Antibacterial activity of crude protein and development of species-specific molecular marker for fungus Ophiocordyceps sobolifera

Biologia ◽  
2020 ◽  
Author(s):  
Sasithorn Thongchai ◽  
Kusavadee Sangdee ◽  
Aphidech Sangdee
Keyword(s):  
Antibacterial Activity ◽  
Molecular Marker ◽  
Crude Protein ◽  
Ophiocordyceps Sobolifera ◽  
Species Specific

Antibacterial Activities of Antibacterial Proteins/Peptides Isolated from Organs and Mucus of Clarias Gariepinus Reared at High Stocking Density

2012 ◽  
Vol 455-456 ◽  
pp. 455-460 ◽  
Author(s):  
Xiao Mei Wang ◽  
Wei Dai ◽  
Ke Zhing Xing ◽  
Tian Jun Li ◽  
Xin Wang
Keyword(s):  
Molecular Weight ◽  
Antibacterial Activity ◽  
Crude Protein ◽  
Clarias Gariepinus ◽  
Gel Filtration ◽  
Stocking Density ◽  
Antibacterial Activities ◽  
Edwardsiella Tarda ◽  
Bacterial Strains ◽  
Sds Page

. Antibacterial proteins/peptides are important parts of the innate immune system in Clarias gariepinus. To examine potential antibacterial proteins/peptides in organs and mucus of C. gariepinus, crude protein/peptide extracts were isolated with ammonium sulfate precipitation from mucus, skin, gill, suprabranchial organ and intestine. Following further extraction using Sephadex G-50 gel filtration chromatography, the proteins/peptides associated with two absorption peaks (AP1 and AP2) were pooled, respectively, and assayed for their antibacterial activities against Escherichia coli, Aeromonas hydrophila and Edwardsiella tarda. The results showed that AP1 and AP2 from all the sampled tissues and mucus at concentration of 100 mg mL-1 exhibited antibacterial activity against the tested bacterial strains. Differences in antibacterial activity were observed among sample extracts. The protein profiles of AP1 obtained by Tricine-SDS-PAGE gel showed a broad range of peptides/proteins, and molecular weight of the mutual abundant peptide obtained was about 27 kDa. Antibacterial activity of AP2 extracted from intestine was due to peptide with molecular weight of 5.5 kDa.

scholarly journals Design, synthesis, and discovery of novel oxindoles bearing 3-heterocycles as species-specific and combinatorial agents in eradicating Staphylococcus species

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Jonghoon Shin ◽  
Krishna Bahadur Somai Magar ◽  
Jungwoon Lee ◽  
Kwang-sun Kim ◽  
Yong Rok Lee
Keyword(s):  
Staphylococcus Aureus ◽  
Antibacterial Activity ◽  
Multidrug Resistant ◽  
Cellular Level ◽  
One Pot ◽  
Design Synthesis ◽  
Reference Drug ◽  
As Species ◽  
Species Specific

Abstract A series of new functionalized 3-indolylindolin-2-ones, 3-(1-methylpyrrol-2-yl)indolin-2-ones, and 3-(thiophen-2-yl)indolin-2-ones were synthesized by using novel indium (III)-catalysed reaction of various 3-diazoindolin-2-ones with indoles, 1-methylpyrrole, or thiophene via one-pot procedure. The newly synthesized compounds were characterized and screened for their in vitro antibacterial activity against various Staphylococcus species, including methicillin-resistant Staphylococcus aureus. results revealed that five compounds KS15, KS16, KS17, KS19, and KS20 exhibited potent and specific antibacterial activity against Staphylococcus species albeit inactive against Gram-negative bacteria. Especially, compounds exhibited superior antibacterial potency against Staphylococcus epidermidis compared to the reference drug streptomycin. The most potential compound KS16 also increased the susceptibility of Staphylococcus aureus to ciprofloxacin, gentamicin, kanamycin, and streptomycin. Among them, KS16 was found to be a synergistic compound with gentamicin and kanamycin. Furthermore, the cellular level of autolysin protein was increased from the KS16-treated Staphylococcus aureus cells. Finally, in vitro CCK-8 assays showed that KS16 exhibited no cytotoxicity at the minimum inhibitory concentrations used for killing Staphylococcus species. From all our results, novel oxindole compounds directly have lethal action or boost existing antibiotic power with the reduction of doses and toxicity in the treatment of multidrug-resistant Staphylococcus species.

scholarly journals Bifidobacterium β-Glucosidase Activity and Fermentation of Dietary Plant Glucosides Is Species and Strain Specific

2020 ◽  
Vol 8 (6) ◽  
pp. 839
Author(s):  
Nikol Modrackova ◽  
Eva Vlkova ◽  
Vaclav Tejnecky ◽  
Clarissa Schwab ◽  
Vera Neuzil-Bunesova
Keyword(s):  
Antibacterial Activity ◽  
Intestinal Microbiota ◽  
Energy Sources ◽  
Glycosyl Hydrolases ◽  
Glucosidase Activity ◽  
Human Adults ◽  
Animal Hosts ◽  
Beta Glucosidase ◽  
Species Specific ◽  
Fermentation Substrate

Dietary plant glucosides are phytochemicals whose bioactivity and bioavailability can be modified by glucoside hydrolase activity of intestinal microbiota through the release of acylglycones. Bifidobacteria are gut commensals whose genomic potential indicates host-adaption as they possess a diverse set of glycosyl hydrolases giving access to a variety of dietary glycans. We hypothesized bifidobacteria with β-glucosidase activity could use plant glucosides as fermentation substrate and tested 115 strains assigned to eight different species and from different hosts for their potential to express β-glucosidases and ability to grow in the presence of esculin, amygdalin, and arbutin. Concurrently, the antibacterial activity of arbutin and its acylglycone hydroquinone was investigated. Beta-glucosidase activity of bifidobacteria was species specific and most prevalent in species occurring in human adults and animal hosts. Utilization and fermentation profiles of plant glucosides differed between strains and might provide a competitive benefit enabling the intestinal use of dietary plant glucosides as energy sources. Bifidobacterial β-glucosidase activity can increase the bioactivity of plant glucosides through the release of acylglycone.

scholarly journals DNA Mini-Barcodes as A Molecular Marker for Various Hairtail Fish Products Traceability

2019 ◽  
Vol 22 (1) ◽  
pp. 33
Author(s):  
Asadatun Abdullah ◽  
Mala Nurilmala ◽  
Kinanti Permata Sitaresmi
Keyword(s):  
Phylogenetic Analysis ◽  
Molecular Marker ◽  
Economic Value ◽  
Specific Primers ◽  
Fish Products ◽  
Traceability System ◽  
Blast Analysis ◽  
Trichiurus Lepturus ◽  
Processed Sample ◽  
Species Specific

Hairtail fishery is an important fishery commodity with high economic value as export commodity. Authentication based on DNA mini-barcodes can be applied to overcome seafood fraud and to support Indonesian traceability system. This study was aimed to design species-specific primers of DNA minibarcodes and authentication of various processed hairtail fish products such as smoked, baked, fried, canned, and boiled. Analytical method applied PCR-based of cytochrome c oxidase 1 (COI) full length and<br />mini-barcodes. Mini-barcode primer specific for hairtail (Trichiurus lepturus) successfully amplified DNA of processed hairtail fish. The BLAST analysis showed the samples were identified as Trichiurus sp. and T. lepturus with homology level of 91% to 100%. Phylogenetic analysis showed the processed sample (LC dan LD) were in the same group with T. lepturus.

Mechanisms of crude protein from medicinal mushroom Ophiocordyceps sobolifera against human breast MCF-7 cancer cells

Biologia ◽  
2020 ◽  
Vol 75 (10) ◽  
pp. 1759-1768 ◽  
Author(s):  
Benjaporn Buranrat ◽  
Kusavadee Sangdee ◽  
Sutthiwan Thammawat ◽  
Aphidech Sangdee
Keyword(s):  
Cancer Cells ◽  
Crude Protein ◽  
Medicinal Mushroom ◽  
Human Breast ◽  
Ophiocordyceps Sobolifera ◽  
Mcf 7
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