Improved anti-biofilm activity and long-lasting effects of novel serratiopeptidase immobilized on cellulose nanofibers

Rouhani, Maryam; Valizadeh, Vahideh; Bakhshandeh, Haleh; Hosseinzadeh, Sara Ali; Molasalehi, Sara; Atyabi, Seyed Mohammad; Norouzian, Dariush

doi:10.1007/s00253-023-12734-7

Cited by 6 publications

(2 citation statements)

References 34 publications

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“…One of the primary mechanisms of SRPs therapeutic action is most likely its anti-biofilm activity. The anti-biofilm properties of SRP has been documented in an increasing number of research 38 . According to a prior study, SRP considerably boosted the efficiency of antibiotics against bacteria that produce biofilms 8 .…”

Section: Discussionmentioning

confidence: 99%

Preparation and Physicochemical Characterization of Hyaluronic Acid-Lysine Nanogels Containing Serratiopeptidase to Control Biofilm Formation

Mahdiani,

Yazdani,

Khoramipour

et al. 2024

Sci Rep

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Remarkable resistance of bacterial biofilms to high doses of antimicrobials and antibiotics is one of their main challenges. Encapsulation of proteolytic enzymes is one of the suggested strategies to tackle this problem. In this regard, the antibacterial and anti-biofilm activity of biocompatible hyaluronic acid- Lysine nanogels containing serratiopeptidase (SRP-loaded HA-Lys nanogel) was assessed against P. aeruginosa and S. aureus strains. SRP-loaded HA-Lys nanogel was prepared using dropping method and optimized by Box-Behnken experimental design. These formulations were studied for physical characterization, release profile, stability, bioactivity, and anti-biofilm effects. The particle size, polydispersity index (PDI), and surface charge were measured by Zetasizer Nano ZS. The average particle size and zeta potential of the optimum sample were 156 nm and -14.1 mV, respectively. SRP release showed an initial burst followed by sustained release and the highest release was around 77%. Enzyme biological activity data revealed the higher efficiency of free SRP compared to SRP-loaded HA-Lys nanogel. The time-kill assay showed that both forms of SRP-loaded HA-Lys nanogel and blank HA-Lys nanogel showed significant antimicrobial activity against examined bacteria in comparison to the free enzyme. The obtained results demonstrated improved anti-biofilm efficacy and down regulation of tested biofilm genes for both SRP-loaded HA-Lys nanogel 100% and blank HA-Lys nanogel 100% compared to SRP 100%.

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Section: Discussionmentioning

confidence: 99%

Preparation and Physicochemical Characterization of Hyaluronic Acid-Lysine Nanogels Containing Serratiopeptidase to Control Biofilm Formation

Mahdiani,

Yazdani,

Khoramipour

et al. 2024

Sci Rep

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“…In this context, serratiopeptidase, a protease (hydrolytic enzyme), is obtained from bacteria such as Serratia marcescens [ 17 , 18 , 19 ]. This enzyme is renowned for its anti-inflammatory, fibrinolytic, antibiofilm, and analgesic effects [ 20 , 21 , 22 , 23 , 24 , 25 ]. The production of serratiopeptidase has been reported using various agro-industrial residues, such as wheat husk and rice bran [ 7 ].…”

Section: Introductionmentioning

confidence: 99%

Scale-Up of the Fermentation Process for the Production and Purification of Serratiopeptidase Using Silkworm Pupae as a Substrate

Melchor-Moncada,

García-Barco,

Zuluaga-Vélez

et al. 2024

MPs

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Serratiopeptidase, a bacterial metalloprotease known for its pain-relieving and anti-inflammatory properties, can be produced through fermentation with S. marcescens. This study aimed to identify key factors related to nutrient composition and physicochemical conditions for production in Erlenmeyer flasks and to scale up the mixture to a bioreactor to obtain the maximum proteolytic activity. A Plackett–Burman design was used to determine whether the presence of silkworm pupae (at 1.5%) was a significant parameter for serratiopeptidase production. Along with the variables pH, temperature, and time, they were optimized using a Taguchi experimental design, resulting in values of 7, 25 °C, and 36 h, respectively. Scaling up with a kLa of 25.45 ± 3.12 h−1 showed the highest serratiopeptidase production at 24 h. A factorial design was used for ultrafiltration, resulting in an LMH (liters per square meter per hour) of 960 L/m2h, a TMP (transmembrane pressure) of 15 psi, and a concentration factor of five, with a specific activity of 24,325.81 ± 1515.69 U/mg. Afterward, the retentate was purified using strong anion exchange chromatography and ultrafiltration, yielding a 19.94 ± 3.07% recovery and a purification factor of 1.59 ± 0.31. In conclusion, waste from the sericulture industry can be used for serratiopeptidase production.

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An up-to-date review of biomedical applications of serratiopeptidase and its biobetter derivatives as a multi-potential metalloprotease

Hosseini,

Azizi,

Nojoumi

et al. 2024

Arch Microbiol

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Improved anti-biofilm activity and long-lasting effects of novel serratiopeptidase immobilized on cellulose nanofibers

Cited by 6 publications

References 34 publications

Preparation and Physicochemical Characterization of Hyaluronic Acid-Lysine Nanogels Containing Serratiopeptidase to Control Biofilm Formation

Preparation and Physicochemical Characterization of Hyaluronic Acid-Lysine Nanogels Containing Serratiopeptidase to Control Biofilm Formation

Scale-Up of the Fermentation Process for the Production and Purification of Serratiopeptidase Using Silkworm Pupae as a Substrate

An up-to-date review of biomedical applications of serratiopeptidase and its biobetter derivatives as a multi-potential metalloprotease

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