In vitro Studies on Stimulation of Gymnemic Acid Production using Fungal Elicitor in Suspension and Bioreactor based Cell Cultures of Gymnema sylvestre R.Br.

Gymnemic acids have become a valuable drug in diabetes treatment due to their potent antidiabetic activity. These compounds are extracted commercially from large quantities of Gymnema sylvestre. Since the intact plant contains low concentrations of active compound, plant cell cultures have employed as an alternative to produce large amounts of these secondary metabolites. Moreover using a bioelicitor the secondary metabolite production can be increased. The objective of this study was to develop a rapid system for the enhanced production of gymnemic acid. Aspergillus niger cell extract was used as an elicitor to stimulate the production of secondary metabolite. Comparatively 9 fold increase of gymnemic acid yield was obtained in elicited cultures

Molecular identification of autochthonous bacterial fibrinolytic protein producers from fermentative food preparations

154-162The current study investigates screening, isolation and characterization of fibrinolytic enzyme producing autochthonous bacteria from fermented foods. About 21 different fermented food samples were screened for fibrinolytic protease producing bacteria. Procured and prepared samples were homogenized, serially diluted and plated onto nutrient agar and soybean casein digest agar medium. A total number of 89 isolates were isolated and screened for caseinolytic and fibrinolytic activities. Out of those 89 isolates, nineteen were found to be potent protease producers. Amongst those isolates MS2, MS3, MS4 and MS9 had notable fibrinolytic activities as well. These isolates were subjected for biochemical and molecular characterization to determine their taxonomy and phylogeny. The strain with highest fibrinolytic potency was found to be Bacillus subtilis VITMS2 isolated from fermented milk of Vigna unguiculata. The clot lysing ability of the selected potent strain B. subtilis was found to be 79.98%. The total and specific activity of the same was found to be 788.82 U/mL and 41.73 U/mg, respectively. Other strains with comparatively low fibrinolytic activity were Pseudomonas aeruginosa VITMS3, Bacillus sp VITMS4 and Alcaligenes sp. VITMS9

Serratiopeptidase: An integrated View of Multifaceted Therapeutic Enzyme

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

Formulation of cost-effective medium and optimization studies for enhanced production of rapamycin

Abstract Background Enhancing rapamycin production using a cost-effective medium is crucial for wider accessibility, reduced manufacturing costs, sustainable pharmaceutical practices, and advancements in therapeutic applications. It promotes global health, biotechnological innovation, research collaboration, and societal well-being through affordable and effective treatments. This study focuses on the development of a novel cost-effective production medium for the synthesis of rapamycin from Streptomyces hygroscopicus. Results In the initial screening, more rapamycin production was observed in medium A. Initially, the organism produced 10 µg/mL rapamycin. Based on the OFT results, a novel cost-effective medium composition was designed, incorporating soyabean, sugarcane juice, and dried tomato components. Using RSM, soyabean and tomato was found to be more significant in rapamycin production than sugarcane. In the optimized medium, the production of rapamycin increased significantly to 24 µg/mL. Furthermore, a comparative analysis of the growth kinetics between the production normal medium (referred to as production medium A) and the newly optimized cost-effective production medium revealed that the optimized cost-effective production medium significantly enhanced the production of rapamycin. Conclusion Overall, this study demonstrates the successful development of a cost-effective production medium for rapamycin synthesis from S. hygroscopicus. The findings highlight the potential of using a cost-effective medium to enhance the production of a valuable secondary metabolite, rapamycin, while reducing production costs

Acid stable α-amylase from Pseudomonas balearica VITPS19—Production, purification and characterization

In the present study, α-amylase from Pseudomonas balearica VITPS19 isolated from Kolathur, Tamil Nadu, India was studied. Initially, one factor at a time (OFAT) approach was used to optimize the medium parameters like pH, temperature, carbon and nitrogen sources and the presence of metal ions to enhance the amylase activity. After the optimization, 6.5-fold increase in the enzyme production was observed. Enzyme purification was carried out in three stages. The molecular weight of purified α-amylase was estimated to be 47 kDa.The optimum activity for the purified enzyme was observed at pH 6 in 0.1 M phosphate buffer at 25 ± 2 °C and the activity is enhanced in the presence of ions like Mn2+, Mo6+, Na+, Mg2+and Zn2+ and was inhibited in the presence of Hg2+ ions. Compounds such as Sodium dodecyl sulfate (SDS), Ethylenediaminetetraacetic acid (EDTA), urea and β- mercaptoethanol reduced the amylase activity. The Km and Vmax of the α-amylase was estimated to be 45.23 mM and 20.83 U/mL, respectively

Additional file 1 of Formulation of cost-effective medium and optimization studies for enhanced production of rapamycin

Supplementary Material

BRAZILIAN ARCHIVES OF BIOLOGY AND TECHNOLOGY A N I N T E R N A T I O N A L J O U R N A L Antimicrobial, Antioxidant and Cytotoxic Activity of Marine Streptomyces parvulus VITJS11 Crude Extract

ABSTRAC

Antimicrobial, Antioxidant and Cytotoxic Activity of MarineStreptomyces parvulus VITJS11 Crude Extract

The main aim of the study was to evaluate the bioactive properties of ethyl acetate crude extract of Streptomyces parvulus VITJS11 with a view to assess their therapeutic potential. The biological activity of ethyl acetate extract was tested against fungal and bacterial pathogens. The free radical scavenging potential of the crude extract was determined by DPPH assay. The chemo preventive properties of S. parvulus VITJS11 ethyl acetate extract was examined by MTT assay on HepG2 cells. The morphological, physiological and the biochemical properties of the strain S. parvulus VITJS11 was confirmed by conventional methods. Genotypic characterization was done using 16S r-DNA partial gene amplification and sequencing. The authenticity of the crude chemical constitutes were determined by the GC-MS. The ethyl acetate extract of VITJS11 showed maximum antifungal activity against three Aspergillus species and prominent antibacterial activity against two Gram positive and Gram negative bacteria at 20 mg/mL. The antioxidant potential of the crude extract exhibited strong reducing power activity at 5mg/ mL with 85% inhibition and the cytotoxic effect was found with IC50 of 500µg/ mL on HepG2 cell lines. The GC-MS analysis and the chromatogram patterns revealed 16 peaks, indicating the presence of bioactive constituents, which included several important organic compounds, namely 9-(2',2'-dimethylpropanoilhydrazono)-3,6-dichloro-2,7-Bis-[2-(diethylamino)-ethoxy]fluorine (23.1) Dotriacontylpentafluoropropionate,(25.0) Octadecanoic acid, (20.0); Trans-2-methyl-4-n-butylthiane, S, S-dioxide.(19.0). The results showed the benefit of ethyl acetate extract from S. parvulus VITJS11 in treating microbial infections and indicated their broad spectrum of activity with beneficial virtues for therapeutic use

Novel Fibrinolytic Protease Producing Streptomyces radiopugnans VITSD8 from Marine Sponges

Fibrinolytic enzymes have received more attention due to their medicinal potential for thrombolytic diseases. The aim of this study is to characterize the in vitro fibrinolytic nature of purified protease producing Streptomyces radiopugnans VITSD8 from marine brown tube sponges Agelas conifera. Three varieties of sponge were collected from the Rameshwaram Sea coast, Tamil Nadu, India. The fibrinolytic activity of Streptomyces sp. was screened and determined by casein plasminogen plate and fibrin plate methods respectively. The crude caseinolytic protease was purified using ammonium sulfate fractionation, affinity and ion-exchange chromatography. Based on the morphological, biochemical, and molecular characterization, the isolate VITSD8 was confirmed as Streptomyces radiopugnans. Maltose and peptone were found to be the best carbon and nitrogen sources for the production of fibrinolytic protease. The carbon and nitrogen source peptone showed (781 U/mL) enzyme activity. The optimum pH and temperature for fibrinolytic protease production was found to be 7.0 and 33 °C respectively. The purified enzyme showed a maximum specific activity of 3891 U. The blood clot lysis activity was compared with the standard, and it was concluded that a minimum of 0.18 U (10 µL) of purified protease was required to dissolve the blood clot. This is the first report which exploits the fibrinolytic protease activity of Streptomyces radiopugnans VITSD8 extracted from a marine sponge. Hence the investigation suggests a potential benefit of purified fibrinolytic protease which will serve as an excellent clot buster alternative