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Fig. 2 | BMC Biotechnology

Fig. 2

From: An engineered food-grade Lactococcus lactis strain for production and delivery of heat-labile enterotoxin B subunit to mucosal sites

Fig. 2

Analysis of cell lysate and culture supernatant proteins of the nisin-induced L. lactis strains. The arrows indicate the expressed UreB. a SDS-PAGE. Lane M, protein markers; lane 1, 2, 3, cell lysates of NZ3900, NZ3900/pNZ8149-SP and NZ3900/pNZ8149-SP-ltB, respectively; lane 4, 5, culture supernatant of NZ3900/pNZ8149-SP and NZ3900/pNZ8149-SP-ltB, respectively. These figures showed that the recombinant LTB was expressed as a secreted protein. b Western blotting assays. L. lactis NZ3900/pNZ8149-SP was used as the negative control, while mouse anti-LTB antibodies as the primary antibodies for detection of LTB. Lane M, protein markers; lane 1, 2, culture supernatant of NZ3900/pNZ8149-SP-ltB and NZ3900/pNZ8149-SP, respectively; lane 3, 4, cell lysates of NZ3900/pNZ8149-SP-ltB and NZ3900/pNZ8149-SP, respectively. These figures showed that the expressed LTB was detectable only in the culture supernatant of NZ3900/pNZ8149-SP-ltB, and possessed immunoreactivity with the commercial anti-LTB antibody

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BMC Biotechnology

ISSN: 1472-6750

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