Table 5 Characterization of Bacillaceae bacteriocins based on their molecular mass and stability towards pH, heat as well as their other physio-chemical property
From: Biomanufacturing process for the production of bacteriocins from Bacillaceae family
Microorganism | Bacteriocin or BLIS | MW (kDa) | pHa | Te (°C)/Ti (min)a | Physio-chemical property | References |
|---|---|---|---|---|---|---|
B. licheniformis | Bacillocin 490 | 2 | 4.5–9 | 100/60 | – | Luca et al. (2002) |
B. licheniformis MKU3 | BLIS | 8 | 3–11 | 100/10 | – | Kayalvizhi and Gunasekaran (2010) |
B. paralicheniformis APC 1576 | Formicin | ~ 3.3–3.4 | – | 100/30 | – | Collins et al. (2016) |
B. mycoides | BLIS | – | 4–11 | 100/10,90/20 | Solubilized in SDS (0.6% wlv) | Basi-Chipalu et al. (2015) |
B. pseudomycoides | Pseudomycoicidin | 2.7 | 2–7 | 100/60 | – | Basi-Chipalu et al. (2015) |
B. thuringiensis subsp. Entomocidus | Entomocin HD110 | 4.8 | – | –/– | Hydrophobic | Cherif et al. (2008) |
B. thuringiensis BMG | Thuricin 7 | 11.6 | – | 98/30 | – | Pacheco-Cano et al. (2014) |
B. thuringiensis | Ticins A1, A3 and A4 | 4 | – | –/– | – | Xin et al. (2015) |
B. thuringiensis | Thuricin 17, tolworthcin 524 | ~ 6 | – | –/– | IEP: 8 | Pacheco-Cano et al. (2014) |
B. thuringiensis | Thurincin H | 3.2 | – | –/– | IEP: 3.7 | Wieckowski et al. (2015) |
B. amyloliquefaciens | Amylolysin, amylocyclicin | 3.3 | 2–9 | 100/60 | – | |
B. amyloliquefaciens An6 | BLIS | 11 | 4–10 | –/– | – | Cavera et al. (2015) |
B. amyloliquefaciens RX7 | Haloduracin-like peptide | 5 | 1–10 | 80/30 | Hydrophobic | |
B. amyloliquefaciens SP-1-13LM | Amysin | 5.2 | 3–9 | 100/60 | – | Kaewklom et al. (2013) |
B. subtilis BS15 | BLIS | 3–5 | 3–9 | 80/30 | Hydrophobic | Alam et al. (2011) |
B. subtilis IH7 | BLIS | 14 | 6–9 | 121/15 | – | Hammami et al. (2011) |
B. subtilis subsp. subtilis H4 | BLIS | 3.3 | 3–10 | –/– | Contains disulfide bridges | Compaoré et al. (2013) |
B. subtilis LFB112 | BLIS | 6.3 | – | –/– | – | Xie et al. (2009) |
B. subtilis R75 | BLIS | 12 | 5–9 | 90/10 | – | Sharma et al. (2011) |
B. subtilis NCIMB 3610 | BLIS | 16 | 6–8.5 | 100/60 | – | Maria et al. (2012) |
B. cereus NS02 | BLIS | 3.5–6 | 3–10 | 100/– | Hydrophobic | Phelan et al. (2013) |
B. cereus | Cerein 8A | 9 | – | 80/30 | – | Dominguez et al. (2007) |
B. cereus | Cerein 7 | 2.9–3.94 | – | –/– | Stimulated by Triton X 100 | Dominguez et al. (2007) |
B. cereus SS28 | BLIS | – | 2–11 | 121/15 | – | Yusra et al. (2014) |
B. cereus LFB 1640 | BLIS | 24.8 | – | 80/30 | – | Leite et al. (2016) |
B. cereus RF140 | BLIS | – | 4–9 | 80/30 | Hydrophobic | Ghanbari et al. (2009) |
Brevibacillus sp. GI-9 | Laterosporulin | 5.6 | 2–10 | 120/15 | No disulfide bridge | Singh et al. (2012) |
Bacillus sp. strain HIL Y-85 | Mersacidin | – | – | –/– | – | Schmitz et al. (2006) |
Bacillus sp. MTCC 43 | BLIS | – | 4–10 | 100/10 | – | Sharma et al. (2009) |
Bacillus and Paenibacillus spp. | SRCAM 602; 1580; 37 | 3.9;3.5;3.2 | 3–9 | 100/15 | – | Svetoch et al. (2005) |
Virgibacillus salexigens | BLIS | 5.3 | – | 121/15 | – | Svetoch et al. (2005) |