Multi-Mechanism Biofilm Interaction for Microbial Balance and GI Ecosystem Resilience*
What It Does
Biofilm Neutralizer* is formulated to support gastrointestinal microbiome balance by targeting the complex structure of microbial biofilms.* Designed to interact with the physical and chemical matrix that protects entrenched microbial communities, this formula promotes microbial diversity, tissue access, and immune recognition.*
How It Works
• Serrapeptidase (metalloprotease): Interacts with structural proteins within biofilms and their formation via distinct catalytic (Ncat) and regulatory (Crtx) domains.* Demonstrated systemic fibrinolytic and biofilm-interaction activity without harming human tissue.*[1–4]
• Trypsin (serine protease): Affects biofilm adhesion to tissue and matrix viscosity, aiding in immune access and microbial turnover; shown to enter circulation intact after oral ingestion.*[5,6]
• Alpha-Lipoic Acid (ALA): Provides antioxidant activity, modulates immune signaling, supports glutathione production, and may enhance hydrogen sulfide signaling which is a novel player in host defense.*[7]
• EDTA (Calcium Disodium Salt): Chelates matrix-stabilizing metal ions (e.g., calcium, magnesium, iron), weakening cross-linking in the biofilm and supporting immune penetration while preserving serum calcium levels.*[8–12]
Who It’s For
Formulated for individuals seeking targeted support for microbial diversity and gastrointestinal resilience.*
Special Features
Combines clinically relevant proteolytic enzymes, chelators, and redox modulators in a delayed-release capsule to affect the structural defenses of biofilm communities.*
Support GI microbial balance and immune visibility with this precision-targeted, multi-pathway formula.*
References
1. Jadhav SB, et al. Biotechnol Rep (Amst). 2020;28:e00544. doi:10.1016/j.btre.2020.e00544
2. Srivastava V, et al. Biochim Biophys Acta Proteins Proteom. 2025;1873(1):141046. doi:10.1016/j.bbapap.2024.141046
3. Nair SR, C SD. Biomolecules. 2022;12(10):1468. doi:10.3390/biom12101468
4. Lister JL, et al. Front Cell Infect Microbiol. 2014;4:178. doi:10.3389/fcimb.2014.00178
5. Zhou J, et al. Front Microbiol. 2022;13:951291. doi:10.3389/fmicb.2022.951291
6. Banar M, et al. PLoS One. 2016;11(10):e0164622. doi:10.1371/journal.pone.0164622
7. Shahid A, et al. Curr Issues Mol Biol. 2023;47(5):322. doi:10.3390/cimb47050322
8. Jiang Y, et al. Microorganisms. 2020;8(8):1222. doi:10.3390/microorganisms8081222
9. Wu RX, et al. Colloids Surf B Biointerfaces. 2022;220:112972. doi:10.1016/j.colsurfb.2022.112972
10. Sivaranjani M, et al. J Glob Antimicrob Resist. 2021;24:148–157. doi:10.1016/j.jgar.2020.12.002
11. Sapi E, et al. PLoS One. 2012;7(10):e48277. doi:10.1371/journal.pone.0048277
12. Finnegan S, Percival SL. Adv Wound Care (New Rochelle). 2015;4(7):415–421. doi:10.1089/wound.2014.0577
