• Journal of Microbiology and Biotechnology
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• v.20 no.7
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• pp.1061-1068
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• 2010

The biological synthesis of nanoparticles has gained considerable attention in view of their excellent biocompatibility and low toxicity. We isolated and purified rhamnolipids from Pseudomonas aeruginosa strain BS-161R, and these purified rhamnolipids were used to synthesize silver nanoparticles. The purified rhamnolipids were further characterized and the structure was elucidated based on one- and two-dimensional $^1H$ and $^{13}C$ NMR, FT-IR, and HR-MS spectral data. Purified rhamnolipids in a pseudoternary system of n-heptane and water system along with n-butanol as a cosurfactant were added to the aqueous solutions of silver nitrate and sodium borohydride to form reverse micelles. When these micelles were mixed, they resulted in the rapid formation of silver nanoparticles. The synthesized nanoparticles were characterized by UV-Visible spectroscopy, transmission electron microscopy, and energy dispersive X-ray spectroscopy (EDS). The nanoparticles formed had a sharp adsorption peak at 410 nm, which is characteristic of surface plasmon resonance of the silver nanoparticles. The nanoparticles were monodispersed, with an average particle size of 15.1 nm (${\sigma}={\pm}5.82$ nm), and spherical in shape. The EDS analysis revealed the presence of elemental silver signal in the synthesized nanoparticles. The formed silver nanoparticles exhibited good antibiotic activity against both Grampositive and Gram-negative pathogens and Candida albicans, suggesting their broad-spectrum antimicrobial activity.

• Journal of Marine Bioscience and Biotechnology
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• v.14 no.2
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• pp.133-142
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• 2022

The increased production and consumption of polyethylene terephthalate (PET)-based products over the past several decades has resulted in the discharge of countless tons of PET waste into the marine environment. PET microparticles resulting from the physical erosion of general PET wastes end up in the ocean and pose a threat to the marine biosphere and human health, necessitating the development of new technologies for recycling and upcycling. Notably, enzyme-mediated PET degradation is an appealing option due to its eco-friendly and energy-saving characteristics. PETase, a PET-hydrolyzing enzyme originating from Ideonella sakaiensis, is one of the most thoroughly researched biological catalysts. However, the industrial application of PETase-mediated PET recycling is limited due to the low stability and poor reusability of the enzyme. Here we developed the whole-cell catalyst (WCC) in which functional PETase is attached to the outer membrane of Escherichia coli. Immunoassays are used to identify the surface-expressed PETase, and we demonstrated that the WCC degraded PET microparticles most efficiently at 30℃ and pH 9 without agitation. Furthermore, the WCC increased the PET-degrading activity in a concentration-dependent manner, surpassing the limited activity of soluble PETase above 100 nM. Finally, we demonstrated that the WCC could be recycled up to three times.

• Journal of Life Science
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• v.25 no.11
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• pp.1290-1297
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• 2015

Studies of the inactivation of a gene encoding pyruvate decarboxylase, pdc, in an ethanol-producing bacterium, Zymomonas mobilis, identified a mutant strain with 50% reduced PDC activity. To evaluate the possibility of a carbon-flux shift from an ethanol pathway toward higher value fermentation products, including pyruvate, succinate, and lactate, fermentation studies were carried out. Despite attempts to silence pdc expression in the wild-type strain ZM4 using cat-inserted pdc and pdc-deleted homologs by electroporation, the strain isolated showed partial gene activation. Fermentation experiments with the PDC mutant strain showed that the reduced expression level of PDC activity resulted in decreased rates of substrate uptake and ethanol production, together with increased pyruvate accumulation of 2.5 g l^-1 , although lactate and succinate concentrations were not significantly enhanced in these modified strains. Despite numerous attempts, no strains were isolated in which complete pdc inactivation occurred. This result indicates that the ethanol fermentation pathway of this bacterium is totally dependent on the activity of the PDC enzyme. To ensure a redox balance of intracellular NAD and NADH levels, other enzymes, such as lactate dehydrogenase for lactate, and enzymes involved in the production of succinic acid, such as pyruvate dehydrogenase (PDH) and malic enzymes, may be needed for their increased end-product production.

• Asian-Australasian Journal of Animal Sciences
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• v.19 no.6
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• pp.779-783
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• 2006

The adiponectin gene is known to be involved in the regulation of energy homeostasis involving food intake, carbohydrate and lipid metabolism. Human adiponectin gene polymorphisms have been recently reported to be associated with obesity, insulin sensitivity and the risk of type 2 diabetes. The present study was carried out to investigate the porcine adiponectin gene as a candidate gene for fat deposition and carcass traits. A mutation of A178G of the porcine adiponectin gene that resulted in substitution of the amino acid Isoleucine to Valine was identified. AcyI PCR-RFLP was used to detect the polymorphism of the genotypes in five different pig populations (Large White, Landrace, Duroc, Chinese breeds Meishan and Qingping). The A allele frequency was significantly higher among subjects from Chinsese lard type breeds, while the G allele was the only one present in those from Western lean type breeds. To determine if there was an association of the polymorphism with phenotypic variation, the mutation was tested in 267 pigs of the "Large $White{\times}Meishan$" F2 resource population. The results of association analyses showed significant associations of the genotypes with fat deposition and carcass traits. Allele G was significantly associated with increase in loin eye height, loin eye area and lean meat percentage and bone percentage, and decrease in fat mean percentage, ratio of lean to fat, shoulder fat thickness, 6-7 rib fat thickness, thorax-waist fat thickness and buttock fat thickness. The substitution of A178G (Ile60Val) happened to be located at amino acid 60 in the collagenous domain of porcine adiponectin which might affect the association into higher-order structures, and accordingly affect the posttranslational modifications and optimal biological activity of the multimeric forms. The identified functional polymorphism provides new evidence of adiponectin as an important candidate gene affecting fat deposition and carcass traits in pigs.