scholarly journals Biotransformation of major ginsenoside Rb1 to pharmacologically active ginsenoside Rg3 through fermentation by Weissella hellenica DC06 in newly developed medium

2016 ◽  
Vol 51 (4) ◽  
pp. 271-278 ◽  
Author(s):  
MA Huq ◽  
SK Akter ◽  
Yeon Ju Kim ◽  
Mohamed El Agamy Farh ◽  
Deok Chun Yang
Keyword(s):  
Low Cost ◽  
Transformation Products ◽  
Ginsenoside Rb1 ◽  
Ginsenoside Rg3 ◽  
Cost Growth ◽  
Yeast Extract Medium ◽  
Extract Medium ◽  
Pharmacologically Active ◽  
Almost All ◽  
Mrs Medium

The study was conducted to develop an edible and low cost growth medium for cultivation of Weissella hellenica DC06, a lactic acid bacteria (LAB) and to study whether, the medium is suitable for bioconversion of major ginsenoside Rb1 into ginsenoside Rg3 through fermentation by W. hellenica DC06. Fourteen different media compositions were investigated to cultivate W. hellenica DC06. Among these, W. hellenica DC06 exhibited the highest growth in media containing 20 g/l radish, 20 g/l glucose, and 10 g/l yeast extract (Medium 3). The optical density of W. hellenica DC06 cultivated in medium 3 reached 1.8 (1.066 x 1010 CFU/ml) after 24 h of incubation. Importantly, the optimized medium was approximately four times cheaper compared to MRS medium. In addition to being economical, the new medium was also edible. Also W. hellenica DC06 showed strong fermentation ability in newly developed medium regarding on major ginsenoside Rb1 biotransformation. Ginsenoside Rb1 was converted into pharmacologically active ginsenoside Rg3 in new medium. In contrast,W. hellenica DC06 showed weak fermentation ability in MRS medium where ginsenoside Rb1 was converted intoginsenoside Rd. The transformation products were analyzed by TLC, and HPLC. Within seven days of fermentation, almost all ginsenoside Rb1 was decomposed and converted into Rg3 in optimized medium. W. hellenica DC06 hydrolyzed two glucose moieties attached to the C-20 position of the ginsenoside Rb1aglyconeand synthesized Rg3 in newly developed medium.Bangladesh J. Sci. Ind. Res. 51(4), 271-278, 2016

scholarly journals Distribution, composition and functions of gelatinous tissues in deep-sea fishes

2017 ◽  
Vol 4 (12) ◽  
pp. 171063 ◽  
Author(s):  
Mackenzie E. Gerringer ◽  
Jeffrey C. Drazen ◽  
Thomas D. Linley ◽  
Adam P. Summers ◽  
Alan J. Jamieson ◽  
...  
Keyword(s):  
Deep Sea ◽  
Low Cost ◽  
Ionic Composition ◽  
Extracellular Fluid ◽  
Fish Locomotion ◽  
Cost Growth ◽  
Locomotory Performance ◽  
Distribution Composition ◽  
Almost All ◽  
And Function

Many deep-sea fishes have a gelatinous layer, or subdermal extracellular matrix, below the skin or around the spine. We document the distribution of gelatinous tissues across fish families (approx. 200 species in ten orders), then review and investigate their composition and function. Gelatinous tissues from nine species were analysed for water content (96.53 ± 1.78% s.d.), ionic composition, osmolality, protein (0.39 ± 0.23%), lipid (0.69 ± 0.56%) and carbohydrate (0.61 ± 0.28%). Results suggest that gelatinous tissues are mostly extracellular fluid, which may allow animals to grow inexpensively. Further, almost all gelatinous tissues floated in cold seawater, thus their lower density than seawater may contribute to buoyancy in some species. We also propose a new hypothesis: gelatinous tissues, which are inexpensive to grow, may sometimes be a method to increase swimming efficiency by fairing the transition from trunk to tail. Such a layer is particularly prominent in hadal snailfishes (Liparidae); therefore, a robotic snailfish model was designed and constructed to analyse the influence of gelatinous tissues on locomotory performance. The model swam faster with a watery layer, representing gelatinous tissue, around the tail than without. Results suggest that the tissues may, in addition to providing buoyancy and low-cost growth, aid deep-sea fish locomotion.

scholarly journals Exploration and Characterization of Novel Glycoside Hydrolases from the Whole Genome of Lactobacillus ginsenosidimutans and Enriched Production of Minor Ginsenoside Rg3(S) by a Recombinant Enzymatic Process

Biomolecules ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 288 ◽  
Author(s):  
Muhammad Zubair Siddiqi ◽  
Sathiyaraj Srinivasan ◽  
Hye Yoon Park ◽  
Wan-Taek Im
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolases ◽  
Vector System ◽  
Whole Genome ◽  
Ginsenoside Rb1 ◽  
Ginsenoside Rg3 ◽  
Food Grade ◽  
Minor Ginsenoside ◽  
Pharmaceutical Industries ◽  
Pharmacologically Active

Background: Several studies have reported that ginsenoside Rg3(S) is effective in treating metastatic diseases, obesity, and various cancers, however, its presence in white ginseng cannot be estimated, and only a limited amount is present in red ginseng. Therefore, the use of recombinant glycosidases from a Generally Recognized As Safe (GRAS) host strain is a promising approach to enhance production of Rg3(S), which may improve nutritional activity, human health, and quality of life. Method: Lactobacillus ginsenosidimutans EMML 3041T, which was isolated from Korean fermented pickle (kimchi), presents ginsenoside-converting abilities. The strain was used to enrich the production of Rg3(S) by fermenting protopanaxadiol (PPD)-mix-type major ginsenosides (Rb1, Rb2, Rc, and Rd) in four different types of food-grade media (1, MRS; 2, Basel Food-Grade medium; 3, Basel Food-Grade medium-I, and 4, Basel Food-Grade medium-II). Due to its tendency to produce Rg3(S), the presence of glycoside hydrolase in Lactobacillus ginsenosidimutans was proposed, the whole genome was sequenced, and the probable glycoside hydrolase gene for ginsenoside conversion was cloned. Results: The L. ginsenosidimutans EMML 3041T strain was whole genome sequenced to identify the target genes. After genome sequencing, 12 sets of glycoside hydrolases were identified, of which seven sets (α,β-glucosidase and α,β-galactosidase) were cloned in Escherichia coli BL21 (DE3) using the pGEX4T-1 vector system. Among the sets of clones, only one clone (BglL.gin-952) showed ginsenoside-transforming abilities. The recombinant BglL.gin-952 comprised 952 amino acid residues and belonged to glycoside hydrolase family 3. The enzyme exhibited optimal activity at 55 °C and a pH of 7.5 and showed a promising conversion ability of major ginsenoside Rb1→Rd→Rg3(S). The recombinant enzyme (GST-BglL.gin-952) was used to mass produce Rg3(S) from major ginsenoside Rb1. Scale-up of production using 50 g of Rb1 resulted in 30 g of Rg3(S) with 74.3% chromatography purity. Conclusion: Our preliminary data demonstrated that this enzyme would be beneficial in the preparation of pharmacologically active minor ginsenoside Rg3(S) in the functional food and pharmaceutical industries.

scholarly journals Podophyllotoxin: History, Recent Advances and Future Prospects

Biomolecules ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 603
Author(s):  
Zinnia Shah ◽  
Umar Farooq Gohar ◽  
Iffat Jamshed ◽  
Aamir Mushtaq ◽  
Hamid Mukhtar ◽  
...  
Keyword(s):  
Structure Optimization ◽  
Cytokine Storm ◽  
Chemotherapeutic Drug ◽  
Future Prospects ◽  
Naturally Occurring ◽  
Pharmacologically Active ◽  
Almost All ◽  
Pharmacologically Active Compounds ◽  
Synthetic Derivatives ◽  
Related Compounds

Podophyllotoxin, along with its various derivatives and congeners are widely recognized as broad-spectrum pharmacologically active compounds. Etoposide, for instance, is the frontline chemotherapeutic drug used against various cancers due to its superior anticancer activity. It has recently been redeveloped for the purpose of treating cytokine storm in COVID-19 patients. Podophyllotoxin and its naturally occurring congeners have low bioavailability and almost all these initially discovered compounds cause systemic toxicity and development of drug resistance. Moreover, the production of synthetic derivatives that could suffice for the clinical limitations of these naturally occurring compounds is not economically feasible. These challenges demanded continuous devotions towards improving the druggability of these drugs and continue to seek structure-optimization strategies. The discovery of renewable sources including microbial origin for podophyllotoxin is another possible approach. This review focuses on the exigency of innovation and research required in the global R&D and pharmaceutical industry for podophyllotoxin and related compounds based on recent scientific findings and market predictions.

Isolation and identification of N2-fixing Pseudomonas associated with wetland rice

1983 ◽  
Vol 29 (8) ◽  
pp. 867-873 ◽  
Author(s):  
W. L. Barraquio ◽  
J. K. Ladha ◽  
I. Watanabe
Keyword(s):  
New Species ◽  
Yeast Extract ◽  
Heterotrophic Bacteria ◽  
Fluorescent Antibody ◽  
Wetland Rice ◽  
Isolation And Identification ◽  
Biochemical Characteristics ◽  
Yeast Extract Medium ◽  
Extract Medium ◽  
A New Species

Semisolid yeast extract medium amended with glucose and tryptic soy agar were used to isolate aerobically N2-fixing (C2H2-reducing) heterotrophic bacteria from the root of wetland rice. The isolates were identified as Pseudomonas by gel immunodiffusion and fluorescent antibody techniques in combination with their morphological, cultural, and biochemical characteristics. The N2-fixing H2-utilizing Pseudomonas described in this paper is a new species.

STRAIN IMPROVEMENT OF A FUNGUS PRODUCING CHITINASE BY A CHEMICAL MUTAGEN

INDIAN DRUGS ◽  
2013 ◽  
Vol 50 (11) ◽  
pp. 25-28
Author(s):  
K Narayanan ◽  
◽  
N.D. Chopade ◽  
V.M Subrahmanyam ◽  
J. Venkata Rao
Keyword(s):  
Protein Content ◽  
Ethidium Bromide ◽  
Yeast Extract ◽  
Wild Strain ◽  
Strain Improvement ◽  
Cost Effective ◽  
Specific Protein ◽  
Chemical Mutagen ◽  
Yeast Extract Medium ◽  
Extract Medium

Microbial chitinases are commercially exploited for their biocontrol properties and generation of useful products from chitinous waste. Availability of highly active chitinolytic enzymes is a major problem. The present study was carried out to improve chitinase production by Aspergillus terreus using a chemical mutagen, ethidium bromide. The organism was cultivated on lactose- yeast extract medium. The production medium consisting of chitin- yeast extract medium was seeded at 10% level. The wild strains were exposed to ethidium bromide in the concentration range 1.5- 6.0 µg/mL. Generally, all the mutated strains showed an improved chitinase yield compared to the control. Highest yield was observed with the strain exposed to 6 µg/mL of ethidium bromide. The yield was 25.03 % higher compared to the wild strain. The mutated strain was slimy in nature. Protein content of the mutated strain decreased by 11%. Ethidium bromide at a concentration of 1.5 µg/mL was considered optional, at which the strain was stable with increase of 21.80 % in enzyme activity and 4.41% increase in protein content. Increased enzyme yield with decreased non-specific protein could be useful in producing cost effective enzyme.

Low-cost growth of AlN using vectored-flow epitaxy for the purpose of water sterilisation in a rural environment

2008 ◽  
Vol 5 (2) ◽  
pp. 559-562 ◽  
Author(s):  
Matthew Branch ◽  
Mike Robinson ◽  
Glyn Jones ◽  
Nigel Mason ◽  
Jim Dixon
Keyword(s):  
Low Cost ◽  
Rural Environment ◽  
Cost Growth

scholarly journals Degradation of methylene blue by natural manganese oxides: kinetics and transformation products

2019 ◽  
Vol 6 (7) ◽  
pp. 190351 ◽  
Author(s):  
Shuangxi Zhou ◽  
Zhiling Du ◽  
Xiuwen Li ◽  
Yunhai Zhang ◽  
Yide He ◽  
...  
Keyword(s):  
Methylene Blue ◽  
Manganese Oxides ◽  
Ph Value ◽  
Low Cost ◽  
Reaction System ◽  
Transformation Products ◽  
Low Ph ◽  
Initial Concentration ◽  
Environmental Material ◽  
High Redox Potential

In this study, natural manganese oxides (MnO x ), an environmental material with high redox potential, were used as a promising low-cost oxidant to degrade the widely used dyestuff methylene blue (MB) in aqueous solution. Although the surface area of MnO x was only 7.17 m 2 g −1 , it performed well in the degradation of MB with a removal percentage of 85.6% at pH 4. It was found that MB was chemically degraded in a low-pH reaction system and the degradation efficiency correlated negatively with the pH value (4–8) and initial concentration of MB (10–50 mg l −1 ), but positively with the dosage of MnO x (1–5 g l −1 ). The degradation of MB fitted well with the second-order kinetics. Mathematical models were also built for the correlation of the kinetic constants with the pH value, the initial concentration of MB and the dosage of MnO x . Furthermore, several transformation products of MB were identified with HPLC-MS, which was linked with the bond energy theory to reveal that the degradation was initiated with demethylation.

scholarly journals The low-cost Shifter microscope stage transforms the speed and robustness of protein crystal harvesting

2021 ◽  
Vol 77 (1) ◽  
pp. 62-74
Author(s):  
Nathan David Wright ◽  
Patrick Collins ◽  
Lizbé Koekemoer ◽  
Tobias Krojer ◽  
Romain Talon ◽  
...  
Keyword(s):  
Low Cost ◽  
Complete Removal ◽  
Protein Crystal ◽  
Fine Motor ◽  
Data Repository ◽  
X Ray ◽  
Fragment Screening ◽  
Protective Cover ◽  
Almost All ◽  
Microscope Stage

Despite the tremendous success of X-ray cryo-crystallography in recent decades, the transfer of crystals from the drops in which they are grown to diffractometer sample mounts remains a manual process in almost all laboratories. Here, the Shifter, a motorized, interactive microscope stage that transforms the entire crystal-mounting workflow from a rate-limiting manual activity to a controllable, high-throughput semi-automated process, is described. By combining the visual acuity and fine motor skills of humans with targeted hardware and software automation, it was possible to transform the speed and robustness of crystal mounting. Control software, triggered by the operator, manoeuvres crystallization plates beneath a clear protective cover, allowing the complete removal of film seals and thereby eliminating the tedium of repetitive seal cutting. The software, either upon request or working from an imported list, controls motors to position crystal drops under a hole in the cover for human mounting at a microscope. The software automatically captures experimental annotations for uploading to the user's data repository, removing the need for manual documentation. The Shifter facilitates mounting rates of 100–240 crystals per hour in a more controlled process than manual mounting, which greatly extends the lifetime of the drops and thus allows a dramatic increase in the number of crystals retrievable from any given drop without loss of X-ray diffraction quality. In 2015, the first in a series of three Shifter devices was deployed as part of the XChem fragment-screening facility at Diamond Light Source, where they have since facilitated the mounting of over 120 000 crystals. The Shifter was engineered to have a simple design, providing a device that could be readily commercialized and widely adopted owing to its low cost. The versatile hardware design allows use beyond fragment screening and protein crystallography.

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