Effect of Properties of Silver Nanoparticles Coated with Polar Material and the Antibacterial Activity on Marine Pathogenic Bacteria

Silver nanoparticles (Ag NPs) have become one of the current research hotspots and are used in many fields such as electrochemistry, energy, bioanalysis, and environmental monitoring, especially in the field of antibacterial research. In this study, we investigated the effect of properties of Ag NPs coated with polar materials. Ag NPs covered by a dispersant that was triethylene glycol monoethyl ether was stable and conquered the aggregation of Ag NPs. The effect of the dispersant on biocompatibility was explored through interaction experiments between Ag NPs and DNA sequence. The coated Ag NPs could adsorb DNA, and the fluorescence of FAM-DNA could be quenched by Ag NPs. The adsorption and desorption experiments of DNA showed that the order of DNA functional groups on the interaction process was phosphate>T>C>A>G. Moreover, we selected marine pathogenic bacteria to test the antibacterial effect of Ag NPs coated with a polar dispersant. The polar material had a certain inhibitory effect on the antibacterial activity of Ag NPs. However, small molecules such as bases could interact on the surface Ag NPs and release Ag+ to perform the antibacterial activity. The results could contribute to the further application of Ag NPs

Purification and Characterization of a Biofilm-Degradable Dextranase from a Marine Bacterium

This study evaluated the ability of a dextranase from a marine bacterium Catenovulum sp. (Cadex) to impede formation of Streptococcus mutans biofilms, a primary pathogen of dental caries, one of the most common human infectious diseases. Cadex was purified 29.6-fold and had a specific activity of 2309 U/mg protein and molecular weight of 75 kDa. Cadex showed maximum activity at pH 8.0 and 40 °C and was stable at temperatures under 30 °C and at pH ranging from 5.0 to 11.0. A metal ion and chemical dependency study showed that Mn2+ and Sr2+ exerted positive effects on Cadex, whereas Cu2+, Fe3+, Zn2+, Cd2+, Ni2+, and Co2+ functioned as inhibitors. Several teeth rinsing product reagents, including carboxybenzene, ethanol, sodium fluoride, and xylitol were found to have no effects on Cadex activity. A substrate specificity study showed that Cadex specifically cleaved the α-1,6 glycosidic bond. Thin layer chromatogram and high-performance liquid chromatography indicated that the main hydrolysis products were isomaltoogligosaccharides. Crystal violet staining and scanning electron microscopy showed that Cadex impeded the formation of S. mutans biofilm to some extent. In conclusion, Cadex from a marine bacterium was shown to be an alkaline and cold-adapted endo-type dextranase suitable for development of a novel marine agent for the treatment of dental caries

Research Progress on Rolling Circle Amplification (RCA)-Based Biomedical Sensing

Enhancing the limit of detection (LOD) is significant for crucial diseases. Cancer development could take more than 10 years, from one mutant cell to a visible tumor. Early diagnosis facilitates more effective treatment and leads to higher survival rate for cancer patients. Rolling circle amplification (RCA) is a simple and efficient isothermal enzymatic process that utilizes nuclease to generate long single stranded DNA (ssDNA) or RNA. The functional nucleic acid unit (aptamer, DNAzyme) could be replicated hundreds of times in a short period, and a lower LOD could be achieved if those units are combined with an enzymatic reaction, Surface Plasmon Resonance, electrochemical, or fluorescence detection, and other different kinds of biosensor. Multifarious RCA-based platforms have been developed to detect a variety of targets including DNA, RNA, SNP, proteins, pathogens, cytokines, micromolecules, and diseased cells. In this review, improvements in using the RCA technique for medical biosensors and biomedical applications were summarized and future trends in related research fields described

The Adsorption of Dextranase onto Mg/Fe-Layered Double Hydroxide: Insight into the Immobilization

We report the adsorption of dextranase on a Mg/Fe-layered double hydroxide (Mg/Fe-LDH). We focused the effects of different buffers, pH, and amino acids. The Mg/Fe-LDH was synthesized, and adsorption experiments were performed to investigate the effects. The maximum adsorption occurred in pH 7.0 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES) buffer, and the maximum dextranase adsorption uptake was 1.38 mg/g (416.67 U/mg); histidine and phenylalanine could affect the adsorption. A histidine tag could be added to the protein to increase the adsorption significantly. The performance features and mechanism were investigated with X-ray diffraction patterns (XRD) and Fourier transform infrared spectra (FTIR). The protein could affect the crystal structure of LDH, and the enzyme was adsorbed on the LDH surface. The main interactions between the protein and LDH were electrostatic and hydrophobic. Histidine and phenylalanine could significantly affect the adsorption. The hexagonal morphology of LDH was not affected after adsorption

Virgibacillus halodenitrificans ST-1 for fermentation of shrimp paste and hydrolysates of its protease

The nutrition and flavor of shrimp paste came from hydrolyzation by enzymes that were produced by microorganisms. The salt-tolerant strain Virgibacillus halodenitrificans ST-1 isolated from shrimp paste was studied and used in the fermentation of shrimp paste. The strain and the protease produced by ST-1 were investigated. The optimum pH of the protease was 8.0, and the reaction temperature was 30°C. The protease showed high activity in the range of pH (5.0–11.0) and NaCl concentration (1%–15%). Divalent cations such as Ba2+, Ca2+, Mg2+, Mn2+, and Si2+ could enhance the protease activity. Residual activity of protease was more than 90% when it was incubated with PMSF and H2O2. Also, the enzyme retained more than 90% of initial activity after it was incubated with organic solvents. Variety of natural proteins could be substrates of the protease. By analyzing the release rate of free amino acids, it was predicted that the cleavage sites of the protease were mainly Glu, Asp, Gly, Leu, and Lys. Moreover, the hydrolysates of the protease had antioxidant activity, especially for DPPH and superoxide anion radical scavenging. The strain ST-1 and the protease both were excellent candidates for food industries

A Multi-Scale Approach to Investigate Adhesion Properties of Pseudomonas aeruginosa PAO1 to Geotrichum candidum LG-8, a Potential Probiotic Yeast

This study investigated properties of Pseudomonas aeruginosa PAO1 adhesion to Geotrichum candidum LG-8 cells in variable pH and salt conditions. The primary mechanism was revealed by multi-scale microscopy technics. The adhesion of PAO1 to the living fungus occurred within 1 h and was limited at concentrations of bile salts higher than 0.5%. The adhesion efficiency gradually increased to 58.1% with the pH increasing from 2.0 to 7.0 and then decreased to 48.2% at pH 9.0. However, the dead LG-8 has an advantage over the living ones to adhere PAO1 in same pH and bile salt conditions. Optical microscopy showed that both unsterilized and sterilized G. candidum LG-8 cells removed approximately one hundred fold bacteria in 4 h. Laser scanning confocal microscopy (LSCM) analysis indicated that polysaccharides of the fungus contributed to adhesion. Scanning electron microscopy (SEM) analysis proved that syrup-like EPS (extracellular polymeric substances) of LG-8 coating PAO1 was in part a mechanism. Atomic force microscopy (AFM) showed roughness of the LG-8 surface changed in the adhesion process. Furthermore, a pedestal-like structure of bacteria was observed by transmission electron microscopy (TEM) analysis, indicating that the bacteria were also actively involved in the adhesion process. G. candidum LG-8 is a potential candidate for the control of P. aeruginosa PAO1 in the food industry and immunodeficiency patients

Anti-Helicobacter pylori Activity of a Lactobacillus sp. PW-7 Exopolysaccharide

Helicobacter pylori is a cause of gastric cancer. We extracted the exopolysaccharide (EPS) of Lactobacillus plajomi PW-7 for antibacterial activity versus H. pylori, elucidating its biological activity and structural characteristics. The minimum inhibitory concentration (MIC) of EPS against H. pylori was 50 mg/mL. Disruption of the cell membranes of pathogenic bacteria by EPS was indicated via the antibacterial mechanism test and confirmed through electron microscopy. EPS also has antioxidant capacity. The IC50 of EPS for 2,2-Diphenyl-1-picrylhydrazyl (DPPH) radical, superoxide anions, and hydroxyl radicals were 300 μg/mL, 180 μg/mL, and 10 mg/mL, respectively. The reducing power of EPS was 2 mg/mL, equivalent to 20 μg/mL of ascorbic acid. EPS is a heteropolysaccharide comprising six monosaccharides, with an approximate molecular weight of 2.33 × 104 Da. Xylose had a significant effect on H. pylori. EPS from L. plajomi PW-7 showed potential as an antibacterial compound and antioxidant, laying a foundation for the development of EPS-based foods

Isolation of a Novel Anti-Diabetic α-Glucosidase Oligo-Peptide Inhibitor from Fermented Rice Bran

At present, the incidence rate of diabetes is increasing gradually, and inhibiting α-glucosidase is one of the effective methods used to control blood sugar. This study identified new peptides from rice bran fermentation broth and evaluated their inhibitory activity and mechanism against α-glucosidase. Rice bran was fermented with Bacillus subtilis MK15 and the polypeptides of <3 kDa were isolated by ultrafiltration and chromatographic column, and were then subjected to LC-MS/MS mass spectrometry analysis. The results revealed that the oligopeptide GLLGY showed the greatest inhibitory activity in vitro. Docking studies with GLLGY on human α-glucosidase (PDB ID 5NN8) suggested a binding energy of −7.1 kcal/mol. GLLGY acts as a non-competitive inhibitor and forms five hydrogen bonds with Asp282, Ser523, Asp616, and His674 of α-glucosidase. Moreover, it retained its inhibitory activity even in a simulated digestion environment in vitro. The oligopeptide GLLGY could be developed into a potential anti-diabetic agent

Cloning of Cold-Adapted Dextranase and Preparation of High Degree Polymerization Isomaltooligosaccharide

Intestinal diseases are mainly caused by a decrease in the relative abundance of probiotics and an increase in the number of pathogenic bacteria due to dysbiosis of the intestinal flora. High degree polymerization isomaltooligosaccharide (IMO) can promote probiotic metabolism and proliferation. In this study, the dextranase (PsDex1711) gene of marine bacterial Pseudarthrobacter sp. RN22 was cloned and expressed in Escherichia coli BL21 (DE3). The optimal pH and temperature of the dextranase were 6.0 and 30 °C, respectively, showing the highest stability at 20 °C. The dextran T70 could be hydrolyzed to produce IMO3, IMO4, IMO5, and IMO6 with a high degree of polymerization. The hydrolysate of 1 mg/mL could significantly promote the growth of Lactobacillus and Bifidobacterium after 12 h culture and the formation of biofilms by 58.2%. The hydrolysates could promote the proliferation of probiotics. Furthermore, the IC50 of scavenging rate of DPPH, hydroxyl radical, and superoxide anion was less than 20 mg/mL. This study provides a crucial theoretical basis for the application of dextranase such as pharmaceutical and food industries

The Screening and Identification of a Dextranase-Secreting Marine Actinmycete <i>Saccharomonospora</i> sp. K1 and Study of Its Enzymatic Characteristics

In this study, an actinomycete was isolated from sea mud. The strain K1 was identified as Saccharomonospora sp. by 16S rDNA. The optimal enzyme production temperature, initial pH, time, and concentration of the inducer of this actinomycete strain K1 were 37 °C, pH 8.5, 72 h, and 2% dextran T20 of medium, respectively. Dextranase from strain K1 exhibited maximum activity at 8.5 pH and 50 °C. The molecular weight of the enzyme was 2+ and K+ enhanced its activity, whereas Fe3+ and Co2+ had an opposite effect. In addition, high-performance liquid chromatography showed that dextran was mainly hydrolyzed to isomaltoheptose and isomaltopentaose. Also, it could effectively remove biofilms of Streptococcus mutans. Furthermore, it could be used to prepare porous sweet potato starch. This is the first time a dextranase-producing actinomycete strain was screened from marine samples