We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Immobilization of nisin producer Lactococcus lactis strains to chitin with surface-displayed chitin-binding domain.
- Authors
Şimşek, Ömer; Sabanoğlu, Seba; Çon, Ahmet; Karasu, Nihat; Akçelik, Mustafa; Saris, Per
- Abstract
In this study, nisin producer Lactococcus lactis strains displaying cell surface chitin-binding domain (ChBD) and capable of immobilizing to chitin flakes were constructed. To obtain ChBD-based cell immobilization, Usp45 signal sequence with ChBD of chitinase A1 enzyme from Bacillus circulans was fused with different lengths of PrtP (153, 344, and 800 aa) or AcmA (242 aa) anchors derived from L. lactis. According to the whole cell ELISA analysis, ChBD was successfully expressed on the surface of L. lactis cells. Scanning electron microscope observations supported the conclusion of the binding analysis that L. lactis cells expressing the ChBD with long PrtP anchor (800 aa) did bind to chitin surfaces more efficiently than cells with the other ChBD anchors. The attained binding affinity of nisin producers for chitin flakes retained them in the fermentation during medium changes and enabled storage for sequential productions. Initial nisin production was stably maintained with many cycles. These results demonstrate that an efficient immobilization of L. lactis cells to chitin is possible for industrial scale repeated cycle or continuous nisin fermentation.
- Subjects
LACTOCOCCUS lactis; STREPTOCOCCUS uberis; CHITIN; NISIN; ENZYME-linked immunosorbent assay; BACTERIAL growth; SCANNING electron microscopy
- Publication
Applied Microbiology & Biotechnology, 2013, Vol 97, Issue 10, p4577
- ISSN
0175-7598
- Publication type
Article
- DOI
10.1007/s00253-013-4700-9