Enzyme-mediated coupling of a bi-functional phenolic compound onto wool to enhance its physical,mechanical and functional properties

Wool fibres have been modified with nordihydroguaiaretic acid (NDGA) to improve their performance at use. This water insoluble bi-functional phenolic compound has been grafted on wool through a laccase enzyme catalyzed reaction in an aqueous–ethanol mixture. The capacity of laccase to oxidise NDGA in this aqueous–organic medium has been studied electrochemically. The increase of CH₂, CH₃ and aromatic groups signal in the DRIFT spectra, together with SEM images of the enzymatically modified fabrics confirmed the covalent grafting of NDGA on wool. This one step enzymatic process for grafting of NDGA improved the physical and mechanical properties of wool fabrics such as shrink resistance, crease recovery and tensile strength. Furthermore, the NDGA imparted to the textile material strong antioxidant activity and UV protection.     

Bacterial community analysis of Indonesian hot springs

We report the first attempts to describe thermophilic bacterial communities in Indonesia's thermal springs using molecular phylogenetic analyses. 16S rRNA genes from laboratory cultures and DNA directly amplified from three hot springs in West Java were sequenced. The 22 sequences obtained were assignable to the taxa Proteobacteria, Bacillus and Flavobacterium, including a number of clades not normally associated with thermophily.     

Babesia bovis merozoites invade human, ovine, equine, porcine and caprine erythrocytes by a sialic acid-dependent mechanism followed by developmental arrest after a single round of cell fission

Babesia bovis infections have only been observed in bovine species in contrast to Babesia divergens that also can infect humans, sheep and rodents. Using an in vitro assay that assesses invasion of erythrocytes by free merozoites after a 1-h incubation period, it was shown that specificity is not determined by host-specific interactions associated with invasion. Human erythrocytes were invaded more efficiently than bovine erythrocytes whereas erythrocytes of sheep, pigs and horses were invaded only slightly less efficiently. In contrast, goat erythrocytes were refractory to efficient invasion. Significant differences in invasion efficiency into erythrocytes from different individuals of the same species were observed. Erythrocytes from all species, except for goats, supported intracellular development of newly invaded merozoites and high numbers of duplicated parasites, located in a morphologically normal accole position, were present. Only in bovine erythrocytes did subsequent rounds of invasion, leading to increased parasitaemia, take place. This suggests that host specificity is determined by factors operating late in the erythrocytic stage of the B. bovis life cycle. Incubation of erythrocytes with neuraminidase prior to invasion led to a decrease in invasion efficiency of 80%. This effect was observed for several species. The removal of either (2-3)-linked or (2-6)-linked sialic acid residues gave similar levels of reduction whereas simultaneous removal did not show an additive effect. Pre-incubation of merozoites with N-acetylneuraminyl-lactose decreased invasion efficiency by 45% whereas addition just prior to invasion had no significant effect. The results demonstrate that invasion is dependent on the presence of sialic-acid containing membrane receptors on erythrocytes that interact with merozoite ligands that are probably already accessible during pre-incubation prior to invasion.     

Biostimulation potential of biochar for remediating the crude oil contaminated soil and plant growth

Crude oil contamination is a serious environmental threat to soil and plants growing in it. Biochar has the potential of biostimulation for remediation of crude oil-contaminated soil. Therefore, the current research was designed to analyze the bio-stimulatory impact of biochar for remediating the crude oil contaminated soil (10%, and 15%), and growth of maize under glasshouse conditions. Biochar was produced by pyrolysis of Australian pines at 350 °C. Soil incubations were done for 20 days. The results of soil analysis showed that the crude oil degradation efficiency of biochar was 34%. The soil enzymatic activities had shown 38.5% increase in fluorescein diacetate (FDA) hydrolysis and 55.6% increase in dehydrogenase activity in soil incubated with biochar in comparison to control. The soil microbial diversity was improved to 41% in biochar treated soil with respect to untreated one, while microbial respiration rate had shown a 33.67% increase in soil incubated with biochar with respect to control under oil stress. Gas Chromatography Mass spectrometry (GC-MS) analysis had shown the high content of low molecular weight hydrocarbons (C₉-C₁₃) in the soil incubated with biochar in comparison to untreated soil. Biochar showed a significant increase in fresh and dry biomass (25%, 14.61%), leaf area (10%), total chlorophyll (11%), water potential (21.6%), osmotic potential (21%), and membrane stability index (12.7%). Moreover, biochar treatment showed a higher increase in the contents of proline (29%), total amino acids (18%), soluble sugars (30.4%), and antioxidant enzymes like superoxide dismutase (16.5%), catalase (11%), and peroxidase (12%). Overall, the results of the present study suggest the bio-stimulating potential of biochar for degradation of hydrocarbons in crude oil contaminated soil and their growth-stimulating effects on maize.     

Synthesis and histamine H3 receptor activity of 4-(n-alkyl)-1H-imidazoles and 4-(omega-phenylalkyl)-1H-imidazoles

The influence of lipophilic moieties attached to a 4-1H-imidazole ring on the histamine H₃ receptor activity was systematically investigated. Series of 4-(n-alkyl)-1H-imidazoles and 4-(ω-phenylalkyl)-1H-imidazoles were prepared, with an alkyl chain varying from 2–9 methylene groups and from 1–9 methylene groups, respectively. The compounds were tested for their activity on the H₃ receptor under in vitro conditions. For the 4-(n-alkyl)-1H-imidazoles the activity is proportional to chain length, ranging from a pA₂ value of 6.3±0.2 for 4-(n-propyl)-1H-imidazole to a pA₂ value of 7.2±0.1 for 4-(n-decyl)-1H-imidazole. For the series 4-(ω-phenylalkyl)-4H-imidazoles an optimum in H₃ activity was found for the pentylene spacer: 4-(ω-phenylpentyl)-1H-imidazole has a pA₂ value of 7.8±0.1.     

Strategies for the design and use of tumor-reactive human monoclonal antibodies

Human hybridomas secreting monoclonal antibodies (MoAb) reactive with tumor cell antigens were produced in our laboratory by the immortalization of UC 729-6 with B lymphocytes isolated from regional draining lymph nodes of cancer patients. MoAbs were purified from the hybridoma supernates by standard biochemical procedures for in vivo studies and by affinity methods for in vitro experiments. Using a novel method in the preparation of slides containing adherent tumor cells, immunoreactivities of the MoAbs were evaluated by an indirect immunofluorescence assay. Based on this data, human MoAbs can, therefore, be used as research reagents.     

Biocatalysis of immobilized chlorophyllase in a ternary micellar system.

The immobilization of chlorophyllase was optimized by physical adsorption on various inorganic supports, including alumina, celite, Dowex-1-chloride, glass beads and silica gel. The enzyme was also immobilized in different media, including water, Tris-HCl buffer solution and a ternary micellar system containing Tris-HCl buffer solution, hexane and surfactant. The highest immobilization efficiency (84.56%) and specific activity (0.34 mumol hydrolyzed chlorophyll mg protein-1 per min) were obtained when chlorophyllase was suspended in Tris-HCl buffer solution and adsorbed onto silica gel. The effect of different ratios of chlorophyllase to the support and the optimum incubation time for the immobilization of chlorophyllase were determined to be 1-4 and 60 min, respectively. The experimental results showed that the optimum pH and temperature for the immobilized chlorophyllase were 8.0 and 35 degrees C, respectively. The use of optimized amounts of selected membrane lipids increased the specific activity of the immobilized chlorophyllase by approximately 50%. The enzyme kinetic studies indicated that the immobilized chlorophyllase showed a higher affinity towards chlorophyll than pheophytin as substrate.