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.
The taxonomic position of novel bianthraquinone antibiotic producer
Streptomyces
strain RA-WS2, a soil isolate from Shivalik region of NW Himalayas, India, has been described. The isolate produces ...Setomimycin as a major secondary metabolite under defined submerged fermentation conditions. 16S rRNA partial gene sequencing of the isolate indicated its closest similarity (99.4%) with
Streptomyces cyaneochromogenes
, followed by
Streptomyces aquilus.
However
,
the morphological characteristics i.e. colony colour, mycelium and spore chain arrangement were found to be close to
Streptomyces aquilus.
Therefore, a polyphasic approach was used for taxonomic positioning of the isolate. The Whole genome based similarity with 88.4% dDDH value, 98.65% ANI and 96.99% AAI value indicated its closest identity with
Streptomyces justiciae
. The taxonomic characteristics such as white colony with smooth surface, cylindrical spores arranged in straight chain, diffusible melanin production, high salt tolerance, 16S rRNA gene sequencing and phylogenomic studies, led to the identification of the strain as
Streptomyces justiciae
RA-WS2. The predicted biosynthetic gene clusters further confirmed the presence of the BGC for setomimycin biosynthesis in
Streptomyces justiciae
strain RA-WS2.
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.
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