Serratiopeptidase: a statistical approach towards enhancement of fermentation and biomass product recovery

Luthra, Umesh; Babu, P. Jawahar; Patel, Yogesh; Ramesh, j; Sharma, Mehak; Majeed, Ilma; Subbiah, Suresh Kumar; Pandiyan, Rajesh

doi:10.1007/s13399-022-02323-5

Cited by 3 publications

(2 citation statements)

References 11 publications

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“…The determination of significant nutrients during the process was carried out at the agitation flask level through a Plackett–Burman experimental design to identify significant components and to determine the optimal combination of nutrients for the production of serratiopeptidase, focusing on proteolytic activity [ 27 ]. Twelve experiments were conducted to assess the relative importance of six variables, namely, silkworm pupae, casein, soybean oil, ammonium dihydrogen phosphate ((NH 4 ) 2 HPO 4 ), zinc chloride (ZnCl 2 ), and calcium chloride (CaCl 2 ·2H 2 O).…”

Section: Methodsmentioning

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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Section: Methodsmentioning

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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“…An appropriate study on dosage of the enzyme must be conducted in order to control levels of the enzyme concentration in plasma, as it was found that the amount of enzymes in blood varies with body mass [ 59 ]. In 2022, it was reported that the enzyme was not able to bind with LOX or to block lipoxygenase-catalyzed biosynthesis of specialized pro-resolving mediators [ 60 ]. A pre-clinical study reported by Jadav et al [ 61 ] indicated that serratiopeptidase was orally effective, and had anti-inflammatory activity which was equivalent to diclofenac sodium in both chronic and acute phases of inflammation.…”

Section: Therapeutic Aspects Of Serratiopeptidasementioning

confidence: 99%

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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A review on pharmaceutical, pharmacological and chemical aspects of serratiopeptidase as anti-inflammatory agent

Kumar¹,

Verma

Abbot³

2023

Materials Today: Proceedings

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Serratiopeptidase: a statistical approach towards enhancement of fermentation and biomass product recovery

Cited by 3 publications

References 11 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

Serratiopeptidase: An integrated View of Multifaceted Therapeutic Enzyme

A review on pharmaceutical, pharmacological and chemical aspects of serratiopeptidase as anti-inflammatory agent

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