Serrapeptase 5mg gastro-resistant tablets

Abstract Staphylococcus aureus biofilms are implicated in hospital infections due to elevated antibiotic and host immune system resistance. Molecular components of cell wall including amyloid proteins, peptidoglycans (PGs), and lipoteichoic acid (LTA) are crucial for biofilm formation and tolerance of methicillin-resistant S. aureus (MRSA). Significance of alkaline phosphatases (ALPs) for biofilm formation has been recorded. Serrapeptase (SPT), a protease of Serratia marcescens , possesses antimicrobial properties similar or superior to those of many antibiotics. In the present study, SPT anti-biofilm activity was demonstrated against S. aureus (ATCC 25923, methicillin-susceptible strain, methicillin-susceptible S. aureus (MSSA)) and MRSA (ST80), with IC 50 values of 0.67 μg/mL and 7.70 μg/mL, respectively. SPT affected bacterial viability, causing a maximum inhibition of − 46% and − 27%, respectively. Decreased PGs content at [SPT] ≥ 0.5 μg/mL and ≥ 8 μg/mL was verified for MSSA and MRSA, respectively. In MSSA, LTA levels decreased significantly (up to − 40%) at lower SPT doses but increased at the highest dose of 2 μg/mL, a counter to spectacularly increased cellular and secreted LTA levels in MRSA. SPT also reduced amyloids of both strains. Additionally, intracellular ALP activity decreased in both MSSA and MRSA (up to − 85% and − 89%, respectively), while extracellular activity increased up to + 482% in MSSA and + 267% in MRSA. Altered levels of DING proteins, which are involved in phosphate metabolism, in SPT-treated bacteria, were also demonstrated here, implying impaired phosphorus homeostasis. The differential alterations in the studied molecular aspects underline the differences between MSSA and MRSA and offer new insights in the treatment of resistant bacterial biofilms. Key points • SPT inhibits biofilm formation in methicillin-resistant and methicillin-susceptible S. aureus. • SPT treatment decreases bacterial viability, ALP activity, and cell wall composition. • SPT-treated bacteria present altered levels of phosphate-related DING proteins. Graphical Abstract

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Abstract Pseudomonas aeruginosa is an emerging threat for hospitalized and cystic fibrosis patients. Biofilm, a microbial community embedded in extracellular polymeric substance, fortifies bacteria against the immune system. In biofilms, the expression of functional amyloids is linked with highly aggregative, multi-resistant strains, and chronic infections. Serrapeptase (SPT), a protease possessing similar or superior anti-microbial properties with many antibiotics, presents anti-amyloid potential. However, studies on the employment of SPT against Pseudomonas biofilms and Fap amyloid, or the possible mechanisms of action are scarce. Here, SPT inhibited biofilm formation of P. aeruginosa ATCC 27853 on both plastic and glass surfaces, with an IC 50 of 11.26 µg/mL and 0.27 µg/mL, respectively. The inhibitory effect of SPT on biofilm was also verified with optical microscopy of crystal violet-stained biofilms and with confocal microscopy. Additionally, SPT caused a dose-dependent decrease of bacterial viability (IC 50 of 3.07 µg/mL) as demonstrated by MTT assay. Reduction of bacterial functional amyloids was also demonstrated, employing both fluorescence microscopy with thioflavin T and photometrical determination of Congo-red-positive compounds. Both viability and functional amyloids correlated significantly with biofilm inhibition. Finally, in silico molecular docking studies provided a mechanistic insight into the interaction of SPT with FapC or FapD, proving that both peptides are possible targets of SPT. These results offer new insights into the biofilm formation of P. aeruginosa and potentiate the involvement of SPT in the prevention and eradication of Pseudomonas biofilms. Graphical abstract Key points • Serrapeptase inhibits biofilm formation of P. aeruginosa on plastic and glass. • Biofilm inhibition correlated with reduced viability and functional amyloid levels. • In silico studies indicated that serrapeptase may target FapC and FapD peptides.

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Escherichia coli biofilms are implicated in the development of persistent infections and increased antibiotic resistance, posing a significant challenge in clinical settings. These biofilms enhance bacterial survival by forming protective extracellular matrices, rendering conventional treatments less effective. Serrapeptase (SPT), a proteolytic enzyme, has emerged as a potential anti-biofilm agent due to its ability to degrade biofilm components and disrupt bacterial adhesion. In this study, we report the inhibitory effect of SPT against E. coli biofilm and its effect on key virulence factors. In vitro assays, including crystal violet staining, optical and fluorescence microscopy, and viability measurements, revealed the dose-dependent inhibition of biofilm formation (IC50 = 14.2 ng/mL), reduced biofilm (−92%, 500 ng/mL) and planktonic viability (−45%, 500 ng/mL), and a marked loss of amyloid curli fibers. SPT treatment also lowered the levels of key virulence factors: cellular and secreted lipopolysaccharides (−76%, 8 ng/mL; −94%, 32 ng/mL), flagellin (−63%, 8 ng/mL), and peptidoglycan (−29%, 125 ng/mL). Mechanistically, SPT induced a phosphate-dysregulating response: secreted alkaline phosphatase activity rose (+70%, 125 ng/mL) while cellular DING/PstS proteins declined (−84%, 64 ng/mL), correlating strongly with biofilm inhibition. In silico docking further suggests direct interactions between SPT and the curli subunits CsgA and CsgB, potentially blocking fiber polymerization. Together, these findings position SPT as a powerful non-antibiotic biofilm disruptor against E. coli, offering a promising strategy to undermine bacterial persistence and resistance by targeting both structural matrix components and metabolic regulatory pathways.

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Background/Objectives: Burn injuries present significant treatment challenges due to the intricate nature of the healing process. Bombyx mori L. (silkworm) derivatives, containing healing-promoting proteins such as sericin and fibroin, as well as the anti-inflammatory enzyme serrapeptase, have shown promise as potential healing agents. This study aimed to identify the optimal dosage of silkworm body and gland extracts for burn healing, compare the selected dose’s effectiveness with that of silkworm cocoons, and assess the combined healing effects of a cocoon dressing and a silkworm body extract gel. Methods: An experimental model was employed using hairless SKH-hr2 female mice subjected to standardized second-degree burns. The mice received treatments with various formulations of silkworm body and gland extracts, silkworm cocoons, and a combined application of a cocoon dressing and silkworm body extract gel. Results: The most effective treatments were the cocoon dressing and the combination of cocoon dressing with 60% body extract gel. By Day 20, complete healing (100%) was observed in the 20% and 60% body and gland extract groups, while the cocoon and 60% gland extract groups exhibited 60% healing, significantly higher than the control group (0% healing). Wound contraction analysis showed the greatest reduction in surface area from Day 3 to Day 17 in the cocoon and 60% body extract groups (p < 0.05). Histopathological assessments revealed that the combination group exhibited the least tissue damage (score: 7), compared to the control (score: 10–13). Conclusions: The study highlights the poorly examined therapeutic potential of silkworm body and gland extracts, demonstrating their efficacy in accelerating burn healing. The effects observed by the silkworm cocoon and body extract suggests a novel and promising approach for burn wound management, warranting further clinical exploration.

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