lunin VGdoi
10.1128/AEM.01517-10subject
Has Abstractpub_date
2010-12-01 00:00:00pages
8071-5issue
24eissn
0099-2240issn
1098-5336pii
AEM.01517-10journal_volume
76pub_type
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