期刊
JOURNAL OF BIOTECHNOLOGY
卷 133, 期 3, 页码 403-411出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jbiotec.2007.09.018
关键词
S-layer; enzyme immobilization; self-assembly; extremophilic enzyme; monolayer; nanobiotechnology
资金
- Austrian Science Fund FWF [P 19047] Funding Source: Medline
A fusion protein based on the S-layer protein SbpA from Bacillus sphaericus CCM 2177 and the enzyme laminarinase (LamA) from Pyrococcus furiosus was designed and overexpressed in Escherichia coli. Due to the construction principle, the S-layer fusion protein fully retained the self-assembly capability of the S-layer moiety, while the catalytic domain of LamA remained exposed at the outer surface of the formed protein lattice. The enzyme activity of the S-layer fusion protein monolayer obtained upon recrystallization on silicon wafers, glass slides and different types of polymer membranes was determined colorimetrically and related to the activity of sole LamA that has been immobilized with conventional techniques. LamA aligned within the S-layer fusion protein lattice in a periodic and orientated fashion catalyzed twice the glucose release from the laminarin polysaccharide substrate in comparison to the randomly immobilized enzyme. In combination with the good shelf-life and the high resistance towards temperature and diverse chemicals, these novel composites are regarded a promising approach for site-directed enzyme immobilization. (C) 2007 Elsevier B.V. All rights reserved.
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