Isolation and Characterization of Serratiopeptidase Producing Bacteria from Mulberry Phyllosphere

Koul, Diksha; Chander, Devtulya; Manhas, Ravi Singh; Chaubey, Asha

doi:10.1007/s00284-020-02280-0

Cited by 7 publications

(5 citation statements)

References 24 publications

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“…The combined application of these analytical techniques not only confirmed the association between increased proteolytic activity and serratiopeptidase production but also provided valuable insights into the structural integrity and purity of the enzymes, which are essential aspects for further downstream applications and industrial-scale processes. Notably, these results are consistent with reported findings on various metalloproteases isolated from distinct strains of S. marcescens, which have molecular weights within the range of 43 to 60 kDa [26,[54][55][56][57][58][59].…”

Section: Discussionsupporting

confidence: 92%

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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Section: Discussionsupporting

confidence: 92%

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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“…Enzymatic activity was observed using casein as a substrate (Salisbury and Likos, 1972), where S. marcescens VS56 has 12.31 units/mL of active enzyme. When compared with the study of Koul et al, 2021 the isolates S. marcescens MES-4 and S. marcescens MRS-11 from mulberry soil had protease activity of 95 units/mL and 156 units/mL, respectively. Currently, wild or mutant strains of S. marcescens are used to meet the industrial and pharmaceutical need for serratiopeptidase.…”

Section: Discussionmentioning

confidence: 93%

Bioprospecting of serratiopeptidase-producing bacteria from different sources

Nair,

Subathra Devi

2024

Front. Microbiol.

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Anti-inflammatory enzymes have wide applications in the pharmaceutical industry. The objective of this study was to find new and efficient strains for the commercial production of serratiopeptidase enzyme. Vast number of samples were processed for the isolation of potent strains. The experimental treatment includes processing of twenty soil samples, silkworm gut, and sugarcane stem. The total protein and protease activity was estimated by Lowry’s method and casein hydrolysis. The HRBC stabilization assay was performed for finding the anti-inflammatory potential of all strains. The serratiopeptidase production was confirmed by HPLC with the standard. Molecular characterization of selected potent strains was done by 16S rDNA and confirmed the taxonomy. The one step rapid purification of serratiopeptidase was performed by Ultra three phase partitioning method. The clot lysis potential of the Serratia marcescens VS56 was observed by modified Holmstorm method. The results of the study revealed that among the 60 strains, 12 strains were protease-positive on skim milk agar plates and showed significant protease activity. All 12 strains were screened for serratiopeptidase using high-performance liquid chromatography (HPLC) and VS56, VS10, VS12 and VS18 showed a similar retention time (4.66 ± 0.10 min) with standard. The selected potent strain, Serratia marcescens VS56 showed a proteolytic activity of 21.30 units/mL and produced a total protein of 102 mg/mL. The HRBC suspension results also showed a percentage of 94.6 ± 1.00 protection, which was compared to the standard diclofenac. The clot lysis potential of Serratia marcescens VS56 was 53% in 4 h. Furthermore, the molecular weight of the protein was identified to confirm the presence of serratiopeptidase. The study hence contributed successfully to isolating, screening, and identifying a potent producer for serratiopeptidase from an environmental source. This inherent advantage of the strain will undoubtedly contribute much to the coco comm commercial production of serratiopeptidase in the near future.

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“…From different species of Serratia, different molecular sizes of serratiopeptidase were identified ( Figure 2 ). Koul et al [ 46 ] identified two potent producers of serratiopeptidase. Serratia marcescens MES-4, an endophyte, showed 95 U/mL, and Serratia marcescens MRS-11, a soil isolate, showed 156 U/mL of activity [ 46 ].…”

Section: Enzyme Productionmentioning

confidence: 99%

“…Koul et al [ 46 ] identified two potent producers of serratiopeptidase. Serratia marcescens MES-4, an endophyte, showed 95 U/mL, and Serratia marcescens MRS-11, a soil isolate, showed 156 U/mL of activity [ 46 ]. Recently, recombinant expression of serratiopeptidase genes in E. coli was reported by Doshi et al [ 47 ].…”

Section: Enzyme Productionmentioning

confidence: 99%

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Serratiopeptidase: An integrated View of Multifaceted Therapeutic Enzyme

Nair

Devi

2022

Biomolecules

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Microbial products have been used for the treatment of different diseases for many centuries. The serratiopeptidase enzyme provides a new hope for COVID-19-infected patients. Nowadays, anti-inflammatory drugs are easy to obtain at minimal expenditure from microbial sources. Serratia sp. is identified as one of the most efficient bacteria produced from serratiopeptidase. Screening for new and efficient bacterial strains from different sources has been of interest in recent years. Serratiopeptidase remains the most well-known anti-inflammatory drug of choice. Serratiopeptidase is a cheaper and safer anti-inflammatory drug alternative to NSAIDs. The multifaceted properties of serratiopeptidase may lead towards arthritis, diabetes, cancer and thrombolytic treatments. Existing serratiopeptidase treatments in combination with antibiotics are popular in the treatment of postoperative swelling. Although an exclusive number of serratiopeptidase-producing strains have been derived, there is an urge for new recombinant strains to enhance the production of the enzyme. This review explores the properties of serratiopeptidase, different therapeutic aspects, industrial production, and various analytical techniques used in enzyme recovery. In addition, the review highlights the therapeutic and clinical aspects of the serratiopeptidase enzyme to combat COVID-19-induced respiratory syndrome.

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Isolation and Characterization of Serratiopeptidase Producing Bacteria from Mulberry Phyllosphere

Cited by 7 publications

References 24 publications

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

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

Bioprospecting of serratiopeptidase-producing bacteria from different sources

Serratiopeptidase: An integrated View of Multifaceted Therapeutic Enzyme

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