Serratiopeptidase (EC 3.4.24.40), a proteolytic enzyme, is one of the most promising enzymes being used in biopharmaceutical industry. Mulberry phyllosphere, being an unexplored niche for exploration ...of protease production, was chosen for the present study. Protease producing bacteria were isolated from the tissues of mulberry plant as well as its rhizospheric soil. Two protease producing bacteria belonging to
Serratia
genus were found to be potential serratiopeptidase producers. Among them, the endophyte, i.e.,
Serratia marcescens
MES-4 presented 95 Units/mL activity, while the soil isolate i.e.,
Serratia marcescens
MRS-11 presented 156 Units/mL activity.
Serratiopeptidase is a proteolytic enzyme extensively used as an anti-inflammatory and analgesic drug. Present work reports a thermoactive serratiopeptidase from
Serratia marcescens
AD-W2, a soil ...isolate from the North-Western Himalayan region of India. The extracellular metalloprotease has been purified by a simple two-step procedure resulting in a specific activity of 20,492 Units/mg protein with 5.28-fold purification. The molecular mass of the metalloprotease, as determined by SDS-PAGE was ~ 51 kDa. The purified serratiopeptidase presented optimum activity at pH 9.0, temperature 50 °C and stability in wide pH and temperature range. Critical temperature of 50 °C confirmed the thermoactivity of the purified serratiopeptidase. The kinetic studies of the purified serratiopeptidase revealed V
max
and K
m
of 57,256 Units/mL and 1.57 mg/mL, respectively, for casein. The purified serratiopeptidase from
S. marcescens
AD-W2 was found to be 100% identical to serralysin from
Serratia marcescens
ATCC 21074/E-15. The catalytic domain comprising of Zn coordinated with three histidine residues (His192, His196, His202), along with glutamate (Glu193) and tyrosine (Tyr232) residues, further confirmed that the purified protein is identical to serralysin.
Serratiopeptidase, a proteolytic enzyme serves as an important anti-inflammatory and analgesic medication. Present study reports the production and purification of extracellular serratiopeptidase ...from an endophyte, Serratia marcescens MES-4, isolated from Morus rubra. Purification of the enzyme by Ion exchange chromatography led to the specific activity of 13,030 U/mg protein of serratiopeptidase, showcasing about 3.1 fold enhanced activity. The catalytic domain of the purified serratiopeptidase, composed of Zn coordinated with three histidine residues (His 209, His 213, and His 219), along with glutamate (Glu 210) and tyrosine (Tyr 249). The molecular mass, as determined by SDS-PAGE was ∼51 kDa. The purified serratiopeptidase displayed optimal activity at pH 9.0, temperature 50°C. Kinetic studies revealed Vmax and Km values of 33,333 U/mL and 1.66 mg/mL, respectively. Further, optimized conditions for the production of serratiopeptidase by Taguchi design led to the productivity of 87 U/mL/h with 87.9 fold enhanced production as compared to the previous conditions.
•Purification and characterization of serratiopeptidase from the endophyte Serratia marcescens MES-4, isolated from Morus rubra.•Enhancement of serratiopeptidase activity by Taguchi L16 orthogonal array design.•Productivity of 87U/mL/h with 87.9 fold enhanced production was achieved as compared to the previous conditions.
Verbenone is a natural monoterpene present as an essential component in rosemary oil from Rosmarinus officinalis, Verbena triphylla and Eucalyptus globule. Microbial biotransformation of ...monoterpenoids to value-added products has immense industrial potential. This study involves the biotransformation of (-)-verbenone to (-)-10-hydroxyverbenone by a fungus i.e. Talaromyces purpurogenus strain MRS-F13 in fermentation broth during the exponential phase. Biotransformation reaction has been successfully demonstrated at 15 L scale in the bioreactor with 70% conversion within 96 h. The anti-inflammatory activity investigations revealed that (-)-verbenone and its biotransformed product exhibited moderate inhibition of TNF-α and nitric oxide, whereas (-)-10-hydroxyverbenone presented an improved anti-oxidant activity.
Highlights
Talaromyces purpurogenus catalysed biotransformation of (-)-verbenone to (-)-10-hydroxyverbenone has been demonstrated.
Approximately 70% bioconversion was obtained in 96 h in submerged culture at 15L bioreactor scale.
Biotransformed product (-)-10-hydroxyverbenone has shown improved anti-inflammatory activity without cytotoxicity.
Background: COVID-19 pandemic has forced the human population to rethink over the lifestyle and food habits being followed by them. During the current scenario, when cases of more virulent new strain ...are emerging and specific treatment are still underway, we must look back to the Darvin’s theory of “Survival of the fittest” and in order to sustain the pandemic, we must follow the rule “Prevention is better than cure”. Traditional Medicinal System can bring possible solution including prevention and control of COVID-19. Humic substances have been used for antiviral activities, signifying that it has potential applications in the management and prevention of infectious diseases.
Summary: Present article is focused on the assessment of the naturally occurring humic substances, which are major constituents of Shilajit, being used in traditional system of medicine and can be used against for the prevention of COVID-19.
Key message: Humic substances not only improve the immune system, but also have anti-inflammatory, antioxidant and antiviral activities against human RNA viruses. Therefore, while the entire world is preparing to deal with alarming threat of community spread of COVID-19, Humic substances may play a vital role in improving the innate immunity for prevention and management of SARS-CoV-2 infection
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